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1. Cytotoxic peptides with insulin-releasing activities from skin secretions of the Italian stream frog Rana italica (Ranidae)

Author

Conlon, J Michael, Musale, Vishal, Attoub, Samir, Mangoni, Maria Luisa, Leprince, Jérôme, Coquet, Laurent, Jouenne, Thierry, Abdel-Wahab, Yasser, Flatt, Peter, Rinaldi, Andrea, Conlon, J. Michael, Faculty of Medicine and Health Science, UAE University, Department of Biochemical Sciences 'Rossi Fanelli', Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)

Subjects
frog skin, antimicrobial peptide, cytotoxicity, ranidae, insulin relase, Ranidae, MESH: Staphylococcus epidermidis, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, MESH: HT29 Cells, MESH: Anura, Microbial Sensitivity Tests, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Hemolysis, Amphibian Proteins, Mice, MESH: Skin, MESH: Amphibian Proteins, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], Escherichia coli, Staphylococcus epidermidis, Animals, Humans, insulin release, MESH: Animals, MESH: Mice, Skin, MESH: Microbial Sensitivity Tests, MESH: Humans, MESH: Ranidae, MESH: Escherichia coli, MESH: Antimicrobial Cationic Peptides, MESH: Hemolysis, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Anura, HT29 Cells, Antimicrobial Cationic Peptides
Abstract

International audience; Peptidomic analysis of norepinephrine-stimulated skin secretions from Italian stream frog Rana italica led to the purification and characterization of two host-defense peptides differing by a single amino acid residue belonging to the brevinin-1 family (brevinin-1ITa and -1ITb), a peptide belonging to the temporin family (temporin-ITa) and a component identified as prokineticin Bv8. The secretions contained relatively high concentrations of the methionine-sulphoxide forms of brevinin-1ITa and -1ITb suggesting that these peptides may have a role as antioxidants in the skin of this montane frog. Brevinin-1ITa (IVPFLLGMVPKLVCLITKKC) displayed potent cytotoxicity against non-small cell lung adenocarcinoma A549 cells (LC50 = 18 μM), breast adenocarcinoma MDA-MB-231 cells (LC50 = 8 μM) and colorectal adenocarcinoma HT-29 cells (LC50 = 18 μM), but the peptide was also strongly hemolytic against mouse erythrocytes (LC50 = 7 μM). Temporin-ITa (VFLGAIAQALTSLLGKL.NH2 ) was between three and fivefold less potent against these cells. Brevinin-1ITa inhibited growth of both Gram-positive Staphylococcus epidermidis and Gram-negative Escherichia coli as well as a strain of the opportunist yeast pathogen Candida parapsilosis, whereas temporin-ITa was active only against S. epidermidis and C. parapsilosis. Both peptides stimulated the release of insulin from BRIN-BD11 clonal β-cells at concentrations ≥1 nM, but brevinin-1ITa was cytotoxic to the cells at concentrations ≥3 μM. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.

Published
2017

2. Characterization of antimicrobial peptides in skin secretions from discrete populations of Lithobates chiricahuensis (Ranidae) from central and southern Arizona

Author

Conlon, J Michael, Mechkarska, Milena, Coquet, Laurent, Jouenne, Thierry, Leprince, Jérôme, Vaudry, Hubert, Kolodziejek, Jolanta, Nowotny, Norbert, King, Jay, Conlon, J. Michael, Faculty of Medicine and Health Science, UAE University, Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), and Zoonoses and Emerging Infections Group

Subjects
Erythrocytes, Ranidae, MESH: Sequence Homology, Amino Acid, Physiology, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Biochemistry, 0302 clinical medicine, Endocrinology, Anti-Infective Agents, Salientia, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], MESH: Animals, Skin, Antibacterial agent, MESH: Microbial Sensitivity Tests, 0303 health sciences, MESH: Ranidae, biology, MESH: Peptides, Ecology, MESH: Erythrocytes, Arizona, MESH: Hemolysis, Taxonomy (biology), Mitochondrial DNA, Molecular Sequence Data, MESH: Anti-Infective Agents, Antimicrobial peptides, Zoology, Microbial Sensitivity Tests, Hemolysis, Lithobates chiricahuensis, 03 medical and health sciences, Cellular and Molecular Neuroscience, MESH: Skin, Animals, Humans, Amino Acid Sequence, 030304 developmental biology, MESH: Humans, MESH: Molecular Sequence Data, Sequence Homology, Amino Acid, Leopard frog, biology.organism_classification, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Peptides, Frog Skin, 030217 neurology & neurosurgery, MESH: Arizona
Abstract

International audience; Populations of the Chiricahua leopard frog Lithobates chiricahuensis (Ranidae) occupying regions in southern Arizona (southern range) are morphologically distinct from those from the Mogollon Rim of central Arizona (northern range) and a comparison of DNA sequences of mitochondrial genes has suggested that they may represent separate species. Peptidomic analysis of norepinephrine-stimulated skin secretions has led to the identification of six peptides with antimicrobial activity in samples from specimens from both groups. The primary structure of the peptides (esculentin-2 CHa, ranatuerin-2 CHa, -CHb, and -CHc, and brevinin-1 CHa and -CHb) isolated from both southern and northern range frogs are identical consistent with the proposal that the two populations are conspecific. However, palustrin-2CHa and the atypical brevinin-1 CHc (FFPTIAG*****LTKLFCA ITKKC), containing a five amino acid residue deletion, were identified only in secretions from southern range specimens. Consequently, there is some support for the proposal that the two populations are closely related but separate species but this support is relatively weak. Esculentin-2 CHa (GFSSIFRGVAKFASKGLG KDLAKLGVDLVACKISKQC) displayed the highest antimicrobial potency (MIC ≤ 10μM) against a variety of microorganisms and was only moderately hemolytic (LC(50) = 150 μM). Cladistic analysis based upon the primary structures of brevinin-1 peptides indicates a close phylogenetic relationship between L. chiricahuensis, L. onca, and L. yavapaiensis.

Published
2011

3. Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families isolated from the skin of the Japanese brown frog, Rana dybowskii

Author

Conlon, J Michael, Kolodziejek, Jolanta, Nowotny, Norbert, Leprince, Jérôme, Vaudry, Hubert, Coquet, Laurent, Jouenne, Thierry, Iwamuro, Shawichi, Conlon, J. Michael, Faculty of Medicine and Health Science, UAE University, Zoonoses and Emerging Infections Group, Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)

Subjects
Erythrocytes, Ranidae, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, MESH: Protein Isoforms, Toxicology, 0302 clinical medicine, MESH: Amphibian Proteins, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], MESH: Staphylococcus aureus, Protein Isoforms, MESH: Proteins, MESH: Animals, MESH: Phylogeny, Peptide sequence, Chromatography, High Pressure Liquid, Phylogeny, MESH: Microbial Viability, Skin, 0303 health sciences, MESH: Tissue Extracts, MESH: Ranidae, Phylogenetic tree, MESH: Escherichia coli, Cytotoxins, MESH: Erythrocytes, MESH: Antimicrobial Cationic Peptides, MESH: Hemolysis, Maximum parsimony, Female, MESH: Cytotoxins, Staphylococcus aureus, Mitochondrial DNA, Molecular Sequence Data, Antimicrobial peptides, Zoology, Biology, Hemolysis, Amphibian Proteins, 03 medical and health sciences, MESH: Skin, Phylogenetics, Escherichia coli, Animals, Humans, Amino Acid Sequence, MESH: Chromatography, High Pressure Liquid, 030304 developmental biology, MESH: Humans, MESH: Molecular Sequence Data, Microbial Viability, Tissue Extracts, Proteins, biology.organism_classification, Rana dybowskii, Temporin, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, MESH: Female, 030217 neurology & neurosurgery, Antimicrobial Cationic Peptides
Abstract

International audience; Peptidomic analysis of an extract of the skins of specimens of Dybowski's brown frog Rana dybowskii Gunther, 1876, collected on Tsushima Island, Japan led to the identification of 10 peptides with differential antibacterial and hemolytic activities. The primary structures of these peptides identified them as belonging to the brevinin-1 (5 peptides) and brevinin-2 (5 peptides) families of antimicrobial peptides. A peptide (FIGPIISALASLFG.NH(2)) with structural similarity to members of the temporin family was also isolated but this component lacked cytolytic activity. Phylogenetic relationships among the Japanese brown frogs (R. dybowskii, R. japonica, R. okinavana, R. ornativentris, R. pirica, R. sakuraii, R. tagoi, and R. tsushimensis) are only incompletely understood. Cladograms based upon maximum parsimony analyses of the brevinin-1 and brevinin-2 amino acid sequences provide strong support for a sister-group relationship between R. dybowskii and R. pirica and somewhat weaker support for a sister-group relationship between R. okinavana and R. tsushimensis. These conclusions are consistent with previous analyses based upon allozyme variations and comparisons of the nucleotide sequences of mitochondrial genes.

Published
2007

4. Antimicrobial peptides from the skin of the Japanese mountain brown frog Rana ornativentris: Evidence for polymorphism among preprotemporin mRNAs

Author

Jérôme Leprince, Hiroaki Kawasaki, Laurent Coquet, Thierry Jouenne, J. Michael Conlon, Shawichi Iwamuro, Hubert Vaudry, Aya Ohnuma, Keiko Yamaguchi, Toho University, United Arab Emirates University (UAEU), Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Institut Fédératif de Recherches Multidisciplinaires sur les Peptides (IFRMP 23), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre de Lutte Contre le Cancer Henri Becquerel Normandie Rouen (CLCC Henri Becquerel)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-CHU Rouen, Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
Male, MESH: Protein Precursors, Ranidae, MESH: Sequence Homology, Amino Acid, Physiology, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, MESH: Base Sequence, Biochemistry, 0302 clinical medicine, Endocrinology, Japan, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], MESH: Animals, MESH: Proteins, Cloning, Molecular, Skin, MESH: Japan, Antibacterial agent, Genetics, MESH: Microbial Sensitivity Tests, 0303 health sciences, MESH: Ranidae, MESH: Antimicrobial Cationic Peptides, Nucleic acid sequence, Rana ornativentris, Female, Signal peptide, DNA, Complementary, Molecular Sequence Data, Antimicrobial peptides, Microbial Sensitivity Tests, Biology, MESH: Sequence Homology, Nucleic Acid, 03 medical and health sciences, Cellular and Molecular Neuroscience, MESH: Skin, Sequence Homology, Nucleic Acid, Complementary DNA, MESH: Polymorphism, Genetic, Animals, MESH: Cloning, Molecular, Amino Acid Sequence, RNA, Messenger, Protein Precursors, MESH: RNA, Messenger, 030304 developmental biology, Polymorphism, Genetic, MESH: Molecular Sequence Data, Base Sequence, Sequence Homology, Amino Acid, Proteins, MESH: DNA, Complementary, biology.organism_classification, Molecular biology, MESH: Male, Temporin, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, MESH: Female, Frog Skin, 030217 neurology & neurosurgery, Antimicrobial Cationic Peptides
Abstract

International audience; A previous study led to the isolation of antimicrobial peptides belonging to the temporin and brevinin-2 families from a pooled extract of the skin of adult specimens of the Japanese mountain brown frog Rana ornativentris Werner 1903. In order to ascertain whether individual frogs expressed the full complement of temporin genes, we individually cloned cDNAs encoding the temporin precursors from total RNA extracted from the skins of 12 frogs by RT-PCR using a set of preprotemporin-specific primers. All the specimens examined contained mRNAs directing the synthesis of the novel, but inactive, temporin-1Oe (ILPLLGNLLNGLL x NH2). Nucleotide sequence analysis revealed marked polymorphism among individual frogs. Twenty-seven distinct preprotemporin-1Oe mRNAs were identified that contained synonymous substitutions in the antimicrobial peptide region and both synonymous and non-synonymous substitutions in the signal peptide and intervening sequence regions. Up to eight preprotemporin-1Oe mRNA variants were found within a single frog. In addition, several cDNAs encoding preprotemporin-1Oa and -1Ob and a single cDNA encoding preprotemporin-1Oc were characterized. Peptidomic analysis of norepinephrine-stimulated skin secretions revealed the presence of temporin-1Oe, temporin-1Of (SLILKGLASIAKLF x NH2), temporin-1Og (FLSSLLSKVVSLFT x NH2), four members of the ranatuerin-2 family and one member of the palustrin-2 family in addition to previously characterized temporin and brevinin-2 peptides.

Published
2007

5. Expression of genes encoding antimicrobial and bradykinin-related peptides in skin of the stream brown frog Rana sakuraii

Author

J. Michael Conlon, Christopher K. Taylor, Laurent Coquet, Hubert Vaudry, Thierry Jouenne, Aya Ohnuma, Peter W. Abel, Jérôme Leprince, Shawichi Iwamuro, Hiroe Suzuki, Tohoku University [Sendai], Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Institut Fédératif de Recherches Multidisciplinaires sur les Peptides (IFRMP 23), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre de Lutte Contre le Cancer Henri Becquerel Normandie Rouen (CLCC Henri Becquerel)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-CHU Rouen, Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Creighton University Medical School [Omaha, NE, USA], and United Arab Emirates University (UAEU)

Subjects
Male, Ranidae, MESH: Sequence Homology, Amino Acid, Physiology, Muscle Relaxation, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Rana tagoi, Gene Expression, Peptide, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Biochemistry, Mice, chemistry.chemical_compound, 0302 clinical medicine, Endocrinology, MESH: Amphibian Proteins, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], MESH: Animals, MESH: Proteins, Cloning, Molecular, Skin, Antibacterial agent, chemistry.chemical_classification, 0303 health sciences, MESH: Ranidae, biology, MESH: Peptides, MESH: Antimicrobial Cationic Peptides, MESH: Melitten, MESH: 5' Untranslated Regions, Female, Signal peptide, DNA, Complementary, MESH: Gene Expression, Molecular Sequence Data, In Vitro Techniques, Bradykinin, Amphibian Proteins, Melittin, 03 medical and health sciences, Cellular and Molecular Neuroscience, MESH: Skin, Complementary DNA, Animals, MESH: Cloning, Molecular, Amino Acid Sequence, MESH: Mice, 030304 developmental biology, MESH: In Vitro Techniques, MESH: Bradykinin, MESH: Molecular Sequence Data, Sequence Homology, Amino Acid, Proteins, MESH: DNA, Complementary, biology.organism_classification, Melitten, Molecular biology, MESH: Male, Temporin, chemistry, MESH: Muscle Relaxation, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, 5' Untranslated Regions, Peptides, MESH: Female, Frog Skin, 030217 neurology & neurosurgery, Antimicrobial Cationic Peptides
Abstract

Peptidomic analysis of an extract of the skin of the stream brown frog Rana sakuraii Matsui and Matsui, 1990 led to the isolation of a C-terminally α-amidated peptide (VR-23; VIGSILGALASGLPTLISWIKNR·NH 2 ) with broad-spectrum antimicrobial activity that shows structural similarity to the bee venom peptide, melittin together with two peptides belonging to the temporin family (temporin-1SKa; FLPVILPVIGKLLNGIL·NH 2 and temporin-1SKb; FLPVILPVIGKLLSGIL·NH 2 ), and peptides whose primary structures identified them as belonging to the brevinin-2 (2 peptides) and ranatuerin-2 (1 peptide) families. Using a forward primer that was designed from a conserved region of the 5′-untranslated regions of Rana temporaria preprotemporins in a 3′-RACE procedure, a cDNA clone encoding preprotemporin-1SKa was prepared from R. sakuraii skin total RNA. Further preprotemporin cDNAs encoding temporin-1SKc (AVDLAKIANIAN KVLSSL F·NH 2 ) and temporin-1SKd (FLPMLAKLLSGFL·NH 2 ) were obtained by RT-PCR. Unexpectedly, the 3′-RACE procedure using the same primer led to amplification of a cDNA encoding a preprobradykinin whose signal peptide region was identical to that of preprotemporin-1SKa except for the substitution Ser 18 → Asn. R. sakuraii bradykinin ([Arg 0 ,Leu 1 ,Thr 6 ,Trp 8 ] BK) was 28-fold less potent than mammalian BK in effecting B2 receptor-mediated relaxation of mouse trachea and the des[Arg 0 ] derivative was only a weak partial agonist. The evolutionary history of the Japanese brown frogs is incompletely understood but a comparison of the primary structures of the R. sakuraii dermal peptides with those of Tago's brown frog Rana tagoi provides evidence for a close phylogenetic relationship between these species .

Published
2007

6. Antimicrobial peptides from diverse families isolated from the skin of the Asian frog, Rana grahami

Author

Conlon, J Michael, Al-Ghaferi, Nadia, Abraham, Bency, Jiansheng, Hu, Cosette, Pascal, Leprince, Jérôme, Jouenne, Thierry, Vaudry, Hubert, Conlon, J. Michael, Vaudry, Hu, Faculty of Medicine and Health Science, UAE University, Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)

Subjects
Male, Ranidae, Physiology, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Molecular Sequence Data, Antimicrobial peptides, Peptide, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, medicine.disease_cause, Biochemistry, Amphibian Proteins, Microbiology, 03 medical and health sciences, Cellular and Molecular Neuroscience, 0302 clinical medicine, Endocrinology, MESH: Skin, Salientia, MESH: Amphibian Proteins, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], medicine, Animals, Humans, MESH: Animals, Amino Acid Sequence, Candida albicans, Skin, 030304 developmental biology, Antibacterial agent, chemistry.chemical_classification, 0303 health sciences, MESH: Humans, MESH: Molecular Sequence Data, MESH: Ranidae, biology, MESH: Antimicrobial Cationic Peptides, biology.organism_classification, Antimicrobial, MESH: Male, chemistry, Staphylococcus aureus, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Frog Skin, 030217 neurology & neurosurgery, Antimicrobial Cationic Peptides
Abstract

International audience; Seven peptides with antimicrobial activity were isolated in pure form from an extract of the skin of the Yunnanfu Kunming frog Rana grahami Boulenger, 1917. The peptides were identified as belonging to the nigrocin-2 (three peptides), brevinin-1 (one peptide), brevinin-2 (three peptides), and esculentin-1 (one peptide) families. Nigrocin-2GRb (GLFGKILGVGKKVLCGLSGMC) containing three lysine residues, represented the peptide with highest potency against microorganisms (MIC = 3 microM against Escherichia coli, 12.5 microM against Staphylococcus aureus and 50 microM against Candida albicans) and the greatest hemolytic activity against human erythrocytes (LD50 = 40 microM). In contrast, nigrocin-2GRa (GLLSGILGAGKHIVCGLSGLC) and nigrocin-2GRc (GLLSGILGAGKNIVCGLSGLC), with only a single lysine residue, showed weak antimicrobial and hemolytic activity. Phylogenetic relationships among Eurasian ranid frogs are less well understood than those of North American ranids but the primary structures of the R. grahami antimicrobial peptides suggest a close relationship of this species with the Japanese pond frogs R. nigromaculata and R. porosa brevipoda.

Published
2006

7. Landmarks and Lineages in the Developing Heart

Author

Margaret Buckingham, Sigolène M. Meilhac, Richard P. Harvey, Victor Chang Cardiac Research Institute, University of New South Wales [Sydney] (UNSW), Biologie du Développement, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), R.P.H. is funded by the National Health and Medical Research Counsel of Australia (NHMRC), the Australian Research Counsel, the Australian Government through the Australia-India Strategic Research Fund, and the Australian Stem Cell Centre. S.M.M. and M.E.B. are funded by the Pasteur Institute and the Centre National de la Recherche Scientifique. R.P.H. is an NHMRC Australia Fellow, and S.M. is an Institut National de la Santé et de la Recherche Médicale research fellow., and Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Mesoderm, MESH: Integrases, MESH: Myocardium, MESH: T-Box Domain Proteins, Physiology, Context (language use), [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], Cell fate determination, Biology, 03 medical and health sciences, 0302 clinical medicine, myocardium, medicine, Paraxial mesoderm, MESH: Animals, cardiovascular diseases, MESH: Vertebrates, 030304 developmental biology, MESH: Mesoderm, 0303 health sciences, MESH: Conserved Sequence, MESH: Humans, MESH: Ranidae, MESH: Genes, Homeobox, [SDV.BDD.MOR]Life Sciences [q-bio]/Development Biology/Morphogenesis, Anatomy, Embryonic stem cell, MESH: Heart, atrioventricular canal, Somite, medicine.anatomical_structure, embryonic development, Embryology, cardiovascular system, Atrioventricular canal, Cardiology and Cardiovascular Medicine, T-box transcription factors, Neuroscience, 030217 neurology & neurosurgery
Abstract

See related article, pages 1267–1274 One of the overarching concepts underpinning mammalian embryonic development is that of “regulation.” This implies that the lineage potential of a particular cell is broader than its actual fate. Although the influential experiments in this area performed by Hans Driesch in the late 1800s concerned the fate of individual embryonic blastomeres, the concept of regulative development has pervaded all aspects of embryology, overlapping with the concept of regenerative fields. In the context of the heart, a good example is that of frog embryo cells fated to form the dorsal mesocardium and dorsal pericardial (splanchnic) mesoderm but which can “regulate” and form myocardial tissue if the normal heart is injured or extirpated.1 As we delve into the molecular mechanisms of developmental processes, we understand that limitations to cell fate are often set, particularly in the embryo, by geographical or environmental parameters, such as the source and strength of a secreted inductive signal, and these may change with time. Anatomic patterns or landmarks provide vital clues to how we should think about development and indeed disease. For example, segmentation of the embryonic paraxial mesoderm into repetitive units called somites, which bear one of the main progenitor populations for the musculoskeletal system, has been widely studied and it is known that somite segmentation is controlled by a network of synchronized molecular oscillators coupled by the Delta-Notch intercellular signaling system.2 The heart has also long been considered to have a segmental prepattern based, in part, on the series of swellings and constrictions that become evident during early heart tube formation and early fate-mapping experiments suggesting that these were the precursor structures of the chambers and their flanking regions, including the atrioventricular canal (AVC). This notion has been perpetuated as fact in embryology and medical textbooks with …

Published
2009

8. Host defense peptides from Lithobates forreri, Hylarana luctuosa, and Hylarana signata (Ranidae): phylogenetic relationships inferred from primary structures of ranatuerin-2 and brevinin-2 peptides

Author

Conlon, J Michael, Kolodziejek, Jolanta, Mechkarska, Milena, Coquet, Laurent, Leprince, Jérôme, Jouenne, Thierry, Vaudry, Hubert, Nielsen, Per, Nowotny, Norbert, King, Jay, Conlon, J. Michael, Faculty of Medicine and Health Science, UAE University, Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), University of Copenhagen = Københavns Universitet (KU), and Zoonoses and Emerging Infections Group

Subjects
Male, Ranidae, Physiology, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Biochemistry, MESH: Amphibian Proteins, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], Hylarana picturata, Lithobates forreri, Antimicrobial peptide Lithobates, MESH: Proteins, MESH: Animals, MESH: Phylogeny, Phylogeny, Skin, MESH: Microbial Sensitivity Tests, biology, MESH: Ranidae, Lithobates, MESH: Antimicrobial Cationic Peptides, Bacterial Infections, Hylarana luctuosa, Anti-Bacterial Agents, Ranatuerin-2, Hylarana, MESH: Bacterial Infections, Molecular Sequence Data, Zoology, Microbial Sensitivity Tests, Amphibian Proteins, MESH: Skin, Phylogenetics, MESH: Anti-Bacterial Agents, Genetics, Animals, Amino Acid Sequence, Molecular Biology, Brevinin-2, MESH: Molecular Sequence Data, Bacteria, Proteins, biology.organism_classification, Temporin, MESH: Male, MESH: Bacteria, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Hylarana signata, Antimicrobial Cationic Peptides
Abstract

International audience; The primary structures of host-defense peptides present in frog skin secretions constitute useful molecular markers for establishing taxonomic classifications and investigating phylogenetic relationships between species within a particular genus. Peptidomic analysis has led to the characterization of multiple host-defense peptides in norepinephrine-stimulated skin secretions of three species of frogs from the family Ranidae: Lithobates forreri (Boulenger, 1883), Hylarana luctuosa (Peters, 1871), and Hylarana signata (Günther, 1872). The L. forreri secretions contain ranatuerin-2 (2 peptides), brevinin-1 (4 peptides), and temporin (1 peptide). The H. luctuosa secretions contain brevinin-2 (4 peptides), esculentin-1 (1 peptide), esculentin-2 (1 peptide), palustrin-2 (2 peptides), and temporin (2 peptides). The H. signata secretions contain brevinin-2 (4 peptides), brevinin-1 (5 peptides), palustrin-2 (1 peptide), and temporin (2 peptides). Cladistic analysis based upon the primary structures of 44 ranatuerin-2 peptides from 20 Lithobates species indicates a close phylogenetic relationship between L. forreri, Lithobates onca, and Lithobates yavapaiensis. A similar cladistic analysis based upon the primary structures of 27 brevinin-2 peptides from 8 Hylarana species provides support for a close phylogenetic relationship between H. signata and Hylarana picturata, while showing that the species are not conspecific, with H. luctuosa more distantly related.

Published
2013

9. Efficient selection of branch-specific models of sequence evolution

Author

Emmanuel J. P. Douzery, Julien Y. Dutheil, Jonathan Romiguier, Nicolas Galtier, Bastien Boussau, Vincent Ranwez, Bioinformatics Research Center (BiRC), Institut des Sciences de l'Evolution de Montpellier (UMR ISEM), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-École pratique des hautes études (EPHE)-Université de Montpellier (UM)-Institut de recherche pour le développement [IRD] : UR226-Centre National de la Recherche Scientifique (CNRS), Amélioration génétique et adaptation des plantes méditerranéennes et tropicales (UMR AGAP), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro), Bioinformatique, phylogénie et génomique évolutive (BPGE), Département PEGASE [LBBE] (PEGASE), Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-École Pratique des Hautes Études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université de Montpellier (UM)-Institut de recherche pour le développement [IRD] : UR226-Centre National de la Recherche Scientifique (CNRS), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), University of California [Berkeley] (UC Berkeley), University of California (UC), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université de Montpellier (UM)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre National de la Recherche Scientifique (CNRS)-Institut de recherche pour le développement [IRD] : UR226, Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad), University of California [Berkeley], and University of California

Subjects
0106 biological sciences, Ranidae, [SDV]Life Sciences [q-bio], Molecular phylogenetics, 01 natural sciences, Cluster Analysis, MESH: Animals, MESH: Models, Genetic, MESH: Phylogeny, Phylogeny, MESH: Evolution, Molecular, Genetics, 0303 health sciences, Sequence, Phylogenetic tree, MESH: Ranidae, [SDV.BID.EVO]Life Sciences [q-bio]/Biodiversity/Populations and Evolution [q-bio.PE], Biological Evolution, MESH: Daphnia, dN, dS, Algorithms, Ancestral character reconstruction, Sequence alignment, MESH: Algorithms, MESH: Biological Evolution, Computational biology, Biology, 010603 evolutionary biology, Paml, Evolution, Molecular, 03 medical and health sciences, MESH: Computer Simulation, Molecular evolution, Animals, Computer Simulation, Cluster analysis, Molecular Biology, Selection, Ecology, Evolution, Behavior and Systematics, Selection (genetic algorithm), 030304 developmental biology, Models, Genetic, Model selection, MESH: Cluster Analysis, Daphnia, RNA, Ribosomal, MESH: Muramidase, MESH: RNA, Ribosomal, Muramidase, [INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM], Maximum likelihood
Abstract

International audience; The analysis of extant sequences shows that molecular evolution has been heterogeneous through time and among lineages. However, for a given sequence alignment, it is often difficult to uncover what factors caused this heterogeneity. In fact, identifying and characterizing heterogeneous patterns of molecular evolution along a phylogenetic tree is very challenging, for lack of appropriate methods. Users either have to a priori define groups of branches along which they believe molecular evolution has been similar or have to allow each branch to have its own pattern of molecular evolution. The first approach assumes prior knowledge that is seldom available, and the second requires estimating an unreasonably large number of parameters. Here we propose a convenient and reliable approach where branches get clustered by their pattern of molecular evolution alone, with no need for prior knowledge about the data set under study. Model selection is achieved in a statistical framework and therefore avoids overparameterization. We rely on substitution mapping for efficiency and present two clustering approaches, depending on whether or not we expect neighbouring branches to share more similar patterns of sequence evolution than distant branches. We validate our method on simulations and test it on four previously published data sets. We find that our method correctly groups branches sharing similar equilibrium GC contents in a data set of ribosomal RNAs and recovers expected footprints of selection through dN/dS. Importantly, it also uncovers a new pattern of relaxed selection in a phylogeny of Mantellid frogs, which we are able to correlate to life-history traits. This shows that our programs should be very useful to study patterns of molecular evolution and reveal new correlations between sequence and species evolution. Our programs can run on DNA, RNA, codon, or amino acid sequences with a large set of possible models of substitutions and are available at http://biopp.univ-montp2.fr/forge/testnh.

Published
2012
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10. Host defense peptides in skin secretions of the Oregon spotted frog Rana pretiosa: implications for species resistance to chytridiomycosis

Author

Conlon, J Michael, Mechkarska, Milena, Ahmed, Eman, Coquet, Laurent, Jouenne, Thierry, Leprince, Jérôme, Vaudry, Hubert, Hayes, Marc, Padgett-Flohr, Gretchen, Conlon, J. Michael, Faculty of Medicine and Health Science, UAE University, Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Différenciation et communication neuronale et neuroendocrine (DC2N)

Subjects
0106 biological sciences, Ranidae, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, 01 natural sciences, MESH: Chytridiomycota, Rana pretiosa, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], MESH: Animals, Peptide sequence, Skin, 0303 health sciences, education.field_of_study, MESH: Microbial Sensitivity Tests, biology, MESH: Ranidae, Ecology, MESH: Antimicrobial Cationic Peptides, MESH: Hemolysis, Rana boylii, Chytridiomycota, MESH: Immunity, Innate, Immunology, Antimicrobial peptides, Population, Molecular Sequence Data, Zoology, Microbial Sensitivity Tests, 010603 evolutionary biology, Hemolysis, 03 medical and health sciences, MESH: Mycoses, MESH: Skin, Animals, Humans, Chytridiomycosis, Amino Acid Sequence, education, 030304 developmental biology, MESH: Humans, MESH: Molecular Sequence Data, Host (biology), biology.organism_classification, Temporin, Immunity, Innate, Mycoses, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Developmental Biology, Antimicrobial Cationic Peptides
Abstract

International audience; Population declines due to chytridiomycosis among frogs belonging to the Amerana (Rana boylii) species group from western North America have been particularly severe. Norepinephrine-stimulated skin secretions from the Oregon spotted frog Rana pretiosa Baird and Girard, 1853 were collected from individuals that had been previously infected with the causative agent Batrachochytrium dendrobatidis but had proved resistant to developing chytridiomycosis. These secretions contained a more diverse array of antimicrobial peptides than found in other species from the Amerana group and 14 peptides were isolated in pure form. Determination of their primary structures identified the peptides as esculentin-2PRa and -2PRb; ranatuerin-2PRa, -2PRb, -2PRc, -2PRd, and -2PRe; brevinin-1PRa, -1PRb, -1PRc, and -1PRd; and temporin-PRa, -PRb, and -PRc. The strongly cationic ranatuerin-2PRd and the esculentin-2 peptides, which have not been identified in the secretions of other Amerana species except for the closely related R. luteiventris, showed the highest growth inhibitory potency against microorganisms. The strongly hydrophobic brevinin-1PRd was the most cytotoxic to erythrocytes. Although no clear correlation exists between production of dermal antimicrobial peptides by a species and its resistance to fatal chytridiomycosis, the diversity of these peptides in R. pretiosa may be pivotal in defending the species against environmental pathogens such as B. dendrobatidis.

Published
2010

11. Acute food deprivation reduces expression of diazepam-binding inhibitor, the precursor of the anorexigenic octadecaneuropeptide ODN, in mouse glial cells

Author

Schouft, Marie-Thérèse, Fontaine, Marc, Scalbert, Elisabeth, Malagon, Maria, Gandolfo, Pierrick, Desrues, Laurence, Cellier, Eric, Decker, Annick, Clerens, Stefan, Vandesande, Frans, Do-Rego, C., Beauvillain, C., Baroncini, Marc, Balment, Richard, Dujardin, Cynthia, Tollemer, Helene, BRUZZONE, FEDERICA, Tollemer, Hélène, Do-Régo, Jean, Simonnet, Guy, VALLARINO, MAURO, Beauvillain, Jean, Costentin, Jean, Do-Régo, Jean-Claude, Beauvillain, Jean-Claude, Chartrel, C, Alvear-Perez, P, Iturrioz, X., Reaux-Le Goazigo, A., Audinot, V., Chomarat, C, Coge, C, Nosjean, O., Rodriguez, M., Galizzi, J., Goazigo, R., Chomarat, P., Coge, F., Chartrel, Nicolas, Alonzeau, Jessy, Alexandre, David, Jeandel, Jean, Alvear-Perez, Rodrigo, Boutin, Jean, Anouar, Youssef, Llorens-Cortes, Catherine, Jeandel, Lydie, Carlier, Ludovic, Ségalas-Milazzo, Isabelle, Guilhaudis, Laure, Oulyadi, Hassan, Davoust, Daniel, Dubessy, Christophe, Scalbert, Elizabeth, Pfeiffer, Bruno, Renard, Pierre, Lihrmann, Isabelle, Pacaud, Pierre, Chevrier, Lucie, De Brevern, Alexandre, Hernandez, Eva, Guedj, Anne Marie, de Roux, Nicolas, Cholez, V, Debuysscher, V, Bourgeais, B, Boudot, B, Tron, F., Brassart, B., Regnier, A., Bissac, E, Pecnard, E, Gouilleux, F., Lassoued, K, Gouilleux-Gruart, V, Cholez, E, Bourgeais, J, Boudot, C., Gouilleux, V, Chuquet, Julien, Lecrux, Clotilde, Chatenet, David, Chazalviel, Laurent, Roussel, Simon, MacKenzie, Eric, Touzani, Omar, Tonon, M.C, Li, S., Leprince, J�r�me, Tonon, M.C., Compère, M, Lanfray, D, Castel, Hélène, Morin, M., Leprince, Jérôme, Dureuil, B, Vaudry, Hubert, Pelletier, G., Tonon, Marie-Christine, Compère, V., Morin, F., Dureuil, D, Vaudry, V, inconnu, Inconnu, Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), Chercheur indépendant, Laboratoire de l'intégration, du matériau au système (IMS), Centre National de la Recherche Scientifique (CNRS)-Institut Polytechnique de Bordeaux-Université Sciences et Technologies - Bordeaux 1, University of Córdoba [Córdoba], Institut de médecine moléculaire de Rangueil (I2MR), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-IFR150-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre de Recherche Jean-Pierre AUBERT Neurosciences et Cancer (JPArc - U837 Inserm), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université Lille 2 - Faculté de Médecine, UMR 5287, Homéostasie-Allostasie-Pathologie-Réhabilitation, Centre National de la Recherche Scientifique (CNRS), Neuropsycho-pharmacologie expérimentale, Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU), Institut de la Vision, Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physique et Physiologie Intégratives de l'Arbre Fruitier et Forestier (PIAF), Institut National de la Recherche Agronomique (INRA)-Université Blaise Pascal - Clermont-Ferrand 2 (UBP), Institut du Cerveau et de la Moëlle Epinière = Brain and Spine Institute (ICM), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Pitié-Salpêtrière [APHP]-Centre National de la Recherche Scientifique (CNRS), Neuropeptides centraux et régulations hydrique et cardiovasculaire, Université Pierre et Marie Curie - Paris 6 (UPMC)-Collège de France (CdF)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Recherches Servier, Centre de Recherches de Croissy, ESPE de l'Académie d'Amiens, Chimie Organique et Bioorganique : Réactivité et Analyse (COBRA), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie Organique Fine (IRCOF), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Equipe de Chimie Organique et Biologie Structurale (ECOBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA), Université Henri Poincaré - Nancy 1 (UHP), Institut de recherches Servier (INSTITUT DE RECHERCHES SERVIER), INSTITUT SERVIER, Les Laboratoires SERVIER, Institut de Recherche Servier, Institut du thorax, Université de Nantes (UN)-IFR26-Institut National de la Santé et de la Recherche Médicale (INSERM), Physiopathologie et neuroprotection des atteintes du cerveau en développement, Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), Bioinformatique génomique et moléculaire ((U 726)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Diderot - Paris 7 (UPD7), Service des Maladies Métaboliques et Endocriniennes, Hôpital Universitaire Carémeau [Nîmes], Neuroprotection du Cerveau en Développement / Promoting Research Oriented Towards Early Cns Therapies (PROTECT), Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Hôpital Robert Debré-Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Fédératif de Recherches Multidisciplinaires sur les Peptides (IFRMP 23), Institut National de la Santé et de la Recherche Médicale (INSERM)-CRLCC Henri Becquerel-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-CHU Rouen, Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Matrice extracellulaire et dynamique cellulaire - UMR 7369 (MEDyC), SFR CAP Santé (Champagne-Ardenne Picardie Santé), Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Université de Reims Champagne-Ardenne (URCA)-Centre National de la Recherche Scientifique (CNRS), STMicroelectronics, Génétique, immunothérapie, chimie et cancer (GICC), UMR 6239 CNRS [2008-2011] (GICC UMR 6239 CNRS), Université de Tours-Centre National de la Recherche Scientifique (CNRS), Matrice extracellulaire et régulations cellulaires (MERC), Université de Reims Champagne-Ardenne (URCA)-Centre National de la Recherche Scientifique (CNRS), Institut Armand Frappier (INRS-IAF), Réseau International des Instituts Pasteur (RIIP)-Institut National de la Recherche Scientifique [Québec] (INRS), Neurodégénérescence : modèles et stratégies thérapeutiques (NMST), Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Aix-Marseille Université - Faculté de pharmacie (AMU PHARM), Aix Marseille Université (AMU), IRCELYON-Ingéniérie, du matériau au réacteur (ING), Institut de recherches sur la catalyse et l'environnement de Lyon (IRCELYON), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Télécom SudParis (TSP), Université Sciences et Technologies - Bordeaux 1-Institut Polytechnique de Bordeaux-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Lille 2 - Faculté de Médecine -Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-CHU Pitié-Salpêtrière [APHP], CHU Rouen, Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-CRLCC Henri Becquerel-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Scientifique [Québec] (INRS)-Réseau International des Instituts Pasteur (RIIP), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre interdisciplinaire de recherche en biologie (CIRB), Collège de France (CdF)-Institut National de la Santé et de la Recherche Médicale (INSERM)-PSL Research University (PSL)-Centre National de la Recherche Scientifique (CNRS)-Collège de France (CdF)-Institut National de la Santé et de la Recherche Médicale (INSERM)-PSL Research University (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Chimie Organique Fine (IRCOF), Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université Le Havre Normandie (ULH), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Hôpital Universitaire Carémeau [Nîmes] (CHU Nîmes), Centre Hospitalier Universitaire de Nîmes (CHU Nîmes)-Centre Hospitalier Universitaire de Nîmes (CHU Nîmes), Université de Reims Champagne-Ardenne (URCA)-SFR CAP Santé (Champagne-Ardenne Picardie Santé), and Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Leptin, Male, Transcription, Genetic, MESH: Sequence Homology, Amino Acid, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, MESH: Receptors, G-Protein-Coupled, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, MESH: Neuropeptides, Energy homeostasis, MESH: Down-Regulation, MESH: Ependyma, Mice, 0302 clinical medicine, Endocrinology, Lateral Ventricles, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], Insulin, MESH: Animals, MESH: Proline-Rich Protein Domains, MESH: Peptide Fragments, MESH: Lateral Ventricles, Diazepam Binding Inhibitor, 2. Zero hunger, 0303 health sciences, MESH: Ranidae, MESH: Receptors, Kisspeptin-1, Fasting, medicine.anatomical_structure, Hypothalamus, Neuroglia, MESH: Neuroglia, Ependyma, Diazepam binding inhibitor, Injections, Intraperitoneal, MESH: Injections, Intraperitoneal, Protein Binding, MESH: Protein Transport, medicine.medical_specialty, MESH: Rats, Central nervous system, Down-Regulation, Neuropeptide, MESH: Fasting, MESH: Insulin, Biology, 03 medical and health sciences, Internal medicine, medicine, Animals, MESH: Protein Binding, Molecular Biology, MESH: Mice, Third Ventricle, MESH: RNA, Messenger, 030304 developmental biology, MESH: Transcription, Genetic, Neuropeptides, MESH: Time Factors, MESH: Rats, Wistar, MESH: Leptin, MESH: Hypothalamus, Peptide Fragments, MESH: Male, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, MESH: Diazepam Binding Inhibitor, 030217 neurology & neurosurgery, MESH: Third Ventricle
Abstract

In the central nervous system of mammals, the gene encoding diazepam-binding inhibitor (DBI) is exclusively expressed in glial cells. Previous studies have shown that central administration of a DBI processing product, the octadecaneuropeptide ODN, causes a marked inhibition of food consumption in rodents. Paradoxically, however, the effect of food restriction on DBI gene expression has never been investigated. Here, we show that in mice, acute fasting dramatically reduces DBI mRNA levels in the hypothalamus and the ependyma bordering the third and lateral ventricles. I.p. injection of insulin, but not of leptin, selectively stimulated DBI expression in the lateral ventricle area. These data support the notion that glial cells, through the production of endozepines, may relay peripheral signals to neurons involved in the central regulation of energy homeostasis.

Published
2010

12. Evidence from the primary structures of dermal antimicrobial peptides that Rana tagoi okiensis and Rana tagoi tagoi (Ranidae) are not conspecific subspecies

Author

Conlon, J Michael, Coquet, Laurent, Jouenne, Thierry, Leprince, Jérôme, Vaudry, Hubert, Iwamuro, Shawichi, Conlon, J. Michael, Faculty of Medicine and Health Science, UAE University, Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Différenciation et communication neuronale et neuroendocrine (DC2N)

Subjects
Male, Ranidae, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Rana tagoi, Peptide, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Subspecies, Toxicology, 0302 clinical medicine, MESH: Structure-Activity Relationship, Anti-Infective Agents, Salientia, Candida albicans, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], MESH: Animals, Chromatography, High Pressure Liquid, Skin, chemistry.chemical_classification, 0303 health sciences, MESH: Microbial Sensitivity Tests, biology, MESH: Ranidae, MESH: Peptides, Protein primary structure, Biochemistry, Female, Mitochondrial DNA, MESH: Terminology as Topic, Antimicrobial peptides, MESH: Anti-Infective Agents, Zoology, Microbial Sensitivity Tests, Structure-Activity Relationship, 03 medical and health sciences, Species Specificity, MESH: Skin, Terminology as Topic, Animals, MESH: Species Specificity, MESH: Chromatography, High Pressure Liquid, 030304 developmental biology, Bacteria, MESH: Candida albicans, biology.organism_classification, Temporin, MESH: Male, MESH: Bacteria, chemistry, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Peptides, MESH: Female, 030217 neurology & neurosurgery
Abstract

Morphological evidence and data from comparisons of nucleotide sequences of mitochondrial genes demonstrate considerable intraspecies variation among populations of the Japanese brown frog Rana tagoi Okada 1928 (Tago's brown frog). Five peptides with antimicrobial activity were isolated from an extract of the skins of specimens of Rana tagoi okiensis collected on the Oki Islands, Japan. Determination of their primary structures demonstrated that two peptides belong to the ranatuerin-2 family, two peptides to the temporin family, and one peptide to the brevinin-1 family. Ranatuerin-2 peptides were not previously identified in the skin of specimens of R. t. tagoi collected in Chiba Prefecture, Japan and the structures of the temporin peptides from R. t. okiensis (temporin-TOa: FLPILGKLLSGFL.NH 2 and temporin-TOb: FLPILGKLLSGLL.NH 2 ) are different from temporin-TGa (FLPILGKLLSGIL.NH 2 ) isolated from R. t. tagoi. Similarly, the acyclic C-terminally α-amidated brevinin-1 peptide from R. t. okiensis (Brevinin-1TOa, GIGSILGVIAKGLPTLISWIKNR.NH 2 ) shows three amino acid substitutions (Gly 1 → Ala, Val 8 → Ala, Ile 9 → Leu) compared to the ortholog from R. t. tagoi . In addition, bradykinin, identical to the mammalian peptide, is present in high concentration in the skin of R. t. okiensis but not R. t. tagoi . The data provide evidence to support the proposal that R. t. tagoi and R. t. okiensis should be regarded as separate species ( R. tagoi and R. okiensis ) rather than conspecific subspecies.

Published
2010

13. Primary structures of skin antimicrobial peptides indicate a close, but not conspecific, phylogenetic relationship between the leopard frogs Lithobates onca and Lithobates yavapaiensis (Ranidae)

Author

Conlon, J Michael, Coquet, Laurent, Leprince, Jérôme, Jouenne, Thierry, Vaudry, Hubert, King, Jay, Conlon, J. Michael, King, Jay., Faculty of Medicine and Health Science, UAE University, Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Différenciation et communication neuronale et neuroendocrine (DC2N)

Subjects
0106 biological sciences, Ranidae, Physiology, Health, Toxicology and Mutagenesis, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Toxicology, medicine.disease_cause, 01 natural sciences, Biochemistry, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], Candida albicans, MESH: Animals, MESH: Phylogeny, Phylogeny, Skin, 0303 health sciences, MESH: Microbial Sensitivity Tests, biology, MESH: Ranidae, Ecology, MESH: Escherichia coli, MESH: Peptides, Lithobates, MESH: Molecular Weight, MESH: Antimicrobial Cationic Peptides, General Medicine, Haemolysis, MESH: Hemolysis, Staphylococcus aureus, Antimicrobial peptides, Molecular Sequence Data, Zoology, Microbial Sensitivity Tests, 010603 evolutionary biology, Hemolysis, 03 medical and health sciences, MESH: Skin, Phylogenetics, medicine, Escherichia coli, Animals, Amino Acid Sequence, 030304 developmental biology, MESH: Molecular Sequence Data, MESH: Candida albicans, Leopard frog, Cell Biology, biology.organism_classification, Temporin, Molecular Weight, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Peptides, Frog Skin, Antimicrobial Cationic Peptides
Abstract

International audience; The phylogenetic relationship between the relict leopard frog Lithobates (Rana) onca (Cope, 1875) and the lowland leopard frog Lithobates (Rana) yavapaiensis (Platz and Frost, 1984) is unclear. Chromatographic analysis of norepinephrine-stimulated skin secretions from L. onca led to the identification of six peptides with antimicrobial activity. Determination of their primary structures indicated that four of the peptides were identical to brevinin-1Ya, brevinin-1Yb, brevinin-1Yc and ranatuerin-2Ya previously isolated from skin secretions of L. yavapaiensis. However, a peptide belonging to the temporin family (temporin-ONa: FLPTFGKILSGLF.NH(2)) and an atypical member of the ranatuerin-2 family containing a C-terminal cyclic heptapeptide domain (ranatuerin-2ONa: GLMDTVKNAAKNLAGQMLDKLKCKITGSC) were isolated from the L. onca secretions but were not present in the L. yavapaiensis secretions. Ranatuerin-2ONa inhibited the growth of Escherichia coli (MIC=50muM) and Candida albicans (MIC=100muM ) and showed hemolytic activity (LC(50)=90muM) but was inactive against Staphylococcus aureus. The data indicate a close phylogenetic relationship between L. onca and L. yavapaiensis but suggest that they are not conspecific species.

Published
2009

14. Antimicrobial peptides from the skin secretions of the South-East Asian frog Hylarana erythraea (Ranidae)

Author

Al-Ghaferi, Nadia, Kolodziejek, Jolanta, Nowotny, Norbert, Coquet, Laurent, Jouenne, Thierry, Leprince, Jérôme, Vaudry, Hubert, King, Jay, Conlon, J Michael, King, Jay., Conlon, J. Michael, Zoonoses and Emerging Infections Group, Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), Faculty of Medicine and Health Science, and UAE University

Subjects
Male, Ranidae, Physiology, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Antimicrobial peptides, Molecular Sequence Data, MESH: Sequence Alignment, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Microbial Sensitivity Tests, medicine.disease_cause, Biochemistry, Rana erythraea, Microbiology, 03 medical and health sciences, Cellular and Molecular Neuroscience, Endocrinology, Hylarana, MESH: Skin, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], medicine, Animals, MESH: Animals, Amino Acid Sequence, MESH: Phylogeny, Peptide sequence, Phylogeny, 030304 developmental biology, Antibacterial agent, Skin, 0303 health sciences, MESH: Microbial Sensitivity Tests, MESH: Molecular Sequence Data, biology, MESH: Ranidae, 030306 microbiology, MESH: Antimicrobial Cationic Peptides, biology.organism_classification, Temporin, MESH: Male, Staphylococcus aureus, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Female, Frog Skin, MESH: Female, Sequence Alignment, Antimicrobial Cationic Peptides
Abstract

International audience; Peptidomic analysis of norepinephrine-stimulated skin secretions of the South-East Asian frog Hylarana erythraea (formerly Rana erythraea partim) has led to the identification of multiple peptides with antimicrobial activity. Structural characterization of the peptides demonstrated that they belong to the brevinin-1 (3), brevinin-2 (2), esculentin-2 (4), and temporin (1) families. The values in parentheses indicate the number of paralogs. In addition, a peptide (GVIKSVLKGVAKTVALG ML.NH(2)) was isolated that shows some structural similarity to the brevinin-2-related peptides (B2RP) previously isolated from North American frogs of the genus Lithobates. A synthetic replicate of the species B2RP showed broad-spectrum growth inhibitory activity against reference strains of Escherichia coli (MIC=12.5 microM), Staphylococcus aureus (MIC=12.5 microM) and Candida albicans (MIC=50 microM) and was active against multidrug-resistant clinical isolates of Acetinobacter baumannii (MIC in the range 6-12.5 microM). The hemolytic activity of the peptide was relatively low (LC(50)=280 microM). Phylogenetic analysis based upon the amino acid sequences of 47 brevinin-2 peptides from 17 Asian species belonging to the family Ranidae provides support for the placement of H. erythraea in the genus Hylarana.

Published
2009

15. Antimicrobial peptides from the skin secretions of the New World frogs Lithobates capito and Lithobates warszewitschii (Ranidae)

Author

Conlon, J Michael, Meetani, Mohammed, Coquet, Laurent, Jouenne, Thierry, Leprince, Jérôme, Vaudry, Hubert, Kolodziejek, Jolanta, Nowotny, Norbert, King, Jay, Conlon, J. Michael, King, Jay., Faculty of Medicine and Health Science, UAE University, Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), and Zoonoses and Emerging Infections Group

Subjects
0106 biological sciences, Bodily Secretions, Ranidae, Physiology, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, 01 natural sciences, Biochemistry, Rana areolata, MESH: Bodily Secretions, Endocrinology, Anti-Infective Agents, Salientia, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], MESH: Animals, MESH: Phylogeny, Phylogeny, Antibacterial agent, Skin, 0303 health sciences, MESH: Microbial Sensitivity Tests, biology, MESH: Ranidae, Ecology, Lithobates, MESH: Antimicrobial Cationic Peptides, MESH: Hemolysis, Lithobates tarahumarae, Antimicrobial peptides, Molecular Sequence Data, MESH: Anti-Infective Agents, MESH: Sequence Alignment, Zoology, Microbial Sensitivity Tests, 010603 evolutionary biology, Hemolysis, 03 medical and health sciences, Cellular and Molecular Neuroscience, MESH: Skin, Animals, Humans, Amino Acid Sequence, 030304 developmental biology, MESH: Humans, MESH: Molecular Sequence Data, biology.organism_classification, Temporin, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Frog Skin, Sequence Alignment, Antimicrobial Cationic Peptides
Abstract

Taxonomic revisions within the anuran family Ranidae have established the genus Lithobates that currently comprises 49 species of frogs from the New World. Peptidomic analysis, using reversed-phase HPLC with on-line detection by electrospray mass spectrometry, has led to the identification of multiple antimicrobial peptides in norepinephrine-stimulated skin secretions of the North American frog Lithobates capito and the Central American frog Lithobates warszewitschii . Structural characterization of the peptides demonstrated that the L. capito secretions contained brevinin-1 (1), esculentin-1 (1), esculentin-2 (1), ranatuerin-2 (3), and temporin (2) peptides. L. warszewitschii secretions contained brevinin-1 (1), esculentin-2 (1), ranatuerin-2 (2), and temporin (1) peptides. Values in parentheses indicate number of peptides in each family. Temporin-CPa from L. capito , with the atypical structure IPPFIKKVLTTVF·NH 2 , also showed atypical growth-inhibitory activity having greater potency against Escherichia coli (MIC = 25 μM) and Candida albicans (MIC = 25 μM) than against Staphylococcus aureus (MIC = 50 μM). Phylogenetic analysis based upon the amino acid sequences of 37 ranatuerin-2 peptides from 17 species belonging to the genus Lithobates provides support for currently accepted taxonomic relationships. L. capito is sister-group to Lithobates sevosus in a clade that also contains Lithobates areolatus , and Lithobates palustris . L. warszewitschii is most closely related to the Central American species Lithobates tarahumarae and Lithobates vaillanti .

Published
2009

16. Peptides with potent cytolytic activity from the skin secretions of the North American leopard frogs, Lithobates blairi and Lithobates yavapaiensis

Author

Conlon, J Michael, Ahmed, Eman, Coquet, Laurent, Jouenne, Thierry, Leprince, Jérôme, Vaudry, Hubert, King, Jay, Conlon, J. Michael, Faculty of Medicine and Health Science, UAE University, Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Différenciation et communication neuronale et neuroendocrine (DC2N)

Subjects
0106 biological sciences, Ranidae, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Peptide, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Toxicology, medicine.disease_cause, 01 natural sciences, Anti-Infective Agents, Candida albicans, MESH: Amphibian Proteins, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], MESH: Staphylococcus aureus, MESH: Animals, Chromatography, High Pressure Liquid, Skin, chemistry.chemical_classification, 0303 health sciences, MESH: Microbial Sensitivity Tests, MESH: Tissue Extracts, biology, MESH: Ranidae, MESH: Peptides, MESH: Escherichia coli, Lithobates, MESH: Antimicrobial Cationic Peptides, MESH: Cell Survival, Staphylococcus aureus, Cell Survival, MESH: Anti-Infective Agents, Antineoplastic Agents, Microbial Sensitivity Tests, 010603 evolutionary biology, Amphibian Proteins, Microbiology, Cell Line, 03 medical and health sciences, MESH: Skin, medicine, Escherichia coli, Animals, Humans, MESH: Chromatography, High Pressure Liquid, 030304 developmental biology, MESH: Humans, MESH: Candida albicans, Lithobates blairi, Leopard frog, biology.organism_classification, MESH: North America, MESH: Cell Line, chemistry, North America, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, MESH: Antineoplastic Agents, Peptides, Frog Skin, Antimicrobial Cationic Peptides
Abstract

International audience; Six structurally similar and strongly cationic peptides belonging to the brevinin-1 family were isolated from skin secretions of the plains leopard frog Lithobates blairi and the lowland leopard frog Lithobates yavapaiensis on the basis of their antimicrobial activities. Brevinin-1BLc (FLPIIAGIAAKFLPKIFCTISKKC) from L. blairi represented the most potent peptide (MIC=25microM Escherichia coli, MIC=1.5microM Staphylococcus aureus, MIC=3microM Candida albicans, LC(50)=9microM human erythrocytes and LC(50)=6microM HepG2 human hepatoma-derived cells). The appreciably lower antimicrobial potencies of brevinin-1Ya and -1Yc from L. yavapaiensis correlate with the decreases in cationicity produced by the amino acid substitutions Lys(11)-->Asn (brevinin-1Ya) and Pro(14)-->Glu (brevinin-1Yc). In addition, a peptide isolated from the skin secretions of L. yavapaiensis belonging to the ranatuerin-2 family (ranatuerin-2Ya; GLMDTIKGVAKTVAASWLDKLKCKIT GC) inhibited the growth of E. coli (MIC=50microM) and S. aureus (MIC=50microM). In contrast to brevinin-1BLc, ranatuerin-2Ya showed appreciably greater cytolytic activity against HepG2 cells (LC(50)=20microM) than against erythrocytes (LC(50)>100microM).

Published
2009

17. Purification of peptides with differential cytolytic activities from the skin secretions of the Central American frog, Lithobates vaillanti (Ranidae)

Author

Conlon, J Michael, Raza, Haider, Coquet, Laurent, Jouenne, Thierry, Leprince, Jérôme, Vaudry, Hubert, King, Jay, Conlon, J. Michael, King, Jay., Faculty of Medicine and Health Science, UAE University, University of Ulster, Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Différenciation et communication neuronale et neuroendocrine (DC2N)

Subjects
Male, Bodily Secretions, Erythrocytes, Ranidae, Physiology, Health, Toxicology and Mutagenesis, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Peptide, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Toxicology, Biochemistry, MESH: Dose-Response Relationship, Drug, MESH: Bodily Secretions, Norepinephrine, 0302 clinical medicine, MESH: Liver Neoplasms, MESH: Amphibian Proteins, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], Candida albicans, MESH: Staphylococcus aureus, MESH: Animals, Pancreatic elastase, Peptide sequence, Skin, chemistry.chemical_classification, 0303 health sciences, MESH: Microbial Sensitivity Tests, biology, MESH: Ranidae, Molecular Structure, MESH: Escherichia coli, MESH: Peptides, Cytotoxins, Lithobates, MESH: Erythrocytes, Liver Neoplasms, MESH: Antimicrobial Cationic Peptides, General Medicine, Antimicrobial, MESH: Hemolysis, Elastase inhibitor, MESH: Cell Survival, Female, MESH: Cytotoxins, Elafin, Costa Rica, Staphylococcus aureus, MESH: Cell Line, Tumor, Cell Survival, MESH: Molecular Structure, Molecular Sequence Data, Microbial Sensitivity Tests, Hemolysis, Amphibian Proteins, Microbiology, 03 medical and health sciences, Scissile bond, MESH: Skin, MESH: Norepinephrine, Cell Line, Tumor, Escherichia coli, Animals, Humans, Amino Acid Sequence, MESH: Costa Rica, 030304 developmental biology, MESH: Humans, MESH: Molecular Sequence Data, Dose-Response Relationship, Drug, MESH: Candida albicans, Cell Biology, biology.organism_classification, MESH: Male, chemistry, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Peptides, MESH: Female, 030217 neurology & neurosurgery, Antimicrobial Cationic Peptides
Abstract

International audience; Peptide-based defenses of ranid frogs from Mexico and Central America have been studied in much less detail than those from North America. Peptides belonging to the brevinin-1 (5 peptides), palustrin-2 (1 peptide), and ranatuerin-2 (3 peptides) families were isolated from norepinephrine-stimulated skin secretions of the Costa Rican frog, Lithobates vaillanti (Ranidae) and characterized structurally. Brevinin-1VLa (FLGAIAGVAAKFLPKVFCFITKKC) and brevinin-1VLc (FLPVIASVAAKVLPK VFCFITKKC) showed particularly high growth-inhibitory potency (MIC < or =3 microM) against a Gram-positive microorganism Staphylococcus aureus and the opportunistic yeast pathogen Candida albicans and potent cytolytic activity (LC(50)< or =8 microM) against both human erythrocytes and HepG2 hepatoma-derived cells. The peptides were also active against a Gram-negative microorganism Escherichia coli (MIC< or =50 microM). Substitutions in brevinin-1VLd (Lys(11) --> Asn) and brevinin-1VLe (Lys(11) --> Ser) that decrease cationicity result in loss of activity against E. coli. Ranatuerin-2VLb (GIMDTIKGAAKDLAGQLLDKLKCKITKC) showed relatively weak antimicrobial activity (MIC> or =75 microM) but selective cytolytic activity against HepG2 tumor cells (LC(50)=30 microM) compared with erythrocytes (LC(50)>200 microM). In addition, a dodecapeptide (RICYAMWIPYPC) were isolated from the secretions that were devoid of antimicrobial activity. This component contains an Ala-Met bond that constitutes the scissile bond in the selective elastase inhibitor, elafin but the peptide did not inhibit pancreatic elastase at concentrations up to 100 microM.

Published
2009

18. A potent, non-toxic insulin-releasing peptide isolated from an extract of the skin of the Asian frog, Hylarana guntheri (Anura:Ranidae)

Author

Conlon, J Michael, Power, Gavin, Abdel-Wahab, Yasser, Flatt, Peter, Jiansheng, Hu, Coquet, Laurent, Leprince, Jérôme, Jouenne, Thierry, Vaudry, Hubert, Conlon, J. Michael, Abdel-Wahab, Yasser H.A., Vaudry, Hu, Faculty of Medicine and Health Science, UAE University, Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Différenciation et communication neuronale et neuroendocrine (DC2N)

Subjects
Blood Glucose, Male, Ranidae, Physiology, medicine.medical_treatment, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Clinical Biochemistry, Peptide, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Pharmacology, MESH: Insulin Secretion, Biochemistry, MESH: Insulin-Secreting Cells, chemistry.chemical_compound, Mice, 0302 clinical medicine, Endocrinology, Insulin-Secreting Cells, MESH: Amphibian Proteins, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], Insulin Secretion, Insulin, MESH: Animals, Peptide sequence, Antibacterial agent, Skin, chemistry.chemical_classification, 0303 health sciences, MESH: Ranidae, MESH: Antimicrobial Cationic Peptides, 3. Good health, medicine.medical_specialty, Basal rate, MESH: Rats, Molecular Sequence Data, 030209 endocrinology & metabolism, MESH: Insulin, Biology, Amphibian Proteins, Cell Line, 03 medical and health sciences, Cellular and Molecular Neuroscience, MESH: Skin, Internal medicine, Lactate dehydrogenase, medicine, Animals, Amino Acid Sequence, MESH: Mice, 030304 developmental biology, MESH: Molecular Sequence Data, Temporin, MESH: Male, MESH: Cell Line, Rats, chemistry, MESH: Blood Glucose, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Frog Skin, Antimicrobial Cationic Peptides
Abstract

Peptides in extract of the skin of the Asian frog Hylarana guntheri Boulenger,1882 were purified by reversed-phase HPLC and individual components analysed for their ability to release insulin from the rat BRIN-BD11 clonal beta cell line. The most potent peptide identified in the extract belonged to the brevinin-2 family (brevinin-2GUb; GVIIDTLKGAAKTVAAELLRKAHCKLTNSC). Other peptides with weaker insulin-releasing activity belonged to the brevinin-1 (2 peptides), brevinin-2 (2 peptides) and temporin (3 peptides) families. Only the brevinin-1 peptides showed cytolytic activity against the BRIN-BD11 cells, as demonstrated by an increased rate of release of the cytosolic enzyme, lactate dehydrogenase. A synthetic replicate of brevinin-2GUb produced a significant stimulation of insulin release (139% of basal rate; P

Published
2008

19. In vitro spermicidal activity of peptides from amphibian skin: dermaseptin S4 and derivatives

Author

Amira Zairi, Khaled Hani, Frédéric Tangy, Catherine Serres, Pierre Jouannet, Laboratoire de biochimie, Faculté de médecine de Sousse [Ibn EL Jazzar], Service de biologie de la reproduction-CECOS, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital Cochin [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Université Paris Descartes - Paris 5 (UPD5)-EA1752, Virus Lents, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-CHU Cochin [AP-HP]-Université Paris Descartes - Paris 5 (UPD5)-EA1752, Assistance publique - Hôpitaux de Paris (AP-HP) - CHU Cochin [AP-HP] - Université Paris Descartes - Paris 5 (UPD5) - EA1752, Institut Pasteur [Paris] - Centre National de la Recherche Scientifique (CNRS), and Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Male, Ranidae, Clinical Biochemistry, Pharmaceutical Science, Peptide, Pharmacology, Biochemistry, MESH: Dose-Response Relationship, Drug, HeLa, MESH: Structure-Activity Relationship, Drug Discovery, MESH: Amphibian Proteins, MESH: Animals, Cytotoxicity, Skin, chemistry.chemical_classification, 0303 health sciences, biology, MESH: Ranidae, Chemistry, MESH: Peptides, MESH: Antimicrobial Cationic Peptides, Antimicrobial, MESH: Spermatocidal Agents, 3. Good health, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Toxicity, Molecular Medicine, Female, Static Electricity, Spermatocidal Agents, Amphibian Proteins, Structure-Activity Relationship, 03 medical and health sciences, MESH: Skin, MESH: Electrostatics, Animals, Humans, Potency, [SDV.MP] Life Sciences [q-bio]/Microbiology and Parasitology, Molecular Biology, 030304 developmental biology, Dermaseptin, MESH: Humans, Dose-Response Relationship, Drug, 030306 microbiology, Spermicide, Organic Chemistry, biology.organism_classification, MESH: Male, MESH: Hela Cells, Immunology, Peptides, MESH: Female, Antimicrobial Cationic Peptides, HeLa Cells
Abstract

Sexually transmitted infections and unplanned pregnancies present a great risk to the reproductive health of women. Therefore, female-controlled vaginal products directed toward disease prevention and contraception are needed urgently. In the present study, efforts were made to evaluate the contraceptive potency of dermaseptin DS4, an antimicrobial peptide derived from frog skin. To assess the structure–activity relationship between the native DS4 and its derivatives, a set of chemically modified peptides was synthesized and evaluated. Normal human semen samples were used to detect the spermicidal activity of the new compounds. HeLa cultures were used to determine the safety of compounds toward their toxicity. Fluorescent-binding assays were performed to evaluate the rapidity and the irreversibility of the sperm-immobilizing activity of peptides. All DS4 derivatives elicited concentration-dependent spermicidal activity at microgram concentrations (EC100 values: 25 μg/ml–l mg/ml). The order was K4S4 = S4a > S4 > K4S4(1–16)a > S4(6–28). In cytotoxicity assay, some compounds were found to be significantly safer than nonoxynol-9, the most widely used spermicide, and their activity was not accompanied by total loss of plasma membrane integrity as detected by fluorescent microscopy. Our data also show that increasing the number of positive charges of the peptide resulted in a reduced cytotoxicity without affecting the spermicidal effect. This study indicates that dermaseptins are spermicidal molecules that deserve to be tested as topical contraceptive with useful activities that can add to their prophylaxis, safety, and effectiveness.

Published
2008

20. Peptidomic analysis of skin secretions from Rana heckscheri and Rana okaloosae provides insight into phylogenetic relationships among frogs of the Aquarana species group

Author

Conlon, J Michael, Coquet, Laurent, Leprince, Jérôme, Jouenne, Thierry, Vaudry, Hubert, Kolodziejek, Jolanta, Nowotny, Norbert, Bevier, Catherine, Moler, Paul, Conlon, J. Michael, Faculty of Medicine and Health Science, UAE University, Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), and Zoonoses and Emerging Infections Group

Subjects
Male, Ranidae, Physiology, MESH: Sequence Analysis, Protein, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Clinical Biochemistry, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Biochemistry, Monophyly, 0302 clinical medicine, Endocrinology, Sequence Analysis, Protein, MESH: Amphibian Proteins, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], MESH: Proteins, MESH: Animals, Cloning, Molecular, MESH: Phylogeny, Chromatography, High Pressure Liquid, Phylogeny, Antibacterial agent, Skin, 0303 health sciences, biology, integumentary system, MESH: Ranidae, Ecology, MESH: Peptides, MESH: Antimicrobial Cationic Peptides, Rana clamitans, Molecular Sequence Data, MESH: Sequence Alignment, Zoology, Peptides, Cyclic, Amphibian Proteins, Rana, 03 medical and health sciences, Cellular and Molecular Neuroscience, Alkaloids, Species Specificity, MESH: Skin, Phylogenetics, MESH: Alkaloids, Animals, MESH: Species Specificity, MESH: Cloning, Molecular, Amino Acid Sequence, MESH: Chromatography, High Pressure Liquid, MESH: Peptides, Cyclic, 030304 developmental biology, MESH: Molecular Sequence Data, Proteins, biology.organism_classification, Temporin, MESH: Male, MESH: Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Rana grylio, Peptides, Frog Skin, Sequence Alignment, 030217 neurology & neurosurgery, Antimicrobial Cationic Peptides
Abstract

International audience; The members of the Aquarana (or Rana catesbeiana species group) form a monophyletic group comprising seven species: R. catesbeiana, Rana clamitans, Rana grylio, Rana virgatipes, Rana septentrionalis, Rana heckscheri and Rana okaloosae. Previous work has led to structural characterization of the antimicrobial peptides present in electrically-stimulated skin secretions from the first five species listed and this study presents the primary structures of orthologs from the river frog R. heckscheri and the Florida bog frog R. okaloosae. Peptidomic analysis of R. heckscheri and R. okaloosae skin secretions led to the identification of peptides with antimicrobial activity belonging to the ranalexin, ranatuerin-2, and temporin families. In addition, a peptide (GFLDIIKDTGKDFAVKILNNLKCKLAGGCPR) was isolated from R. okaloosae whose primary structure identified it as a member of the palustrin-2 family. Consistent with previous data based upon morphological analysis and comparisons of the nucleotide sequences of mitochondrial and ribosomal genes, cladistic analysis based upon a comparison of the amino acid sequences of antimicrobial peptides indicates a sister-group relationship between R. heckscheri and R. grylio and a close, but less well defined, phylogenetic relationship between R. okaloosae and R. clamitans.

Published
2007

21. A family of antimicrobial peptides related to japonicin-2 isolated from the skin of the chaochiao brown frog Rana chaochiaoensis

Author

Conlon, J Michael, Leprince, Jérôme, Vaudry, Hu, Jiansheng, Hu, Nielsen, Per, Conlon, J. Michael, Vaudry, Hubert, Faculty of Medicine and Health Science, UAE University, Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), and University of Copenhagen = Københavns Universitet (KU)

Subjects
0106 biological sciences, Ranidae, Physiology, MESH: Sequence Homology, Amino Acid, Health, Toxicology and Mutagenesis, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Toxicology, medicine.disease_cause, 01 natural sciences, Biochemistry, Japonica, MESH: Amphibian Proteins, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], MESH: Staphylococcus aureus, MESH: Animals, Skin, 0303 health sciences, MESH: Microbial Sensitivity Tests, biology, MESH: Ranidae, MESH: Escherichia coli, MESH: Peptides, MESH: Antimicrobial Cationic Peptides, General Medicine, Antimicrobial, Anti-Bacterial Agents, Staphylococcus aureus, Female, Molecular Sequence Data, Antimicrobial peptides, Microbial Sensitivity Tests, 010603 evolutionary biology, Rana chaochiaoensis, Amphibian Proteins, Microbiology, 03 medical and health sciences, Minimum inhibitory concentration, MESH: Skin, MESH: Anti-Bacterial Agents, Escherichia coli, medicine, Animals, Amino Acid Sequence, 030304 developmental biology, MESH: Molecular Sequence Data, Sequence Homology, Amino Acid, Cell Biology, biology.organism_classification, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Peptides, Frog Skin, MESH: Female, Antimicrobial Cationic Peptides
Abstract

International audience; Four structurally-related peptides with antimicrobial activity were isolated from an extract of the skin of the Chinese brown frog, Rana chaochiaoensis Liu, 1946. Determination of their primary structures revealed that they are members of the japonicin-2 family, previously identified only in the skin of the Japanese brown frog, R. japonica. Japonicin-2CHa (FVLPLLGILPKELCIVLKKNC) represented the most abundant peptide in the extract but its growth-inhibitory potency against Staphylococcus aureus (minimum inhibitory concentration, MIC=100 microM) and Escherichia coli (MIC>100 microM) was appreciably less than that of the more cationic japonicin-2 (FGLPMLSILPKALCILLKRKC). The high degree of structural similarity of japonicin-2CHb (VVPAFVLLKKAICIMLKRNC) with japonicin-2CHc (K9 --> R), and japonicin-2CHd (L16 --> F) is suggestive of recent gene duplication events. The data indicate a close phylogenetic relationship between R. chaochiaoensis and R. japonica but demonstrate that the species are not conspecific.

Published
2006

22. Antimicrobial peptides from the skin of the Tsushima brown frog Rana tsushimensis

Author

Conlon, J Michael, Al-Ghaferi, Nadia, Abraham, Bency, Sonnevend, Agnes, Coquet, Laurent, Leprince, Jérôme, Jouenne, Thierry, Vaudry, Hubert, Iwamuro, Shawichi, Conlon, J. Michael, Faculty of Medicine and Health Science, UAE University, Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Différenciation et communication neuronale et neuroendocrine (DC2N)

Subjects
0106 biological sciences, Ranidae, MESH: Drug Resistance, Microbial, Physiology, MESH: Sequence Homology, Amino Acid, Health, Toxicology and Mutagenesis, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Peptide, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Toxicology, medicine.disease_cause, 01 natural sciences, Biochemistry, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], MESH: Animals, Peptide sequence, Conserved Sequence, Skin, chemistry.chemical_classification, 0303 health sciences, MESH: Microbial Sensitivity Tests, MESH: Conserved Sequence, biology, MESH: Ranidae, MESH: Molecular Weight, MESH: Antimicrobial Cationic Peptides, Drug Resistance, Microbial, General Medicine, MESH: Hemolysis, Amino acid, Staphylococcus aureus, Female, Antimicrobial peptides, Molecular Sequence Data, Microbial Sensitivity Tests, Rana tsushimensis, 010603 evolutionary biology, Hemolysis, Microbiology, 03 medical and health sciences, MESH: Skin, medicine, Animals, Humans, Amino Acid Sequence, 030304 developmental biology, MESH: Molecular Sequence Data, MESH: Humans, Sequence Homology, Amino Acid, MESH: Methicillin Resistance, Cell Biology, biology.organism_classification, Temporin, Molecular Weight, chemistry, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Methicillin Resistance, Frog Skin, MESH: Female, Antimicrobial Cationic Peptides
Abstract

International audience; The Tsushima brown frog Rana tsushimensis Stejneger, 1907 exists in reproductive isolation on the island of Tsushima, Japan. Six peptides with antimicrobial activity were isolated in pure form from an extract of the skin of this species and their amino acid sequences identified them as members of the brevinin-1 (one peptide), brevinin-2 (one peptide) and temporin (four peptides) families. The C-terminally alpha-amidated brevinin-1 peptide (FLGSIVGALASALPSLISKIRN.NH2) lacks the cyclic heptapeptide domain Cys18-(Xaa)4-Lys-Cys24 at the COOH-terminus of the molecule that characterizes other members of that family. A structurally similar brevinin-1 peptide, also lacking the cyclic domain, was previously isolated from the skin of the Ryukyu brown frog Rana okinavana, indicative of a close phylogenetic relationship between the species. Brevinin-2TSa (GIMSLFKGVLKTAGKHVAGSLVDQLKCKITGGC) showed broad-spectrum growth inhibitory activity against a range of Gram-negative and Gram-positive bacteria (including methicillin-resistant Staphylococcus aureus) (minimum inhibitory concentrations< or =25 microM) and relatively low hemolytic activity against human erythrocytes (LD50=100 microM). The peptide therefore represents a candidate for drug development.

Published
2006

23. Structure and functions of the novel hypothalamic RFamide neuropeptides R-RFa and 26RFa in vertebrates

Author

Chartrel, Nicolas, BRUZZONE, FEDERICA, Leprince, Jérôme, Tollemer, Hélène, Anouar, Youssef, Do-Régo, Jean, Ségalas-Milazzo, Isabelle, Guilhaudis, Laure, Cosette, Pascal, Jouenne, Thierry, Simonnet, Guy, VALLARINO, MAURO, Beauvillain, Jean, Costentin, Jean, Vaudry, Hubert, Do-Régo, Jean-Claude, Beauvillain, Jean-Claude, Différenciation et communication neuronale et neuroendocrine (DC2N), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Neuroendocrinologie cellulaire et moléculaire, Chimie Organique et Bioorganique : Réactivité et Analyse (COBRA), Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie Organique Fine (IRCOF), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Equipe de Chimie Organique et Biologie Structurale (ECOBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU), Polymères Biopolymères Surfaces (PBS), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), UMR 5287, Homéostasie-Allostasie-Pathologie-Réhabilitation, Centre National de la Recherche Scientifique (CNRS), Neuropsycho-pharmacologie expérimentale, Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU), Centre de Recherche Jean-Pierre AUBERT Neurosciences et Cancer - U1172 Inserm - U837 (JPArc), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Lille Nord de France (COMUE)-Université de Lille, Institut de Chimie Organique Fine (IRCOF), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherche Jean-Pierre AUBERT Neurosciences et Cancer - U837 (JPArc), and Université Lille Nord de France (COMUE)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille

Subjects
Central Nervous System, Receptors, Neuropeptide, Amphibian, Ranidae, Physiology, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Central nervous system, Hypothalamus, Neuropeptide, Peptide, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, MESH: Neuropeptides, Biochemistry, 03 medical and health sciences, Cellular and Molecular Neuroscience, 0302 clinical medicine, Endocrinology, biology.animal, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], medicine, Animals, Humans, MESH: Central Nervous System, MESH: Animals, Receptor, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, MESH: Humans, biology, MESH: Ranidae, MESH: Receptors, Neuropeptide, Neuropeptides, Protein primary structure, Vertebrate, MESH: Hypothalamus, Cell biology, medicine.anatomical_structure, chemistry, MESH: Oligopeptides, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Oligopeptides, Neuroscience, 030217 neurology & neurosurgery
Abstract

International audience; A number of RFamide peptides have been characterized in invertebrate species and these peptides have been found to exert a broad spectrum of biological activities. In contrast, in vertebrates, our knowledge on RFamide peptides is far more limited and only a few members of the RFamide peptide family have been identified in various vertebrate classes during the last years. The present review focuses on two novel RFamide peptides, Rana RFamide (R-RFa) and 26RFa, that have been recently isolated from the amphibian brain. R-RFa shares the C-terminal LPLRFamide motif with other RFamide peptides previously identified in mammals, birds and fish. The distribution of R-RFa in the frog brain exhibits strong similarities with those of other LPLRFamide peptides, notably in the periventricular region of the hypothalamus. There is also evidence that the physiological functions of R-RFa and other LPLRFamide peptides have been conserved from fish to mammals; in particular, all these peptides appear to be involved in the control of pituitary hormone secretion. 26RFa does not exhibit any significant structural identity with other RFamide peptides and this peptide is the only member of the family that possesses an FRFamide motif at its C-terminus. The strong conservation of the primary structure of 26RFa from amphibians to mammals suggests that this RFamide peptide is involved in important biological functions in vertebrates. As for several other RFamide peptides, 26RFa-containing neurons are present in the hypothalamus, notably in two nuclei involved in the control of feeding behavior. Indeed, 26RFa is a potent stimulator of appetite in mammals. Concurrently, recent data suggest that 26RFa exerts various neuroendocrine regulatory activities at the pituitary and adrenal level.

Published
2006

24. Evidence from peptidomic analysis of skin secretions that the red-legged frogs, Rana aurora draytonii and Rana aurora aurora, are distinct species

Author

Conlon, J Michael, Al-Ghafari, Nadia, Coquet, Laurent, Leprince, Jérôme, Jouenne, Thierry, Vaudry, Hubert, Davidson, Carlos, Conlon, J. Michael, Faculty of Medicine and Health Science, UAE University, Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Différenciation et communication neuronale et neuroendocrine (DC2N)

Subjects
0106 biological sciences, Male, Proteomics, Time Factors, Ranidae, MESH: Sequence Homology, Amino Acid, Physiology, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, 01 natural sciences, Biochemistry, Endocrinology, Salientia, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], MESH: Animals, MESH: Phylogeny, Chromatography, High Pressure Liquid, Phylogeny, Antibacterial agent, Skin, 0303 health sciences, MESH: Ranidae, biology, MESH: Peptides, Ecology, MESH: Proteomics, MESH: Antimicrobial Cationic Peptides, Rana boylii, embryonic structures, Female, biological phenomena, cell phenomena, and immunity, Antimicrobial peptides, Molecular Sequence Data, Zoology, 010603 evolutionary biology, 03 medical and health sciences, Cellular and Molecular Neuroscience, Rana muscosa, MESH: Skin, Species Specificity, MESH: Species Specificity, Animals, Amino Acid Sequence, MESH: Chromatography, High Pressure Liquid, Rana luteiventris, 030304 developmental biology, MESH: Molecular Sequence Data, Sequence Homology, Amino Acid, MESH: Time Factors, Rana aurora, biology.organism_classification, MESH: Male, Temporin, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Peptides, MESH: Female, Antimicrobial Cationic Peptides
Abstract

International audience; The northern red-legged frog Rana aurora aurora and the California red-legged frog Rana aurora draytonii are traditionally classified together in the same species group. Ten peptides with antimicrobial activity were isolated from norepinephrine-stimulated skin secretions of R. aurora draytonii and purified to near homogeneity. The peptides were identified as belonging to the ranatuerin-2 family (two peptides), brevinin-1 family (four peptides), temporin family (three peptides), and a novel peptide, RV-23 (RIGVLLARLPKLFSLFKLMGKKV) that has limited structural similarity to the bee venom peptide, melittin. This distribution of peptides contrasts with that found previously in skin secretions from R. aurora aurora collected under the same conditions and at the same time of year (one ranatuerin-2 peptide, two brevinin-1 peptides, and one temporin peptide). The variation in amino acid sequences between corresponding R. aurora draytonii and R. aurora aurora peptides is comparable with the variation in sequences of orthologs from other members of the Amerana group of New World ranid frogs (Rana boylii, Rana muscosa, and Rana luteiventris). It is proposed, therefore, that the red-legged frogs should be regarded as separate species (R. aurora and R. draytonii) within the Amerana group rather than conspecific subspecies. The data emphasize that amino acid sequences of antimicrobial peptides in skin secretions may be used to infer taxonomic and phylogenetic relationships between species of ranid frogs.

Published
2005

25. Purification and characterization of antimicrobial peptides from the skin secretions of the carpenter frog Rana virgatipes (Ranidae, Aquarana)

Author

Conlon, J Michael, Abraham, Bency, Sonnevend, Agnes, Jouenne, Thierry, Cosette, Pascal, Leprince, Jérôme, Vaudry, Hubert, Bevier, Catherine, Conlon, J. Michael, Faculty of Medicine and Health Science, UAE University, Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Différenciation et communication neuronale et neuroendocrine (DC2N)

Subjects
Male, Bodily Secretions, Ranidae, Physiology, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Clinical Biochemistry, Antimicrobial peptides, Molecular Sequence Data, MESH: Sequence Alignment, MESH: Amino Acid Sequence, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Biochemistry, Microbiology, 03 medical and health sciences, Cellular and Molecular Neuroscience, MESH: Bodily Secretions, Endocrinology, MESH: Skin, Salientia, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], Animals, MESH: Animals, Amino Acid Sequence, Peptide sequence, Pathogen, 030304 developmental biology, Antibacterial agent, Skin, 0303 health sciences, MESH: Molecular Sequence Data, biology, MESH: Ranidae, 030302 biochemistry & molecular biology, MESH: Antimicrobial Cationic Peptides, biology.organism_classification, Temporin, MESH: Male, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Frog Skin, Sequence Alignment, Bacteria, Antimicrobial Cationic Peptides
Abstract

International audience; The members of the Aquarana (or Rana catesbeiana species group) form a well-supported monophyletic clade but phylogenetic relationships between species within the group are incompletely understood. Peptides that differentially inhibited the growth of bacteria were purified from electrically stimulated skin secretions of the carpenter frog Rana virgatipes. Structural characterization identified members of the ranatuerin-2 (3 peptides) and temporin (3-peptides) families, previously found in the skins of R. catesbeiana, R. clamitans, R. grylio and R. septentrionalis. Ranalexin, a peptide previously found only in the Aquarana, was isolated together with a variant (FFGLHNLVPSMLCVVRKKC) that lacks the propensity to adopt an alpha-helical conformation and so was devoid of antimicrobial activity. Two C-terminally alpha-amidated peptides belonging to the brevinin-2 family were isolated from the skin secretions that, like an ortholog from R. septentrionalis, lacked the C-terminal cyclic heptapeptide domain associated with members of this family. Ranatuerin-1, previously isolated from R. catesbeiana, R. clamitans and R. grylio but absent from R. septentrionalis, was also not identified in R. virgatipes. Synthetic replicates of temporin-1Va (FLSSIGKILGNLL.NH2), temporin-IVb (FLSIIAKVLGSLF.NH2) and temporin-1Vc (FLPLVTMLLGKLF.NH2) potently inhibited growth of Gram-positive bacteria (including methicillin-resistant Staphylococcus aureus). Temporin-1Va was also active against Gram-negative bacteria and the opportunistic yeast pathogen Candida albicans and had relatively weak hemolytic activity (LD50=120 microM) and may therefore represent a candidate for drug development. Our data support the placement of R. virgatipes in the Aquarana and indicate a closer phylogenetic relationship of R. virgatipes with R. septentrionalis than with R. catesbeiana, R. clamitans and R. grylio.

Published
2005

26. Second-harmonic microscopy of unstained living cardiac myocytes: measurements of sarcomere length with 20-nm accuracy

Author

Thierry Boulesteix, Marie-Claire Schanne-Klein, Martin-Pierre Sauviat, Emmanuel Beaurepaire, Laboratoire d'optique et biosciences (LOB), and École polytechnique (X)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Ranidae, MESH: Myocardial Contraction, [SDV.IB.IMA]Life Sciences [q-bio]/Bioengineering/Imaging, MESH: Myocytes, Cardiac, 01 natural sciences, Sarcomere, Myosin head, Myosin, Microscopy, Myocyte, Nanotechnology, MESH: Microscopy, Confocal, Myocytes, Cardiac, MESH: Animals, MESH: Nanotechnology, Cells, Cultured, 0303 health sciences, [PHYS.PHYS.PHYS-OPTICS]Physics [physics]/Physics [physics]/Optics [physics.optics], Microscopy, Confocal, MESH: Ranidae, MESH: Sarcomeres, Atrial Function, MESH: Atrial Function, Atomic and Molecular Physics, and Optics, MESH: Reproducibility of Results, medicine.anatomical_structure, medicine.symptom, MESH: Image Enhancement, MESH: Cells, Cultured, Muscle tissue, Sarcomeres, Materials science, Sensitivity and Specificity, 010309 optics, 03 medical and health sciences, Optics, 0103 physical sciences, medicine, Animals, Heart Atria, 030304 developmental biology, business.industry, Reproducibility of Results, Image Enhancement, Myocardial Contraction, MESH: Sensitivity and Specificity, Microscopy, Fluorescence, Multiphoton, MESH: Microscopy, Fluorescence, Multiphoton, Near-field scanning optical microscope, MESH: Heart Atria, Contracture, business, Saxitoxin, MESH: Saxitoxin
Abstract

International audience; We extend second-harmonic generation (SHG) microscopy to the measurement of sarcomere length in unstained living cardiac myocytes with 20-nm accuracy. We quantify individual sarcomere shortening in the presence of saxitoxin and find that it is in agreement with mechanical measurements of atrial tissue contracture. This functional application of SHG microscopy is generally applicable to quantify the physiological effects of drugs on contractile tissue. Our data also suggest that packed myosin heads in sarcomere thick filaments are responsible for the large second-harmonic endogenous signal in muscle tissue.

Published
2004

27. The Hippocampal Cholinergic Neurostimulating Peptide, the N-terminal Fragment of the Secreted Phosphatidylethanolamine-binding Protein, Possesses a New Biological Activity on Cardiac Physiology

Author

Tommaso Angelone, Sylvette Chasserot-Golaz, Dominique Aunis, Ingeborg Welters, Bjørg Almås, Françoise Schoentgen, Keith Langley, Bruno Tota, Miriam M. Fukami, Yannick Goumon, Marie-Hélène Metz-Boutigue, Physiopathologie du système nerveux., Université Louis Pasteur - Strasbourg I-IFR37-Institut National de la Santé et de la Recherche Médicale (INSERM), IFR de neurosciences de Strasbourg (INS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Università della Calabria [Arcavacata di Rende] (Unical), Centre de biophysique moléculaire (CBM), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Neurotransmission et sécrétion neuroendocrine (NSN), Centre National de la Recherche Scientifique (CNRS), University of Bergen (UiB), Justus-Liebig-Universität Gießen = Justus Liebig University (JLU), Goumon, Yannick, and Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)

Subjects
Cytoplasm, Time Factors, Ranidae, Chromaffin Cells, [SDV]Life Sciences [q-bio], MESH: Neuropeptides, Biochemistry, Mass Spectrometry, MESH: Protein Structure, Tertiary, 0302 clinical medicine, Protein structure, MESH: Microscopy, Immunoelectron, MESH: Chromaffin Cells, MESH: Microscopy, Confocal, MESH: Animals, Phospholipid Transfer Proteins, Microscopy, Immunoelectron, Lipid raft, Chromatography, High Pressure Liquid, MESH: Blood Platelets, 0303 health sciences, Microscopy, Confocal, MESH: Ranidae, Kinase, MESH: Peptides, MESH: Phospholipid Transfer Proteins, Heart, Inhibitor protein, Immunohistochemistry, Lipids, 3. Good health, [SDV] Life Sciences [q-bio], MESH: Cattle, medicine.anatomical_structure, Subcellular Fractions, Blood Platelets, Signal peptide, MESH: Myocardium, Blotting, Western, MESH: Carrier Proteins, Biology, Androgen-Binding Protein, 03 medical and health sciences, medicine, Animals, MESH: Blotting, Western, Secretion, MESH: Chromatography, High Pressure Liquid, Molecular Biology, 030304 developmental biology, MESH: Mass Spectrometry, Myocardium, MESH: Cytoplasm, Neuropeptides, MESH: Time Factors, MESH: Immunohistochemistry, Cell Biology, MESH: Lipids, MESH: Androgen-Binding Protein, Protein Structure, Tertiary, MESH: Heart, Phosphatidylethanolamine Binding Protein, MESH: Subcellular Fractions, Chromaffin cell, Cattle, Carrier Proteins, Peptides, MESH: Chromatography, Liquid, 030217 neurology & neurosurgery, Chromatography, Liquid
Abstract

International audience; Phosphatidylethanolamine-binding protein (PEBP), alternatively named Raf-1 kinase inhibitor protein, is the precursor of the hippocampal cholinergic neurostimulating peptide (HCNP) corresponding to its natural N-terminal fragment, previously described to be released by hippocampal neurons. PEBP is a soluble cytoplasmic protein, also associated with plasma and reticulum membranes of numerous cell types. In the present report, using biochemistry and cell biology techniques, we report for the first time the presence of PEBP in bovine chromaffin cell, a well described secretion model. We have examined its presence at the subcellular level and characterized this protein on both secretory granule membranes and intragranular matrix. In addition, its presence in bovine chromaffin cell and platelet exocytotic medium, as well as in serum, was reported showing that it is secreted. Like many other proteins that lack signal sequence, PEBP may be secreted through non-classic signal secretory mechanisms, which could be due to interactions with granule membrane lipids and lipid rafts. By two-dimensional liquid chromatography-tandem mass spectrometry, HCNP was detected among the intragranular matrix components. The observation that PEBP and HCNP were secreted with catecholamines into the circulation prompted us to investigate endocrine effects of this peptide on cardiovascular system. By using as bioassay an isolated and perfused frog (Rana esculenta) heart preparation, we show here that HCNP acts on the cardiac mechanical performance exerting a negative inotropism and counteracting the adrenergic stimulation of isoproterenol. All together, these data suggest that PEBP and HCNP might be considered as new endocrine factors involved in cardiac physiology.

Published
2004

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