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22 results on '"Paroutaud P"'

2. Insect immunity: Two proteinase inhibitors from hemolymph of Locusta migratoria

Author

Coletti-Previero Ma, Hélène Mattras, Michel Brehélin, Paroutaud P, R.-A. Boigegrain, Unité mixte de recherche de pathologie comparée, and Centre National de la Recherche Scientifique (CNRS)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Recherche Agronomique (INRA)

Subjects
Cellular immunity, medicine.medical_treatment, Molecular Sequence Data, Biophysics, Grasshoppers, Biology, Biochemistry, Substrate Specificity, 03 medical and health sciences, Endopeptidases, Hemolymph, medicine, Animals, Chymotrypsin, Protease Inhibitors, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, Pacifastin, Arthropods, Molecular Biology, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, chemistry.chemical_classification, Enzyme Precursors, 0303 health sciences, Protease, 030302 biochemistry & molecular biology, Elastase, Cell Biology, Prophenoloxidase, 3. Good health, INSECTE, Enzyme, chemistry, Enzyme inhibitor, biology.protein, Peptides, Catechol Oxidase
Abstract

Two protease inhibitors were isolated from the plasma of Locusta migratoria and sequenced. They were 35 and 36 amino acids long and revealed very little similitude for the protease inhibitors isolated from other arthropods. They inhibit the proPhenoloxidase Phenoloxidase proteolytic activation cascade in hemocyte extracts of the same insect. This inhibiting activity resulted in a lower production of PO, a key enzyme for the defence mechanism in arthopods. Both peptides however showed a strong in vitro inhibiting activity toward α-chymotrypsin and elastase, LMCI I inhibits the human leukocyte enzyme while LMCI II mostly the pancreatic one, a difference explainable on the basis of the active site sequence changes.

Published
1992
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3. Flow cytometry and immunohistochemistry of the mouse dural meninges for immunological and virological assessments

Author

Roussel-Queval, Annie, Rebejac, Julie, Eme-Scolan, Elisa, Paroutaud, Laurie Arnaud, and Rua, Rejane

Abstract

The highly vascularized meninges protect the surface of the central nervous system and contain a dense network of immune cells controlling neuroinfection and neuroinflammation. Here, we present techniques for the immunological and virological assessment of mouse dural meninges. We describe steps for immunophenotyping including meninges extraction and digestion, immunostaining and flow cytometry. We then describe viral assessment upon Lymphocytic Choriomeningitis Virus infection including steps for fixation of the meninges in the skull, whole mount immunohistochemistry and confocal imaging.

Published
2023
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6. Sequence analysis of peptide fragments from the intrinsic membrane protein of calf lens fibers MP26 and its natural maturation product MP22

Author

Ngoc, Lien Do, Paroutaud, Pierre, Dunia, Irene, Benedetti, E.Lucio, and Hoebeke, Johan

Abstract

Calf lens fiber plasma membranes, containing only the intrinsic membrane protein MP26 and its maturation product MP22 were treated with proteolytic enzymes such as trypsin, protease V8 from S. aureusor with chemical agents as CNBr in formic acid. The cleavage products, purified by electrophoresis, were analysed for their amino acid composition and N-terminal sequences. Proteolysis gave rise to peptides which were mainly shortened at the C-terminal end of the molecules. While the V8 protease produced a fragment with a similar N-terminal sequence as the maturation product MP22, trypsin yielded another cleavage product. Chemical hydrolysis yielded large fragments (11–15 kDa) with hydrophobic N-terminal sequences. Our results suggest that MP26 is characterised by an N-terminal signal sequence and possesses other hydrophobic domains which could function as untranslocated insertion sequences.

Published
1985
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19. Proteomics application exercise of the Swiss Proteomics Society: report of the SPS'02 session.

Author

Binz PA, Abdi F, Affolter M, Allard L, Barblan J, Bhardwaj S, Bienvenut WV, Bulet P, Burgess J, Carrette O, Corthals G, Delalande F, Diemer H, Favreau P, Giuliano E, Gueguen Y, Guillaume E, Hahner S, Man P, Michalet S, Neri D, Noukakis D, Palagi P, Paroutaud P, Pimenta DC, Quadroni M, Resemann A, Richert S, Rybak J, Sanchez JC, Scherl A, Scheurer S, Schweiger Hufnagel U, Siethoff C, Suckau D, van Dorsselaer A, Wagner Redeker W, Walter N, and Stöcklin R

Subjects
Mass Spectrometry, Proteomics
Abstract

After the success of the mass spectrometry (MS) round table that was held at the first Swiss Proteomics Society congress (SPS'01) in Geneva, the SPS has organized a proteomics application exercise and allocated a full session at the SPS'02 congress. The main objective was to encourage the exchange of expertise in protein identification, with a focus on the use of mass spectrometry, and to create a bridge between the users' questions and the instrument providers' solutions. Two samples were sent to fifteen interested labs, including academic groups and MS hardware providers. Participants were asked to identify and partially characterize the samples. They consisted of a complex mixture of peptide/proteins (sample A) and an almost pure recombinant peptide carrying post-translational modifications (sample B). Sample A was an extract of snake venom from the species Bothrops jararaca. Sample B was a recombinant and modified peptide derived from the shrimp Penaeus vannamei penaeidin 3a. The eight labs that returned results reported the use of a wide range of MS instrumentation and techniques. They mentioned a variety of time and manpower allocations. The origin of sample A was generally identified together with a number of database protein entries. The difficulty of the sample identification lay in the incomplete knowledge of the Bothrops species genome sequence and is discussed. Sample B was generally and correctly identified as penaeidin. However, only one group reported the full primary structure. Interestingly, the approaches were again varied and are discussed in the text.

Published
2003
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20. Sequence analysis of peptide fragments from the intrinsic membrane protein of calf lens fibers MP26 and its natural maturation product MP22.

Author

Do Ngoc L, Paroutaud P, Dunia I, Benedetti EL, and Hoebeke J

Subjects
Amino Acid Sequence, Animals, Aquaporins, Cattle, Electrophoresis, Polyacrylamide Gel, Endopeptidases metabolism, Trypsin metabolism, Eye Proteins analysis, Membrane Glycoproteins, Membrane Proteins analysis, Metalloendopeptidases, Peptide Fragments analysis
Abstract

Calf lens fiber plasma membranes, containing only the intrinsic membrane protein MP26 and its maturation product MP22 were treated with proteolytic enzymes such as trypsin, protease V8 from S. aureus or with chemical agents as CNBr in formic acid. The cleavage products, purified by electrophoresis, were analysed for their amino acid composition and N-terminal sequences. Proteolysis gave rise to peptides which were mainly shortened at the C-terminal end of the molecules. While the V8 protease produced a fragment with a similar N-terminal sequence as the maturation product MP22, trypsin yielded another cleavage product. Chemical hydrolysis yielded large fragments (11-15 kDa) with hydrophobic N-terminal sequences. Our results suggest that MP26 is characterised by an N-terminal signal sequence and possesses other hydrophobic domains which could function as untranslocated insertion sequences.

Published
1985
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22. Partial amino acid sequence of a rabbit immunoglobulin light chain of allotype b5.

Author

Ayadi H, Dutka S, Paroutaud P, and Strosberg AD

Subjects
Amino Acid Sequence, Animals, Endopeptidases, Immunoglobulin kappa-Chains, Peptide Fragments analysis, Rabbits, Trypsin, Immunoglobulin Allotypes, Immunoglobulin Light Chains, Metalloendopeptidases
Abstract

The amino acid sequence of a rabbit immunoglobulin light chain of allotype b5 has been nearly completed. A comparison of its structure with that of light chains of allotypes b4, b6, and b9 confirms that the constant regions of these various kappa chains differ by 20-35%. The substitutions are clustered in parts of the second half of the chain, and the b5 form bears more resemblance to the b6 chain than to any other, in good agreement with previous serological data. The analysis of the variable region reveals the existence of certain allotype-associated residues which have also been reported in other b5 chains, but not in proteins of the other allotypes. An examination of the rabbit light chain sequences between positions 96 and 107 suggests that this portion of the chain may be encoded separately by a joining "J" DNA segment, as has been described previously for murine and human immunoglobulins. In the rabbit, however, these J kappa regions appear to differ from one allotype to another. Together with the extensive variations of the constant regions, these data suggest that the rabbit kappa gene organization more closely resembles the murine gamma system (four different C gamma genes each flanked by its J segment) than the murine kappa system (a single C kappa gene).

Published
1983
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