1. Anaerobic sulfatase-maturating enzymes: radical SAM enzymes able to catalyze in vitro sulfatase post-translational modification
- Author
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Bucharles, Christine, Bizet, Patrice, Arthaud, Sébastien, Arabo, Arnaud, Leprince, Jérôme, Lefranc, Benjamin, Cartier, Dorthe, Anouar, Youssef, Lihrmann, Isabelle, 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), Plate-Forme de Recherche en Imagerie Cellulaire de Haute-Normandie (PRIMACEN), Normandie Université (NU)-Normandie Université (NU)-Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Psychologie et Neurosciences de la Cognition et de l'affectivité (PSY-NCA), Normandie Université (NU)-Normandie Université (NU), and Différenciation et communication neuronale et neuroendocrine (DC2N)
- Subjects
Male ,MESH: Signal Transduction ,PPARγ ,Peptide Hormones ,[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: Protein Isoforms ,MESH: Thapsigargin ,autoradiography ,Iodine Radioisotopes ,MESH: Spinal Cord ,antimicrobial peptides ,MESH: Protein Structure, Tertiary ,MESH: Autoradiography ,Candida albicans ,[SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB] ,MESH: Glial Fibrillary Acidic Protein ,MESH: Animals ,c-Fos ,MESH: Proto-Oncogene Proteins c-fos ,MESH: Iodine Radioisotopes ,UT receptor ,MESH: Fourth Ventricle ,dextran ,immunohistochemistry ,Proto-Oncogene Proteins c-fos ,MESH: Ventromedial Hypothalamic Nucleus ,MESH: Rats ,Urotensins ,brain ,CSF ,MESH: Radioimmunoassay ,MESH: Brain ,inflammasome ,Glial Fibrillary Acidic Protein ,host defense peptide ,Animals ,Vimentin ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Rats, Wistar ,ventricular system ,Fourth Ventricle ,Binding Sites ,MESH: Urotensins ,Macrophages ,neuropeptides ,MESH: Immunohistochemistry ,MESH: Rats, Wistar ,MESH: Male ,arachidonic acid metabolism ,MESH: Binding Sites ,drug delivery ,[SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology ,MESH: Peptide Hormones ,nanoparticles ,MESH: Vimentin ,C-type lectin receptors - Abstract
International audience; Urotensin II (UII) and Urotensin II-related peptide (URP) are structurally related paralog peptides that exert peripheral and central effects. UII binding sites have been partly described in brain, and those of URP have never been reported. We exhaustively compared [(125)I]-UII and -URP binding site distributions in the adult rat brain, and found that they fully overlapped at the regional level. We observed UII/URP binding sites in structures lining ventricles, comprising the sphenoid nucleus and cell rafts scattered on a line joining the fourth ventricle and its lateral recess. After injection of UII and URP in the lateral ventricle, we observed c-Fos-positive cell nuclei in areas close to the fourth ventricle, indicating that these receptors are functional. Different c-Fos-containing cell populations were activated. They were all positive for vimentin and glial fibrillary acidic protein (GFAP), excluding the possibility of an ependymal nature. In conclusion, this study demonstrated that UII and URP binding sites are totally overlapping and that these sites were functional in regions bordering the fourth ventricle. These data support a role for UII/URP at the interface between brain parenchyma and cerebrospinal fluid.; Octylglyceryl dextran-graft-poly(lactic acid) nanoparticles formulated by emulsification demonstrate potential for peptide delivery.
- Published
- 2014
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