Search Results - (Author, Cooperation:J. P. Vincent)
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1Latest Papers from Table of Contents or Articles in PressStaff View
Publication Date: 2014-01-07Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Alleles ; Animals ; *Body Patterning/genetics ; Cell Membrane/*metabolism ; Cell Proliferation ; Chemokine CX3CL1/metabolism ; Diffusion ; Drosophila Proteins/deficiency/genetics/*metabolism ; Drosophila melanogaster/cytology/genetics/*growth & development/*metabolism ; Gene Expression Regulation, Developmental ; Mutation ; Organ Specificity ; Promoter Regions, Genetic/genetics ; Signal Transduction ; Time Factors ; Transcription, Genetic ; Wings, Animal/cytology/growth & development/metabolism ; Wnt1 Protein/deficiency/genetics/*metabolismPublished by: -
2Latest Papers from Table of Contents or Articles in PressS. Kakugawa ; P. F. Langton ; M. Zebisch ; S. A. Howell ; T. H. Chang ; Y. Liu ; T. Feizi ; G. Bineva ; N. O'Reilly ; A. P. Snijders ; E. Y. Jones ; J. P. Vincent
Nature Publishing Group (NPG)
Published 2015Staff ViewPublication Date: 2015-03-04Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Acylation ; Animals ; Binding Sites ; Carboxylesterase/chemistry/*metabolism ; Drosophila Proteins/chemistry/*metabolism ; Esterases/chemistry/genetics/*metabolism ; Fatty Acids, Monounsaturated/metabolism ; Glycosylphosphatidylinositols/metabolism ; Glypicans/metabolism ; Humans ; Kinetics ; Ligands ; Mass Spectrometry ; Models, Molecular ; Protein Binding ; Wnt Proteins/*chemistry/*metabolism ; *Wnt Signaling PathwayPublished by: -
3Articles: DFG German National LicensesChecler, Frédéric ; Vincent, J. P. ; Kitabgi, P.
Oxford, UK : Blackwell Publishing Ltd
Published 1985Staff ViewISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract: One of the primary inactivating cleavages of neurotensin (NT) by rat brain synaptic membranes occurs at the Arg8-Arg9 peptide bond, leading to the formation of NT1-8 and NT9-13. The involvement at this site of a recently purified metalloendopeptidase was demonstrated by the use of its specific inhibitor, N-[1(R,S)-carboxy-2-phenylethyl]-alanylalanylphenylalanine-p-aminobenzoate, which exerts an inhibition on NT1-8 formation with an IC50 (0.6 μM) close to its Ki for the purified metalloendopeptidase (1.94 μM). Furthermore, we established the role of a postproline dipeptidyl-aminopeptidase in the secondary processing of NT9-13 formation.Type of Medium: Electronic ResourceURL: -
4Articles: DFG German National LicensesChecler, F. ; Grassi, J. ; Masson, P. ; Vincent, J. P.
Oxford, UK : Blackwell Publishing Ltd
Published 1990Staff ViewISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract: Commercially available and affinity-purified bu-tyrylcholinesterases isolated from human serum were examined for their esterasic activity and their ability to hydrolyze various neuropeptides, including neurotensin, substance P, and leucine-enkephalin. The three pools that displayed the lowest esterasic activities were shown to hydrolyze neurotensin with the same HPLC degradative pattern. By contrast, noticeable qualitative and quantitative discrepancies were observed when hydrolyses of substance P and leucineenkephalin by these three butyrylcholinesterase pools were studied. The pool that exhibited the highest esterasic activity appeared to be homogeneously constituted by 90- and 180-kDa protein bands by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis and was totally unable to hydrolyze these three neuropeptides. This suggested that the three other butyrylcholinesterase preparations could be contaminated by exogenous peptidases. This was confirmed by means of three distinct monoclonal antibodies directed toward human serum butyrylcholinesterase. The three IgG-purified fractions precipitated the esterasic activity, whereas they failed to precipitate the neuropeptide-hydrolyzing activities whatever the substrate examined. Altogether, these results demonstrate that peptidases associated with butyrylcholinesterase are contaminating enzymes that cannot be considered as intrinsic activities of this enzyme.Type of Medium: Electronic ResourceURL: -
5Articles: DFG German National LicensesDauch, P. ; Masuo, Y. ; Vincent, J. P. ; Checler, F.
Oxford, UK : Blackwell Publishing Ltd
Published 1992Staff ViewISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract: The tissue distribution, cerebral regionalization, and ontogeny of endopeptidase 24–16 were established in murines by means of its quenched fluorimetric substrate, Mcc-Pro-Leu-Gly-Pro-D-Lys-Dnp, and its selective dipep-tide blocker, Prolie. Endopeptidase 24–16 was particularly abundant in the liver and kidney, and the lowest specific activity was detected in the heart. In the brain, a 16-fold difference in specific activity was observed between the poorest and the richest cerebral areas. Endopeptidase 24–16 appeared in high concentrations in the olfactory bulb and tubercule, cingulate cortex, medial striatum, and globus pallidus, and was particularly weak in the CA1, CA2, and CA3 parts of the hippocampal formation and in the cerebellum. Endopeptidase 24–16 content in thirteen thalamic nuclei indicated a rather homogeneous distribution. This homogeneity was not observed in the hypothalamus, where pronounced variations occurred between enriched zones such as suprachiasmatic and arcuate nuclei and relatively poor areas such as periventricular and supraoptic nuclei. Endopeptidase 24–16 appeared to be developmentally regulated in the mouse brain; it was already detected at the fetal stage, increased transiently after birth, then regularly declined until adulthood.Type of Medium: Electronic ResourceURL: -
6Articles: DFG German National LicensesCHABRY, J. ; CHECLER, F. ; VINCENT, J. P. ; MAZELLA, J.
Oxford, UK : Blackwell Publishing Ltd
Published 1992Staff ViewISSN: 1749-6632Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: Natural Sciences in GeneralType of Medium: Electronic ResourceURL: -
7Articles: DFG German National LicensesMAZELLA, J. ; CHABRY, J. ; LEONARD, K. ; KITABGI, P. ; VINCENT, J. P. ; BEAUDET, A.
Oxford, UK : Blackwell Publishing Ltd
Published 1992Staff ViewISSN: 1749-6632Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: Natural Sciences in GeneralType of Medium: Electronic ResourceURL: -
8Articles: DFG German National LicensesChecler, Frédéric ; Emson, P. C. ; Vincent, J. P. ; Kitabgi, P.
Oxford, UK : Blackwell Publishing Ltd
Published 1984Staff ViewISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract: It was shown previously that the tridecapeptide neurotensin is inactivated by rat brain synaptic membranes and that one of the primary inactivating cleavages occurs at the Pro10-Tyr11 peptide bond, leading to the formation of NT1–10 and NT11–13.The present study was designed to investigate the possibility that this cleavage was catalyzed by proline endopeptidase and/or endopeptidase 24.11 (enkephalinase). Purified rat brain synaptic membranes were found to contain a N-benzyloxycarbonyl-Gly-Pro-4-methyl-coumarinyl-7-amide-hydrolyzing activity that was markedly inhibited (93%) by the proline endopeptidase inhibitor N-benzyloxycarbonyl-Pro-Prolinal and partially blocked (25%) by an antiproline endopeptidase antiserum. In contrast, the cleavage of neurotensin at the Pro10-Tyr11 bond by synaptic membranes was not affected by N-benzyloxycarbonyl-Pro-Prolinal and the antiserum. When the conversion of NT1–10 to NT1–8 by angiotensin converting enzyme was blocked by captopril and when the processing of NT11–13 by aminopeptidase(s) was inhibited by bestatin, it was found that thiorphan, a potent endopeptidase 24.11 inhibitor, partially decreased the formation of NT1–10 and NT11–13 by synaptic membranes. In conclusion: (1) proline endopeptidase, although it is present in synaptic membranes, is not involved in the cleavage of neurotensin at the Pro10-Tyr11 bond; (2) endopeptidase 24.11 only partially contributes to this cleavage; (3) there exists in rat brain synaptic membranes a peptidase different from proline endopeptidase and endopeptidase 24.11 that is mainly responsible for inactivating neurotensin by cleaving at the Pro10-Tyr11 bond.Type of Medium: Electronic ResourceURL: -
9Articles: DFG German National LicensesStaff View
ISSN: 0005-2736Keywords: (Canine intestine) ; Neurotensin receptor ; Neurotensin, iodine labeled ; Plasma membrane ; Smooth muscleSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyMedicinePhysicsType of Medium: Electronic ResourceURL: -
10Articles: DFG German National LicensesStaff View
ISSN: 0005-2736Keywords: (Axonal membrane) ; Cardiotoxin ; Freeze fracture ; Lipid vesicle ; Phospholipase A"2Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyMedicinePhysicsType of Medium: Electronic ResourceURL: -
11Articles: DFG German National LicensesStaff View
ISSN: 0014-5793Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyPhysicsType of Medium: Electronic ResourceURL: -
12Articles: DFG German National LicensesStaff View
ISSN: 0014-5793Keywords: (Human colonic HT29 cell) ; Inositol trisphosphate ; Neurotensin receptor ; Phosphatidylinositol turnover ; intracellular Ca^2^+Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyPhysicsType of Medium: Electronic ResourceURL: -
13Articles: DFG German National LicensesBozou, J.-C. ; Couvineau, A. ; Rouyer-Fessard, C. ; Laburthe, M. ; Vincent, J.-P. ; Kitabgi, P.
Amsterdam : ElsevierStaff ViewISSN: 0014-5793Keywords: (Human colonic HT29 cell) ; Adenylate cyclase ; Phorbol ester ; Protein kinase C ; VIP ; VIP receptorSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyPhysicsType of Medium: Electronic ResourceURL: -
14Articles: DFG German National LicensesStaff View
ISSN: 0012-1606Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyType of Medium: Electronic ResourceURL: -
15Articles: DFG German National LicensesStaff View
ISSN: 0012-1606Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyType of Medium: Electronic ResourceURL: -
16Articles: DFG German National LicensesStaff View
ISSN: 0012-1606Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyType of Medium: Electronic ResourceURL: -
17Articles: DFG German National LicensesStaff View
ISSN: 0012-1606Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyType of Medium: Electronic ResourceURL: -
18Articles: DFG German National LicensesStaff View
ISSN: 0006-291XSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyPhysicsType of Medium: Electronic ResourceURL: -
19Articles: DFG German National LicensesStaff View
ISSN: 0006-291XSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyPhysicsType of Medium: Electronic ResourceURL: -
20Articles: DFG German National LicensesSadoul, J.-L. ; Kitabgi, P. ; Rostene, W. ; Javoy-Agid, F. ; Agid, Y. ; Vincent, J.-P.
Amsterdam : ElsevierStaff ViewISSN: 0006-291XSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyPhysicsType of Medium: Electronic ResourceURL: