Peptidomic analysis of the neurolysin-knockout mouse brain

Show simple item record Castro, Leandro M. [UNIFESP] Cavalcanti, Diogo M. L. P. Araujo, Christiane B. Rioli, Vanessa Icimoto, Marcelo Y. [UNIFESP] Gozzo, Fabio C. Juliano, Maria [UNIFESP] Juliano, Luiz [UNIFESP] Oliveira, Vitor [UNIFESP] Ferro, Emer S. 2016-01-24T14:38:18Z 2016-01-24T14:38:18Z 2014-12-05
dc.identifier.citation Journal of Proteomics. Amsterdam: Elsevier B.V., v. 111, p. 238-248, 2014.
dc.identifier.issn 1874-3919
dc.description.abstract A large number of intracellular peptides are constantly produced following protein degradation by the proteasome. A few of these peptides function in cell signaling and regulate protein protein interactions. Neurolysin (Nln) is a structurally defined and biochemically well-characterized endooligopeptidase, and its subcellular distribution and biological activity in the vertebrate brain have been previously investigated. However, the contribution of Nln to peptide metabolism in vivo is poorly understood. in this study, we used quantitative mass spectrometry to investigate the brain peptidome of Nln-knockout mice. An additional in vitro digestion assay with recombinant Nln was also performed to confirm the identification of the substrates and/or products of Nln. Altogether, the data presented suggest that Nln is a key enzyme in the in vivo degradation of only a few peptides derived from proenkephalin, such as Met-enkephalin and octapeptide. Nln was found to have only a minor contribution to the intracellular peptide metabolism in the entire mouse brain. However, further studies appear necessary to investigate the contribution of Nln to the peptide metabolism in specific areas of the murine brain.Biological significanceNeurolysin was first identified in the synaptic membranes of the rat brain in the middle 80's by Frederic Cheder and colleagues. Neurolysin was well characterized biochemically, and its brain distribution has been confirmed by immunohistochemical methods. the neurolysin contribution to the central and peripheral neurotensin-mediated functions in vivo has been delineated through inhibitor-based pharmacological approaches, but its genuine contribution to the physiological inactivation of neuropeptides remains to be firmly established. As a result, the main significance of this work is the first characterization of the brain peptidome of the neurolysin-knockout mouse. (C) 2014 Published by Elsevier B.V. en
dc.description.sponsorship Pro-Reitoria de Pesquisa, University of São Paulo through the Support Center for Research in Proteolysis and Cell Signaling (NAPPS)
dc.description.sponsorship Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorship Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.format.extent 238-248
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof Journal of Proteomics
dc.rights Acesso restrito
dc.subject Intracellular peptides en
dc.subject Neurolysin en
dc.subject Hemopressin en
dc.subject Peptide metabolism en
dc.subject Endopeptidase en
dc.subject Oligopeptidase en
dc.title Peptidomic analysis of the neurolysin-knockout mouse brain en
dc.type Artigo
dc.contributor.institution Universidade de São Paulo (USP)
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.contributor.institution LETA CETICS
dc.contributor.institution Universidade Estadual de Campinas (UNICAMP)
dc.description.affiliation Univ São Paulo, Support Ctr Res Proteolysis & Cell Signaling NAPP, Dept Pharmacol, BR-05508000 São Paulo, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Dept Biophys, BR-04039032 São Paulo, Brazil
dc.description.affiliation LETA CETICS, Butantan Inst, BR-05503900 São Paulo, Brazil
dc.description.affiliation Univ Estadual Campinas, Inst Chem, BR-13083970 Campinas, SP, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Dept Biophys, BR-04039032 São Paulo, Brazil
dc.description.sponsorshipID Pro-Reitoria de Pesquisa, University of São Paulo through the Support Center for Research in Proteolysis and Cell Signaling (NAPPS): 2012.1.17607.1.2
dc.description.sponsorshipID CNPq: 559698/2009-7
dc.description.sponsorshipID FAPESP: 04/04933-2
dc.identifier.doi 10.1016/j.jprot.2014.03.043
dc.description.source Web of Science
dc.identifier.wos WOS:000345949300019


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