Peptidomic Analysis of Human Cell Lines

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dc.contributor.authorGelman, Julia S.
dc.contributor.authorSironi, Juan
dc.contributor.authorCastro, Leandro M. [UNIFESP]
dc.contributor.authorFerro, Emer S.
dc.contributor.authorFricker, Lloyd D.
dc.contributor.institutionAlbert Einstein Coll Med
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T14:06:23Z
dc.date.available2016-01-24T14:06:23Z
dc.date.issued2011-04-01
dc.description.abstractPeptides have been proposed to function in intracellular signaling within the cytosol. Although cytosolic peptides are considered to be highly unstable, a large number of peptides have been detected in mouse brain and other biological samples. in the present study, we evaluated the peptidome of three diverse cell lines: SH-SY5Y, MCF7, and HEIC293 cells. A comparison of the peptidomes revealed considerable overlap in the identity of the peptides found in each cell line. the majority of the observed peptides are not derived from the most abundant or least stable proteins in the cell, and approximately half of the cellular peptides correspond to the N- or C- termini of the precursor proteins. Cleavage site analysis revealed a preference for hydrophobic residues in the PI position. Quantitative peptidomic analysis indicated that the levels of most cellular peptides are not altered in response to elevated intracellular calcium, suggesting that calpain is not responsible for their production. the similarity of the peptidomes of the three cell lines and the lack of correlation with the predicted cellular degradome implies the selective formation or retention of these peptides, consistent with the hypothesis that they are functional in the cells.en
dc.description.affiliationAlbert Einstein Coll Med, Dept Mol Pharmacol, Bronx, NY 10461 USA
dc.description.affiliationAlbert Einstein Coll Med, Dept Neurosci, Bronx, NY 10461 USA
dc.description.affiliationUniv São Paulo, Dept Cell Biol & Dev, Inst Biomed Sci, BR-05508900 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biochem, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biochem, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipNational Institutes of Health
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipFinanciadora de Estudos e Projetos (FINEP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipIDNational Institutes of Health: DA-04494
dc.description.sponsorshipIDFAPESP: 04/14846
dc.description.sponsorshipIDFinanciadora de Estudos e Projetos (FINEP): A-03/134
dc.description.sponsorshipIDCNPq: 559698/2009-7
dc.format.extent1583-1592
dc.identifierhttp://dx.doi.org/10.1021/pr100952f
dc.identifier.citationJournal of Proteome Research. Washington: Amer Chemical Soc, v. 10, n. 4, p. 1583-1592, 2011.
dc.identifier.doi10.1021/pr100952f
dc.identifier.issn1535-3893
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/33611
dc.identifier.wosWOS:000288924000014
dc.language.isoeng
dc.publisherAmer Chemical Soc
dc.relation.ispartofJournal of Proteome Research
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectpeptidesen
dc.subjectpeptidomicsen
dc.subjecthemopressinen
dc.subjectHEK293en
dc.subjectSH-SY5Yen
dc.subjectMCF7en
dc.titlePeptidomic Analysis of Human Cell Linesen
dc.typeinfo:eu-repo/semantics/article
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