Peptidomic Analysis of HEK293T Cells: Effect of the Proteasome Inhibitor Epoxomicin on Intracellular Peptides

dc.creatorFricker, Lloyd D.
dc.creatorGelman, Julia S.
dc.creatorCastro, Leandro M.
dc.creatorGozzo, Fabio C.
dc.creatorFerro, Emer S.
dc.date2012
dc.date2013-09-19T18:06:10Z
dc.date2016-07-01T12:54:28Z
dc.date2013-09-19T18:06:10Z
dc.date2016-07-01T12:54:28Z
dc.date.accessioned2018-03-29T01:53:48Z
dc.date.available2018-03-29T01:53:48Z
dc.identifierJournal of Proteome Research. Amer Chemical Soc, v.11, n.3, p.1981-1990, 2012
dc.identifier1535-3893
dc.identifierWOS:000300916200050
dc.identifier10.1021/pr2012076
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/1944
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/1944
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1308485
dc.descriptionPeptides derived from cytosolic, mitochondrial, and nuclear proteins have been detected in extracts of animal tissues and cell lines. To test whether the proteasome is involved in their formation, HEK293T cells were treated with epoxomicin (0.2 or 2 mu M) for 1 h and quantitative peptidomics analysis was performed. Altogether, 147 unique peptides were identified by mass spectrometry sequence analysis. Epoxomicin treatment decreased the levels of the majority of intracellular peptides, consistent with inhibition of the proteasome beta-2 and beta-5 subunits. Treatment with the higher concentration of epoxomicin elevated the levels of some peptides. Most of the elevated peptides resulted from cleavages at acidic residues, suggesting that epoxomicin increased the processing of proteins through the beta-1 subunit. Interestingly, some of the peptides that were elevated by the epoxomicin treatment had hydrophobic residues in P1 cleavage sites. Taken together, these findings suggest that, while the proteasome is the major source of intracellular peptides, other peptide-generating mechanisms exist. Because intracellular peptides are likely to perform intracellular functions, studies using proteasome inhibitors need to be interpreted with caution, as it is possible that the effects of these inhibitors are due to a change in the peptide levels rather than inhibition of protein degradation.
dc.description11
dc.description3
dc.description1981
dc.description1990
dc.descriptionNational Institutes of Health [DA-004494]
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionUniversidade de São Paulo (USP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.languageeng
dc.publisherAmer Chemical Soc
dc.publisherWashington
dc.relationJournal of Proteome Research
dc.rightsfechado
dc.sourceWOS
dc.subjectpeptides
dc.subjectproteasome
dc.subjectprotease
dc.subjectpeptidase
dc.subjectMHC CLASS-I
dc.subjectMASS-SPECTROMETRY
dc.subjectQUANTITATIVE PEPTIDOMICS
dc.subjectTHIMET OLIGOPEPTIDASE
dc.subjectANTIGEN PRESENTATION
dc.subjectSUBSTRATE-SPECIFICITY
dc.subjectPROTEIN INTERACTIONS
dc.subjectNATURAL REGULATORS
dc.subjectMOUSE-BRAIN
dc.subjectDEGRADATION
dc.titlePeptidomic Analysis of HEK293T Cells: Effect of the Proteasome Inhibitor Epoxomicin on Intracellular Peptides
dc.typeArtículos de revistas


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