Please use this identifier to cite or link to this item: http://repositorio.unifesp.br/handle/11600/26035
Title: Thimet oligopeptidase and the stability of MHC class I epitopes in macrophage cytosol
Authors: Portaro, FCV
Gomes, M. D.
Cabrera, A.
Fernandes, B. L.
Silva, C. L.
Ferro, E. S.
Juliano, L.
Camargo, ACM de
Inst Butantan
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Keywords: cytosolic oligopeptidases
MHC class I epitopes
thimet oligopeptidase
Issue Date: 24-Feb-1999
Publisher: Academic Press Inc
Citation: Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc, v. 255, n. 3, p. 596-601, 1999.
Abstract: In this study we investigated the fate of a class of proteasome-generated oligopeptides, exposing them to the crude cytosol of macrophages or to the purified recombinant thimet oligopeptidase. Among the proteasome products of known sequences are MHC class I epitopes, 13 of which were randomly chosen to be used as putative substrates. Surprisingly, our results clearly showed that the majority of the peptides were poorly or not degraded, either by the purified enzyme or by the crude macrophage cytosol. the peptides, which were resistant to hydrolysis, displayed high affinity for the thimet oligopeptidase as competitive inhibitors. Regardless of the fact that our data do not allow prediction of whether or not a specific peptide would be degraded, it seems very likely that the structural features, which rule out the stability of the MAC class I peptides in the cytosol, may have implications in an optimized repertoire selection for antigen presentation. (C) 1999 Academic Press.
URI: http://repositorio.unifesp.br/handle/11600/26035
ISSN: 0006-291X
Other Identifiers: http://dx.doi.org/10.1006/bbrc.1999.0251
Appears in Collections:Em verificação - Geral

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