Thimet oligopeptidase and the stability of MHC class I epitopes in macrophage cytosol

Thimet oligopeptidase and the stability of MHC class I epitopes in macrophage cytosol

Autor Portaro, FCV Google Scholar
Gomes, M. D. Google Scholar
Cabrera, A. Google Scholar
Fernandes, B. L. Google Scholar
Silva, C. L. Google Scholar
Ferro, E. S. Google Scholar
Juliano, L. Google Scholar
Camargo, ACM de Google Scholar
Instituição Inst Butantan
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Resumo 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.
Palavra-chave cytosolic oligopeptidases
MHC class I epitopes
thimet oligopeptidase
Idioma Inglês
Data de publicação 1999-02-24
Publicado em Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc, v. 255, n. 3, p. 596-601, 1999.
ISSN 0006-291X (Sherpa/Romeo, fator de impacto)
Publicador Academic Press Inc
Extensão 596-601
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000078970800009
Endereço permanente

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