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Titolo:
Interferon-gamma inducible exchanges of 20S proteasome active site subunits: Why?
Autore:
Groettrup, M; Khan, S; Schwarz, K; Schmidtke, G;
Indirizzi:
Canton Hosp St Gall, Res Dept, CH-9007 St Gallen, Switzerland Canton Hosp St Gall St Gallen Switzerland CH-9007 St Gallen, Switzerland
Titolo Testata:
BIOCHIMIE
fascicolo: 3-4, volume: 83, anno: 2001,
pagine: 367 - 372
SICI:
0300-9084(200103/04)83:3-4<367:IIEO2P>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
MAJOR HISTOCOMPATIBILITY COMPLEX; I ANTIGEN PRESENTATION; PEPTIDASE ACTIVITIES; DENDRITIC CELLS; BETA-SUBUNITS; CTL EPITOPE; MECL-1; PROTEIN; YEAST; LMP2;
Keywords:
proteasome; interferon-gamma; antigen presentation; MHC class I;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Groettrup, M Canton Hosp St Gall, Res Dept, CH-9007 St Gallen, SwitzerlandCanton Hosp St Gall St Gallen Switzerland CH-9007 itzerland
Citazione:
M. Groettrup et al., "Interferon-gamma inducible exchanges of 20S proteasome active site subunits: Why?", BIOCHIMIE, 83(3-4), 2001, pp. 367-372

Abstract

When cells are stimulated with the cytokines IFN-gamma or TNF-alpha, the synthesis of three proteasome subunits LMP2 (beta 1i), LMP7 (beta 5i), and MECL-1 (beta 2i) is induced. These subunits replace the three subunits delta(beta1), MB1 (beta5), and Z (beta2), which bear the catalytically active sites of the proteasome, during proteasome neosynthesis. The cytokine-induced exchanges of three active site subunits of a complex protease is unprecedented in biology and one may expect a strong functional driving force for this system to evolve. These cytokine-induced replacements of proteasome subunits are believed to favour the production of peptide ligands of major histocompatibility complex (MHC) class I molecules for the stimulation of cytotoxic T cells. Although the peptide production by constitutive proteasomes is able to maintain peptide-dependent MHC class I cell surface expression in the absence of LMP2 and LMP7, these subunits were recently shown to be pivotal for the generation or destruction of several unique epitopes. In thisreview we discuss the recent data on LMP2/LMP7/MECL-1-dependent epitope generation and the functions of each of these subunit exchanges. We propose that these subunit exchanges have evolved not only to optimize class I peptide loading but also to generate LMP2/LMP7/MECL-1-dependent epitopes in inflammatory sites which are not proteolytically generated in uninflamed tissues. This difference in epitope generation may serve to better stimulate T cells in the sites of an ongoing immune response and to avoid autoimmunity inuninflamed tissues. (C) 2001 Societe francaise de biochimie et biologie moleculaire / Editions scientifiques et medicales Elsevier SAS. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/10/20 alle ore 05:23:22