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Titolo:
Discrete cleavage motifs of constitutive and immunoproteasomes revealed byquantitative analysis of cleavage products
Autore:
Toes, REM; Nussbaum, AK; Degermann, S; Schirle, M; Emmerich, NPN; Kraft, M; Laplace, C; Zwinderman, A; Dick, TP; Muller, J; Schonfisch, B; Schmid, C; Fehling, HJ; Stevanovic, S; Rammensee, HG; Schild, H;
Indirizzi:
Univ Tubingen, Inst Cell Biol, Dept Immunol, D-72076 Tubingen, Germany Univ Tubingen Tubingen Germany D-72076 mmunol, D-72076 Tubingen, Germany Univ Tubingen, Inst Cell Biol, Dept Biomath, D-72076 Tubingen, Germany Univ Tubingen Tubingen Germany D-72076 iomath, D-72076 Tubingen, Germany Leiden Univ, Med Ctr, Dept Rheumatol, Dept Immunohematol & Blood Transfus,NL-2333 ZA Leiden, Netherlands Leiden Univ Leiden Netherlands NL-2333 ZA NL-2333 ZA Leiden, Netherlands Yale Univ, Sch Med, Howard Hughes Med Inst, Immunobiol Sect, New Haven, CT06520 USA Yale Univ New Haven CT USA 06520 Immunobiol Sect, New Haven, CT06520 USA Basel Inst Immunol, CH-4005 Basel, Switzerland Basel Inst Immunol Basel Switzerland CH-4005 CH-4005 Basel, Switzerland Univ Clin Ulm, Fac Med, Dept Immunol, D-89070 Ulm, Germany Univ Clin Ulm Ulm Germany D-89070 ed, Dept Immunol, D-89070 Ulm, Germany
Titolo Testata:
JOURNAL OF EXPERIMENTAL MEDICINE
fascicolo: 1, volume: 194, anno: 2001,
pagine: 1 - 12
SICI:
0022-1007(20010702)194:1<1:DCMOCA>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
MHC CLASS-I; DENDRITIC CELLS; APOPTOTIC CELLS; 20S PROTEASOME; BETA-SUBUNITS; CTL EPITOPE; PEPTIDE; INTERFERON; GENERATION; EXPRESSION;
Keywords:
constitutive proteasomes; immunoproteasomes; CTL epitope; peptide repertoire; tolerance;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Schild, H Univ Tubingen, Inst Cell Biol, Dept Immunol, Morgenstelle 15, D-72076 Tubingen, Germany Univ Tubingen Morgenstelle 15 Tubingen Germany D-72076 Germany
Citazione:
R.E.M. Toes et al., "Discrete cleavage motifs of constitutive and immunoproteasomes revealed byquantitative analysis of cleavage products", J EXP MED, 194(1), 2001, pp. 1-12

Abstract

Proteasomes are the main proteases responsible for cytosolic protein degradation and the production of major histocompatibility complex class I ligands. Incorporation of the interferon gamma -inducible subunits low molecularweight protein (LMP)-2, LMP-7, and multicatalytic endopeptidase complex-like (MECL)-1 leads to the formation of immunoproteasomes which have been associated with more efficient class I antigen processing. Although differences in cleavage specificities of constitutive and immunoproteasomes have beenobserved frequently, cleavage motifs have not been described previously. We now report that cells expressing immunoproteasomes display a different peptide repertoire changing the overall cytotoxic T cell-specificity as indicated by the observation that LMP-7(-/-) mice react again cells of LMP-7 wild type mice. Moreover, using the 436 amino acid protein enolase-1 as an unmodified model substrate in combination with a quantitative approach, we analyzed a large collection of peptides generated by either set of proteasomes. Inspection of the amino acids flanking proteasomal cleavage sites allowed the description of two different cleavage motifs. These motifs finally explain recent findings describing differential processing of epitopes by constitutive and immunoproteasomes and are important to the understanding of peripheral T cell tolerization/activation as well as for effective vaccine development.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 15:07:33