Production of an antigenic peptide by insulin-degrading enzyme

被引：52

作者：

Parmentier, Nicolas ^{[1
,2
]}

Stroobant, Vincent ^{[1
,2
]}

Colau, Didier ^{[1
,2
]}

de Diesbach, Philippe ^{[3
]}

Morel, Sandra ^{[1
,2
]}

Chapiro, Jacques ^{[1
,2
]}

van Endert, Peter ^{[4
,5
]}

Van den Eynde, Benoit J. ^{[1
,2
]}

机构：

[1] Ludwig Inst Canc Res, Brussels Branch, Brussels, Belgium

[2] Catholic Univ Louvain, Cellular Genet Unit, Duve Inst, B-1200 Brussels, Belgium

[3] Catholic Univ Louvain, Cell Unit, Duve Inst, B-1200 Brussels, Belgium

[4] INSERM, U103, Paris, France

[5] Univ Paris 05, Fac Med Rene Descartes, Paris, France

来源：

NATURE IMMUNOLOGY | 2010年 / 11卷 / 05期

关键词：

CYTOLYTIC T-LYMPHOCYTES; TRIPEPTIDYL-PEPTIDASE; CELL RESPONSES; ANTIBODY; 57B; GENERATION; IDENTIFICATION; PURIFICATION; DEGRADATION; PROTEASOME; MELANOMA;

D O I：

10.1038/ni.1862

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Most antigenic peptides presented by major histocompatibility complex (MHC) class I molecules are produced by the proteasome. Here we show that a proteasome-independent peptide derived from the human tumor protein MAGE-A3 is produced directly by insulin-degrading enzyme (IDE), a cytosolic metallopeptidase. Cytotoxic T lymphocyte recognition of tumor cells was reduced after metallopeptidase inhibition or IDE silencing. Separate inhibition of the metallopeptidase and the proteasome impaired degradation of MAGE-A3 proteins, and simultaneous inhibition of both further stabilized MAGE-A3 proteins. These results suggest that MAGE-A3 proteins are degraded along two parallel pathways that involve either the proteasome or IDE and produce different sets of antigenic peptides presented by MHC class I molecules.

引用

页码：449 / U114

页数：8

共 46 条

[1] Authier F, 1996, CLIN INVEST MED, V19, P149
[2] Evidence for genetic linkage of Alzheimer's disease to chromosome 10q
Bertram, L
Blacker, D
Mullin, K
Keeney, D
Jones, J
Basu, S
Yhu, S
McInnis, MG
Go, RCP
Vekrellis, K
Selkoe, DJ
Saunders, AJ
Tanzi, RE
[J]. SCIENCE, 2000, 290 (5500) : 2302 - +
[3] Human T cell responses against melanoma
Boon, Thierry
Coulie, Pierre G.
Van den Eynde, Benoit J.
van der Bruggen, Pierre
[J]. ANNUAL REVIEW OF IMMUNOLOGY, 2006, 24 : 175 - 208
[4] CHESNEAU V, 1994, J BIOL CHEM, V269, P2056
[5] Nardilysin cleaves peptides at monobasic sites
Chow, KM
Oakley, O
Goodman, J
Ma, ZL
Juliano, MA
Juliano, L
Hersh, LB
[J]. BIOCHEMISTRY, 2003, 42 (07) : 2239 - 2244
[6] Two distinct proteolytic processes in the generation of a major histocompatibility complex class I-presented peptide
Craiu, A
Akoplan, T
Goldberg, A
Rock, KL
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (20) : 10850 - 10855
[7] de Diesbach P, 2000, NUCLEIC ACIDS RES, V28, P868
[8] Insulin degradation: Progress and potential
Duckworth, WC
Bennett, RG
Hamel, FG
[J]. ENDOCRINE REVIEWS, 1998, 19 (05) : 608 - 624
[9] PURIFICATION OF A PROTEASE IN RED-BLOOD-CELLS THAT DEGRADES OXIDATIVELY DAMAGED HEMOGLOBIN
FAGAN, JM
WAXMAN, L
[J]. BIOCHEMICAL JOURNAL, 1991, 277 : 779 - 786
[10] Insulin-degrading enzyme regulates the levels of insulin, amyloid β-protein, and the β-amyloid precursor protein intracellular domain in vivo
Farris, W
Mansourian, S
Chang, Y
Lindsley, L
Eckman, EA
Frosch, MP
Eckman, CB
Tanzi, RE
Selkoe, DJ
Guénette, S
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (07) : 4162 - 4167

← 1 2 3 4 5 →