Antigen degradation or presentation by MHC class I molecules via classical and non-classical pathways

被引:139
作者
Grommé, M [1 ]
Neefjes, J [1 ]
机构
[1] Netherlands Canc Inst, Div Tumor Biol, NL-1066 CX Amsterdam, Netherlands
关键词
antigen degradation; MHC class I molecules; classical and non-classical pathways; cross priming; antigen presentation; polymorphism;
D O I
10.1016/S0161-5890(02)00101-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Major histocompatibility complex (MHC) class I molecules usually present endogenous peptides at the cell surface. This is the result of a cascade of events involving various dedicated proteins like the peptide transporter associated with antigen processing (TAP) and the ER chaperone tapasin. However, alternative ways for class I peptide loading exist which may be highly relevant in a process called cross-priming. Both pathways are described here in detail. One major difference between these pathways is that the proteases involved in the generation of peptides are different. How proteases and peptidases influence peptide generation and degradation will be discussed. These processes determine the amount of peptides available for TAP translocation and class I binding and ultimately the immune response. (C) 2002 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:181 / 202
页数:22
相关论文
共 280 条
[61]  
DICK LR, 1994, J IMMUNOL, V152, P3884
[62]   Coordinated dual cleavages induced by the proteasome regulator PA28 lead to dominant MHC ligands [J].
Dick, TP ;
Ruppert, T ;
Groettrup, M ;
Kloetzel, PM ;
Kuehn, L ;
Koszinowski, UH ;
Stevanovic, S ;
Schild, H ;
Rammensee, HG .
CELL, 1996, 86 (02) :253-262
[63]   Decelerated degradation of short peptides by the 20S proteasome [J].
Dolenc, I ;
Seemüller, E ;
Baumeister, W .
FEBS LETTERS, 1998, 434 (03) :357-361
[64]   MARKEDLY DECREASED EXPRESSION OF CLASS-I HISTOCOMPATIBILITY ANTIGENS, PROTEIN, AND MESSENGER-RNA IN HUMAN SMALL-CELL LUNG-CANCER [J].
DOYLE, A ;
MARTIN, WJ ;
FUNA, K ;
GAZDAR, A ;
CARNEY, D ;
MARTIN, SE ;
LINNOILA, I ;
CUTTITTA, F ;
MULSHINE, J ;
BUNN, P ;
MINNA, J .
JOURNAL OF EXPERIMENTAL MEDICINE, 1985, 161 (05) :1135-1151
[65]   MHC-LINKED LMP GENE-PRODUCTS SPECIFICALLY ALTER PEPTIDASE ACTIVITIES OF THE PROTEASOME [J].
DRISCOLL, J ;
BROWN, MG ;
FINLEY, D ;
MONACO, JJ .
NATURE, 1993, 365 (6443) :262-264
[66]  
DUBIEL W, 1992, J BIOL CHEM, V267, P22369
[67]   THE CLEAVAGE PREFERENCE OF THE PROTEASOME GOVERNS THE YIELD OF ANTIGENIC PEPTIDES [J].
EGGERS, M ;
BOESFABIAN, B ;
RUPPERT, T ;
KLOETZEL, PM ;
KOSZINOWSKI, UH .
JOURNAL OF EXPERIMENTAL MEDICINE, 1995, 182 (06) :1865-1870
[68]   Effects of major-histocompatibility-complex-encoded subunits on the peptidase and proteolytic activities of human 20S proteasomes - Cleavage of proteins and antigenic peptides [J].
Ehring, B ;
Meyer, TH ;
Eckerskorn, C ;
Lottspeich, F ;
Tampe, R .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1996, 235 (1-2) :404-415
[69]   PROCESSING OF MAJOR HISTOCOMPATIBILITY CLASS-I-RESTRICTED ANTIGENS IN THE ENDOPLASMIC-RETICULUM [J].
ELLIOTT, T ;
WILLIS, A ;
CERUNDOLO, V ;
TOWNSEND, A .
JOURNAL OF EXPERIMENTAL MEDICINE, 1995, 181 (04) :1481-1491
[70]   PEPTIDE MOTIFS OF HLA-A1, HLA-A11, HLA-A31, AND HLA-A33 MOLECULES [J].
FALK, K ;
ROTZSCHKE, O ;
TAKIGUCHI, M ;
GRAHOVAC, B ;
GNAU, V ;
STEVANOVIC, S ;
JUNG, G ;
RAMMENSEE, HG .
IMMUNOGENETICS, 1994, 40 (03) :238-241