N-glycosylation processing and glycoprotein folding -: Lessons from the tyrosinase-related proteins

被引:36
作者
Branza-Nichita, N
Petrescu, AJ
Negroiu, G
Dwek, RA
Petrescu, SM
机构
[1] Romanian Acad, Inst Biochem, Bucharest 77700 17, Romania
[2] Univ Oxford, Dept Biochem, Oxford Glycobiol Inst, Oxford OX1 3QU, England
关键词
D O I
10.1021/cr990291y
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Tyrosinase is an attractive model because of its long in vivo processing time in the endoplastic reticulum (ER). Tyrosinase-derived antigenic peptides are a model system to study human leukocyte antigen (HLA) loading and presentation mechanisms which take place in the ER. This review outlines the results that have been obtained from tyrosinase and some tyrosinase-related proteins which provide insight into the role of ER chaperones in processes related to glycoprotein folding and degradation in vivo.
引用
收藏
页码:4697 / +
页数:16
相关论文
共 76 条
[1]   The lectin ERGIC-53 is a cargo transport receptor for glycoproteins [J].
Appenzeller, C ;
Andersson, H ;
Kappeler, F ;
Hauri, HP .
NATURE CELL BIOLOGY, 1999, 1 (06) :330-334
[2]   THE ACTION OF GLYCOSYLASES ON DOPACHROME (2-CARBOXY-2,3-DIHYDROINDOLE-5,6-QUINONE) TAUTOMERASE [J].
AROCA, P ;
MARTINEZLIARTE, JH ;
SOLANO, F ;
GARCIABORRON, JC ;
LOZANO, JA .
BIOCHEMICAL JOURNAL, 1992, 284 :109-113
[3]   Human tyrosinase related protein-1 (TRP-1) does not function as a DHICA oxidase activity in contrast to murine TRP-1 [J].
Boissy, RE ;
Sakai, C ;
Zhao, HQ ;
Kobayashi, T ;
Hearing, VJ .
EXPERIMENTAL DERMATOLOGY, 1998, 7 (04) :198-204
[4]   ISOLATION OF A HOMOGENEOUS GLUCOSIDASE-II FROM PIG-KIDNEY MICROSOMES [J].
BRADA, D ;
DUBACH, UC .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1984, 141 (01) :149-156
[5]   Mutations at critical N-glycosylation sites reduce tyrosinase activity by altering folding and quality control [J].
Branza-Nichita, N ;
Negroiu, G ;
Petrescu, AJ ;
Garman, EF ;
Platt, FM ;
Wormald, MR ;
Dwek, RA ;
Petrescu, SM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (11) :8169-8175
[6]   Tyrosinase folding and copper loading in vivo:: A crucial role for calnexin and α-glucosidase II [J].
Branza-Nichita, N ;
Petrescu, AJ ;
Dwek, RA ;
Wormald, MR ;
Platt, FM ;
Petrescu, SM .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1999, 261 (03) :720-725
[7]   The copper chaperone for superoxide dismutase [J].
Culotta, VC ;
Klomp, LWJ ;
Strain, J ;
Casareno, RLB ;
Krems, B ;
Gitlin, JD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (38) :23469-23472
[8]   Genetic evidence for the heterodimeric structure of glucosidase II -: The effect of disrupting the subunit-encoding genes on glycoprotein folding [J].
D'Alessio, C ;
Fernández, F ;
Trombetta, ES ;
Parodi, AJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (36) :25899-25905
[9]   THE FET3 GENE-PRODUCT REQUIRED FOR HIGH-AFFINITY IRON TRANSPORT IN YEAST IS A CELL-SURFACE FERROXIDASE [J].
DESILVA, DM ;
ASKWITH, CC ;
EIDE, D ;
KAPLAN, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (03) :1098-1101
[10]  
ELBEIN AD, 1987, ANNU REV BIOCHEM, V56, P497, DOI 10.1146/annurev.biochem.56.1.497