Roles of heat-shock proteins in innate and adaptive immunity

被引：841

作者：

Srivastava, P ^{[1
]}

机构：

[1] Univ Connecticut, Sch Med, Ctr Immunotherapy Canc & Infect Dis, Farmington, CT 06030 USA

来源：

NATURE REVIEWS IMMUNOLOGY | 2002年 / 2卷 / 03期

关键词：

D O I：

10.1038/nri749

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Heat-shock proteins (HSPs) are the most abundant and ubiquitous soluble intracellular proteins. In single-cell organisms, invertebrates and vertebrates, they perform a multitude of housekeeping functions that are essential for cellular survival. In higher vertebrates, their ability to interact with a wide range of proteins and peptides - a property that is shared by major histocompatibility complex molecules - has made the HSPs uniquely suited to an important role in organismal survival by their participation in innate and adaptive immune responses. The immunological properties of HSPs enable them to be used in new immunotherapies of cancers and infections.

引用

页码：185 / 194

页数：10

共 104 条

[1] Peptide and major histocompatibility complex-specific breaking of humoral tolerance to native insulin with the B9-23 peptide in diabetes-prone and normal mice [J].

Abiru, N ;

Maniatis, AK ;

Yu, LP ;

Miao, DM ;

Moriyama, H ;

Wegmann, D ;

Eisenbarth, GS .

DIABETES, 2001, 50 (06) :1274-1281

[2] THE ENDOPLASMIC RETICULAR HEAT-SHOCK PROTEIN GP96 IS TRANSCRIPTIONALLY UP-REGULATED IN INTERFERON-TREATED CELLS [J].

ANDERSON, SL ;

SHEN, T ;

LOU, J ;

XING, L ;

BLACHERE, NE ;

SRIVASTAVA, PK ;

RUBIN, BY .

JOURNAL OF EXPERIMENTAL MEDICINE, 1994, 180 (04) :1565-1569

[3] α2-macroglobulin:: an evolutionarily conserved arm of the innate immune system [J].

Armstrong, PB ;

Quigley, JP .

DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY, 1999, 23 (4-5) :375-390

[4] Influences of transporter associated with antigen processing (TAP) on the repertoire of peptides associated with the endoplasmic reticulum-resident stress protein gp96 [J].

Arnold, D ;

Wahl, C ;

Faath, S ;

Rammensee, HG ;

Schild, H .

JOURNAL OF EXPERIMENTAL MEDICINE, 1997, 186 (03) :461-466

[5] CROSS-PRIMING OF MINOR HISTOCOMPATIBILITY ANTIGEN-SPECIFIC CYTOTOXIC T-CELLS UPON IMMUNIZATION WITH THE HEAT-SHOCK PROTEIN GP96 [J].

ARNOLD, D ;

FAATH, S ;

RAMMENSEE, HG ;

SCHILD, H .

JOURNAL OF EXPERIMENTAL MEDICINE, 1995, 182 (03) :885-889

[6] Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-κB pathway [J].

Basu, S ;

Binder, RJ ;

Suto, R ;

Anderson, KM ;

Srivastava, PK .

INTERNATIONAL IMMUNOLOGY, 2000, 12 (11) :1539-1546

[7] CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin [J].

Basu, S ;

Binder, RJ ;

Ramalingam, T ;

Srivastava, PK .

IMMUNITY, 2001, 14 (03) :303-313

[8] Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- and peptide-specific immunity [J].

Basu, S ;

Srivastava, PK .

JOURNAL OF EXPERIMENTAL MEDICINE, 1999, 189 (05) :797-802

[9] Replisome-mediated DNA replication [J].

Benkovic, SJ ;

Valentine, AM ;

Salinas, F .

ANNUAL REVIEW OF BIOCHEMISTRY, 2001, 70 :181-208

[10] Cutting edge:: Heat shock protein gp96 induces maturation and migration of CD11c+ cells in vivo [J].

Binder, RJ ;

Anderson, KM ;

Basu, S ;

Srivastava, PK .

JOURNAL OF IMMUNOLOGY, 2000, 165 (11) :6029-6035

← 1 2 3 4 5 6 7 8 9 10 →