Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum

被引：566

作者：

Michalak, Marek ^{[1
]}

Groenendyk, Jody ^{[1
]}

Szabo, Eva ^{[2
]}

Gold, Leslie I. ^{[3
,4
]}

Opas, Michal ^{[2
]}

机构：

[1] Univ Alberta, Dept Biochem, Edmonton, AB T6G 2H7, Canada

[2] Univ Toronto, Lab Med & Pathobiol, Toronto, ON M5S 1A8, Canada

[3] NYU, Sch Med, Dept Med, New York, NY 10016 USA

[4] NYU, Sch Med, Dept Pathol, New York, NY 10016 USA

来源：

BIOCHEMICAL JOURNAL | 2009年 / 417卷

基金：

加拿大健康研究院;

关键词：

calcium homoeostasis; calreticulin; endoplasmic reticulum (ER); protein folding; quality control; CELL-SURFACE CALRETICULIN; CLASS-I MOLECULES; BINDING PROTEIN CALRETICULIN; RECEPTOR-RELATED PROTEIN; TUMOR-SPECIFIC IMMUNITY; QUALITY-CONTROL; MUTATIONAL ANALYSIS; CA2+ CONCENTRATION; INDUCED APOPTOSIS; GENE-EXPRESSION;

D O I：

10.1042/BJ20081847

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：

Calreticulin is an ER (endoplasmic reticulum) luminal Ca2+-buffering chaperone. The protein is involved ill regulation of intracellular Ca2+ homoeostasis and ER Ca2+ capacity. The protein impacts on store-operated Ca2+ influx and influences Ca2+ dependent transcriptional pathways during embryonic development. Calreticulin is also involved in the folding of newly synthesized proteins and glycoproteins and, together with calnexin (an integral ER membrane chaperone similar to calreticulin) and ERp57 [ER protein of 57 kDa; a PDI (protein disulfide-isomerase)-like ER-resident protein], constitutes the 'calreticulin/calnexin cycle' that is responsible for folding and quality control of newly synthesized glycoproteins. In recent years, calreticulin has been implicated to play a role in many biological systems, including functions inside and outside the ER, indicating that the protein is a multi-process molecule. Regulation of Ca2+ homoeostasis and ER Ca2+ buffering by calreticulin might be the key to explain its multi-process property.

引用

页码：651 / 666

页数：16

共 189 条

[41] Anti-Ro/SSA and La/SSB antibodies [J].

Franceschini, F ;

Cavazzana, I .

AUTOIMMUNITY, 2005, 38 (01) :55-63

[42] TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain [J].

Frickel, EM ;

Riek, R ;

Jelesarov, I ;

Helenius, A ;

Wüthrich, K ;

Ellgaard, L .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (04) :1954-1959

[43] Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin [J].

Gao, B ;

Adhikari, R ;

Howarth, M ;

Nakamura, K ;

Gold, MC ;

Hill, AB ;

Knee, R ;

Michalak, M ;

Elliott, T .

IMMUNITY, 2002, 16 (01) :99-109

[44] Cell-surface calreticulin initiates clearance of viable or apoptotic cells through trans-activation of LRP on the phagocyte [J].

Gardai, SJ ;

McPhillips, KA ;

Frasch, SC ;

Janssen, WJ ;

Starefeldt, A ;

Murphy-Ullrich, JE ;

Bratton, DL ;

Oldenborg, PA ;

Michalak, M ;

Henson, PM .

CELL, 2005, 123 (02) :321-334

[45] By binding SIRPα or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation [J].

Gardai, SJ ;

Xiao, YQ ;

Dickinson, M ;

Nick, JA ;

Voelker, DR ;

Greene, KE ;

Henson, PM .

CELL, 2003, 115 (01) :13-23

[46] GC1q-R/p33: Structure-function predictions from the crystal structure [J].

Ghebrehiwet, B ;

Jesty, J ;

Peerschke, EIB .

IMMUNOBIOLOGY, 2002, 205 (4-5) :421-432

[47] Characterization of natural vasostatin-containing peptides in rat heart [J].

Glattard, Elise ;

Angelone, Tommaso ;

Strub, Jean-Marc ;

Corti, Angelo ;

Aunis, Dominique ;

Tota, Bruno ;

Metz-Boutigue, Marie-Helene ;

Goumon, Yannick .

FEBS JOURNAL, 2006, 273 (14) :3311-3321

[48] The anti-adhesive activity of thrombospondin is mediated by the N-terminal domain of cell surface calreticulin [J].

Goicoechea, S ;

Pallero, MA ;

Eggleton, P ;

Michalak, M ;

Murphy-Ullrich, JE .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (40) :37219-37228

[49] Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin [J].

Goicoechea, S ;

Orr, AW ;

Pallero, MA ;

Eggleton, P ;

Murphy-Ullrich, JE .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (46) :36358-36368

[50] Overview of the role for calreticulin in the enhancement of wound healing through multiple biological effects [J].

Gold, Leslie I. ;

Rahman, Mohammad ;

Blechman, Keith M. ;

Greives, Matthew R. ;

Churgin, Samara ;

Michaels, Joseph ;

Callaghan, Matthew J. ;

Cardwell, Nancy L. ;

Pollins, Alonda C. ;

Michalak, Marek ;

Siebert, John W. ;

Levine, Jamie P. ;

Gurtner, Geoffrey C. ;

Nanney, Lillian B. ;

Galiano, Robert D. ;

Cadacio, Caprice L. .

JOURNAL OF INVESTIGATIVE DERMATOLOGY SYMPOSIUM PROCEEDINGS, 2006, 11 (01) :57-65

← 1 2 3 4 5 6 7 8 9 10 →