The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review
- PMID: 9749880
- DOI: 10.1016/s0163-7258(98)00013-8
The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review
Abstract
The 90-kDa molecular chaperone family (which comprises, among other proteins, the 90-kDa heat-shock protein, hsp90 and the 94-kDa glucose-regulated protein, grp94, major molecular chaperones of the cytosol and of the endoplasmic reticulum, respectively) has become an increasingly active subject of research in the past couple of years. These ubiquitous, well-conserved proteins account for 1-2% of all cellular proteins in most cells. However, their precise function is still far from being elucidated. Their involvement in the aetiology of several autoimmune diseases, in various infections, in recognition of malignant cells, and in antigen-presentation already demonstrates the essential role they likely will play in clinical practice of the next decade. The present review summarizes our current knowledge about the cellular functions, expression, and clinical implications of the 90-kDa molecular chaperone family and some approaches for future research.
Similar articles
-
GRP94, an ER chaperone with protein and peptide binding properties.Semin Cell Dev Biol. 1999 Oct;10(5):495-505. doi: 10.1006/scdb.1999.0320. Semin Cell Dev Biol. 1999. PMID: 10597632 Review.
-
The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications.Crit Rev Eukaryot Gene Expr. 1994;4(1):1-18. doi: 10.1615/critreveukargeneexpr.v4.i1.10. Crit Rev Eukaryot Gene Expr. 1994. PMID: 7987045 Review.
-
Hop: more than an Hsp70/Hsp90 adaptor protein.Bioessays. 2004 Oct;26(10):1058-68. doi: 10.1002/bies.20107. Bioessays. 2004. PMID: 15382137 Review.
-
Roles of molecular chaperones in protein misfolding diseases.Semin Cell Dev Biol. 2004 Feb;15(1):17-29. doi: 10.1016/j.semcdb.2003.12.010. Semin Cell Dev Biol. 2004. PMID: 15036203 Review.
-
The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding.EMBO J. 1996 Jun 17;15(12):2969-79. EMBO J. 1996. PMID: 8670798 Free PMC article.
Cited by
-
Identification of epipolythiodioxopiperazines HDN-1 and chaetocin as novel inhibitor of heat shock protein 90.Oncotarget. 2015 Mar 10;6(7):5263-74. doi: 10.18632/oncotarget.3029. Oncotarget. 2015. PMID: 25742791 Free PMC article.
-
Immunohistochemical detection of Hsp90 and Ki-67 in pterygium.Diagn Pathol. 2013 Feb 21;8:32. doi: 10.1186/1746-1596-8-32. Diagn Pathol. 2013. PMID: 23432803 Free PMC article.
-
Extracellular Hsp90 (eHsp90) as the actual target in clinical trials: intentionally or unintentionally.Int Rev Cell Mol Biol. 2013;303:203-35. doi: 10.1016/B978-0-12-407697-6.00005-2. Int Rev Cell Mol Biol. 2013. PMID: 23445811 Free PMC article. Review.
-
Small molecule activators of the heat shock response: chemical properties, molecular targets, and therapeutic promise.Chem Res Toxicol. 2012 Oct 15;25(10):2036-53. doi: 10.1021/tx300264x. Epub 2012 Jul 31. Chem Res Toxicol. 2012. PMID: 22799889 Free PMC article. Review.
-
Hsp90 interaction with INrf2(Keap1) mediates stress-induced Nrf2 activation.J Biol Chem. 2010 Nov 19;285(47):36865-75. doi: 10.1074/jbc.M110.175802. Epub 2010 Sep 23. J Biol Chem. 2010. Retraction in: J Biol Chem. 2014 Apr 18;289(16):11568. doi: 10.1074/jbc.A110.175802. PMID: 20864537 Free PMC article. Retracted.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Miscellaneous