Gene Symbol: CLU
Alias: GP80, clusterin, clusterin (complement lysis inhibitor, SP-40,40, sulfated glycoprotein 2, testosterone-repressed prostate message 2, apolipoprotein J), glycoprotein 80
Hartmann K, Rauch J, Urban J, Parczyk K, Diel P, Pilarsky C, et al
. Molecular cloning of gp 80, a glycoprotein complex secreted by kidney cells in vitro and in vivo. A link to the reproductive system and to the complement cascade. J Biol Chem. 1991;266:9924-31 pubmed
..The protein is expressed in the embryonic kidney already early during organogenesis. In the adult kidney the protein has been localized along the luminal surfaces of the proximal and distal tubule and the collecting duct cells. ..
Humphreys D, Carver J, Easterbrook Smith S, Wilson M. Clusterin has chaperone-like activity similar to that of small heat shock proteins. J Biol Chem. 1999;274:6875-81 pubmed
b>Clusterin is a highly conserved protein which is expressed at increased levels by many cell types in response to a broad variety of stress conditions. A genuine physiological function for clusterin has not yet been established...
Li Y, Qu J, Shelat H, Gao S, Wassler M, Geng Y. Clusterin induces CXCR4 expression and migration of cardiac progenitor cells. Exp Cell Res. 2010;316:3435-42 pubmed publisher
b>Clusterin (CST) is a stress-responding protein with multiple biological functions, including the inhibition of apoptosis and inflammation and transport of lipids. It may also participate in cell traffic and migration...
Wilson M, Easterbrook Smith S. Clusterin is a secreted mammalian chaperone. Trends Biochem Sci. 2000;25:95-8 pubmed
Bando Y, Ogawa S, Yamauchi A, Kuwabara K, Ozawa K, Hori O, et al
. 150-kDa oxygen-regulated protein (ORP150) functions as a novel molecular chaperone in MDCK cells. Am J Physiol Cell Physiol. 2000;278:C1172-82 pubmed
..of MDCK cells to hypoxia resulted in an increase of ORP150 antigen and increased binding of ORP150 to GP80/clusterin (80-kDa glycoprotein), a natural secretory protein in this cell line...
Poon S, Easterbrook Smith S, Rybchyn M, Carver J, Wilson M. Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state. Biochemistry. 2000;39:15953-60 pubmed
We recently reported that the ubiquitous, secreted protein clusterin has chaperone activity in vitro [Humphreys et al. (1999) J. Biol. Chem. 274, 6875-6881]...
Yerbury J, Poon S, Meehan S, Thompson B, Kumita J, Dobson C, et al
. The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures. FASEB J. 2007;21:2312-22 pubmed
b>Clusterin is an extracellular chaperone present in all disease-associated extracellular amyloid deposits, but its roles in amyloid formation and protein deposition in vivo are poorly understood...
Nizard P, Tetley S, Le Drean Y, Watrin T, Le Goff P, Wilson M, et al
. Stress-induced retrotranslocation of clusterin/ApoJ into the cytosol. Traffic. 2007;8:554-65 pubmed
b>Clusterin is a usually secreted glycoprotein with chaperone properties...
Wyatt A, Yerbury J, Poon S, Dabbs R, Wilson M. Chapter 6: The chaperone action of Clusterin and its putative role in quality control of extracellular protein folding. Adv Cancer Res. 2009;104:89-114 pubmed publisher
The function(s) of clusterin may depend upon its topological location. A variety of intracellular "isoforms" of clusterin have been reported but further work is required to better define their identity...