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Titolo:
Clusterin has chaperone-like activity similar to that of small heat shock proteins
Autore:
Humphreys, DT; Carver, JA; Easterbrook-Smith, SB; Wilson, MR;
Indirizzi:
Univ Wollongong, Dept Sci Biol, Wollongong, NSW 2522, Australia Univ Wollongong Wollongong NSW Australia 2522 ongong, NSW 2522, Australia Univ Wollongong, Dept Chem, Wollongong, NSW 2522, Australia Univ Wollongong Wollongong NSW Australia 2522 ongong, NSW 2522, Australia Univ Sydney, Dept Biochem, Sydney, NSW 2006, Australia Univ Sydney SydneyNSW Australia 2006 iochem, Sydney, NSW 2006, Australia
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 11, volume: 274, anno: 1999,
pagine: 6875 - 6881
SICI:
0021-9258(19990312)274:11<6875:CHCAST>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
SULFATED GLYCOPROTEIN-2; HUMAN PLASMA; APOLIPOPROTEIN-J/CLUSTERIN; ALPHA-CRYSTALLIN; EPITHELIAL-CELLS; TESTIS FLUID; COMPLEMENT; STRESS; DEATH; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Wilson, MR Univraliaongong, Dept Sci Biol, Northfields Ave, Wollongong, NSW 2522, Aust Univ Wollongong Northfields Ave Wollongong NSW Australia 2522 t
Citazione:
D.T. Humphreys et al., "Clusterin has chaperone-like activity similar to that of small heat shock proteins", J BIOL CHEM, 274(11), 1999, pp. 6875-6881

Abstract

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. The results presented here demonstrate for the first time that clusterin has chaperone-like activity. At physiological concentrations, clusterin potently protected glutathione S-transferase and catalase from heat-induced precipitation and alpha-lactalbumin and bovine serum albumin from precipitation induced by reduction with dithiothreitol. Enzyme-linked immunosorbent assay data showed that clusterin bound preferentially to heat-stressed glutathione S-transferase and to dithiothreitol-treated bovine serum albumin and alpha-lactalbumin. Size exclusion chromatography and SDS-polyacrylamide gel electrophoresis analyses showed that clusterin formed high molecular weight complexes (HMW) with all four proteins tested. Small heat shock proteins (sHSP) also act in this way to prevent protein precipitation and protect cells from heat and other stresses. The stoichiometric subunit molar ratiosof clusterin:stressed protein during formation of HMW complexes (which forthe four proteins tested ranged from 1.0:1.3 to 1.0:11) is less than the reported ratios for sHSP-mediated formation of HMW complexes (1.0:1.0 or greater), indicating that clusterin is a very efficient chaperone. Our resultssuggest that clusterin may play a sHSP-like role in cytoprotection.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 06:55:56