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Titolo:
Clusterin, a binding protein with a molten globule-like region
Autore:
Bailey, RW; Dunker, AK; Brown, CJ; Garner, EC; Griswold, MD;
Indirizzi:
Washington State Univ, Sch Mol Biosci, Pullman, WA 99164 USA Washington State Univ Pullman WA USA 99164 Biosci, Pullman, WA 99164 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 39, volume: 40, anno: 2001,
pagine: 11828 - 11840
SICI:
0006-2960(20011002)40:39<11828:CABPWA>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
SULFATED GLYCOPROTEIN-2 CLUSTERIN; CIRCULAR-DICHROISM SPECTRA; AMYLOID BETA-PEPTIDE; APOPTOTIC CELL-DEATH; APOLIPOPROTEIN-J; SERTOLI CELLS; SECONDARY STRUCTURE; LIMITED PROTEOLYSIS; CRYSTAL-STRUCTURES; OXIDATIVE STRESS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
85
Recensione:
Indirizzi per estratti:
Indirizzo: Griswold, MD Washington State Univ, Sch Mol Biosci, Pullman, WA 99164 USA Washington State Univ Pullman WA USA 99164 man, WA 99164 USA
Citazione:
R.W. Bailey et al., "Clusterin, a binding protein with a molten globule-like region", BIOCHEM, 40(39), 2001, pp. 11828-11840

Abstract

Clusterin is a heterodimeric glycoprotein found in many tissues of the body and is the most abundant protein secreted by cultured rat Sertoli cells. The function of clusterin is unknown, but it has been associated with cellular injury, lipid transport, apoptosis, and it may be involved in the clearance of cellular debris caused by cell injury or death. Consistent with this last idea, clusterin has been shown to bind to a variety of molecules with high affinity including lipids, peptides, and proteins and the hydrophobic probe 1-anilino-8-naphthalenesulfonate (ANS). Given this variety of ligands, clusterin must have specific structural features that provide the protein with its promiscuous binding activity. Using sequence analyses, we show that clusterin likely contains three long regions of natively disordered ormolten globule-like structures containing putative amphipathic alpha -helices. These disordered regions were highly sensitive to trypsin digestion, indicating a flexible nature. The effects of denaturation on the fluorescence of the clusterin-ANS complex were compared between proteins with structured binding pockets and molten globular forms of proteins. Clusterin bound ANS in a manner that was very similar to that of molten globular proteins. Furthermore, we found that, when bound to ANS, at least one cleavage site within the protease-sensitive disordered regions of clusterin was protected fron) trypsin digestion. In addition, we show that clusterin can function asa biological detergent that can solubilize bacteriorhodopsin. We propose that natively disordered regions with amphipathic helices form a dynamic, molten globule-like binding site and provide clusterin the ability to bind toa variety of molecules.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 09:33:51