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Titolo:
Biglycan, a vascular proteoglycan, binds differently to HDL2 and HDL3 - Role of ApoE
Autore:
Olin, KL; Potter-Perigo, S; Barrett, PHR; Wight, TN; Chait, A;
Indirizzi:
Univ Washington, Dept Med, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 ton, Dept Med, Seattle, WA 98195 USA Univ Washington, Dept Pathol, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 , Dept Pathol, Seattle, WA 98195 USA Univ Western Australia, Dept Med, Perth, WA 6009, Australia Univ Western Australia Perth WA Australia 6009 Perth, WA 6009, Australia
Titolo Testata:
ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY
fascicolo: 1, volume: 21, anno: 2001,
pagine: 129 - 135
SICI:
1079-5642(200101)21:1<129:BAVPBD>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
LOW-DENSITY LIPOPROTEINS; SMOOTH-MUSCLE CELLS; APOLIPOPROTEIN-A-I; HUMAN CORONARY-ARTERIES; RECEPTOR-BINDING; WALL PROTEOGLYCANS; HUMAN-FIBROBLASTS; GROWTH-FACTOR; DECORIN; MACROPHAGES;
Keywords:
high density lipoproteins; biglycan; atherosclerosis; proteoglycans; apolipoprotein E;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Chait, A Univ Washington, Dept Med, Box 356426, Seattle, WA 98195 USA UnivWashington Box 356426 Seattle WA USA 98195 tle, WA 98195 USA
Citazione:
K.L. Olin et al., "Biglycan, a vascular proteoglycan, binds differently to HDL2 and HDL3 - Role of ApoE", ART THROM V, 21(1), 2001, pp. 129-135

Abstract

Lipoprotein retention by vascular extracellular matrix proteoglycans is important in atherogenesis; Proteoglycans bind apolipoprotein (apo)B- and apoE-containing lipoproteins. However, the colocalization of apoA-I and apoE with biglycan in atherosclerotic lesions suggests that vascular proteoglycans also may trap high density lipoproteins (HDLs), Because the major HDL subclasses may be atheroprotective to different degrees, we investigated the role of apoE in mediating HDL2 and HDL3 binding to the extracellular vascular proteoglycan, biglycan. ApoE-free HDL2 and HDL3 did not bind to purified [S-35]SO4-biglycan, whereas apoE-containing HDL2 and HDL3 (HDL+E) did. The extent of binding correlated positively with the apoE content for both HDL2and HDL3, although HDL2+E had a 3.5-fold higher affinity than did HDL3+E. ApoE on HDL3 was cleaved into 22- and 12-kDa fragments, whereas apoE on HDL2 remained intact. These results suggest that the cleaved apoE on HDL3 results in diminished biglycan binding of HDL3+E relative to HDL2+E. Reducing positive charges on lysine and arginine residues on HDL+E eliminated biglycan binding, suggesting an ionic interaction. Thus, apoE is an important determinant of HDL binding to extracellular vascular proteoglycans and may playa role in HDL retention in the artery wall.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/10/20 alle ore 14:00:08