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Titolo:
Characterization of peroxynitrite-oxidized low density lipoprotein bindingto human CD36
Autore:
Guy, RA; Maguire, GF; Crandall, I; Connelly, PW; Kain, KC;
Indirizzi:
Univ Toronto, Inst Med Sci, Dept Med, Toronto, ON M5S 1A8, Canada Univ Toronto Toronto ON Canada M5S 1A8 t Med, Toronto, ON M5S 1A8, Canada Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8, Canada Univ Toronto Toronto ON Canada M5S 1A8 ochem, Toronto, ON M5S 1A8, Canada Univ Toronto, Dept Lab Med & Pathobiol, Toronto, ON M5S 1A8, Canada Univ Toronto Toronto ON Canada M5S 1A8 obiol, Toronto, ON M5S 1A8, Canada Toronto Hosp, Trop Dis Unit, Div Infect Dis, Toronto, ON M5G 2C4, Canada Toronto Hosp Toronto ON Canada M5G 2C4 t Dis, Toronto, ON M5G 2C4, Canada St Michaels Hosp, Dept Med, Toronto, ON M5B 1W8, Canada St Michaels Hosp Toronto ON Canada M5B 1W8 d, Toronto, ON M5B 1W8, Canada
Titolo Testata:
ATHEROSCLEROSIS
fascicolo: 1, volume: 155, anno: 2001,
pagine: 19 - 28
SICI:
0021-9150(200103)155:1<19:COPLDL>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
SMOOTH-MUSCLE CELLS; HUMAN-ENDOTHELIAL-CELLS; PLASMODIUM-FALCIPARUM; SCAVENGER RECEPTOR; NITRIC-OXIDE; ATHEROSCLEROTIC LESIONS; MACROPHAGE GROWTH; HUMAN MALARIA; PPAR-GAMMA; KAPPA-B;
Keywords:
oxidation; copper; peroxynitrite; scavenger receptors; CD36; atherosclerosis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
71
Recensione:
Indirizzi per estratti:
Indirizzo: Crandall, I Univ Toronto, Inst Med Sci, Dept Med, Rm 7202 Med Sci Bldg,8 Taddle Creek Rd, Toronto, ON M5S 1A8, Canada Univ Toronto Rm 7202 Med Sci Bldg,8 Taddle Creek Rd Toronto ON Canada M5S 1A8
Citazione:
R.A. Guy et al., "Characterization of peroxynitrite-oxidized low density lipoprotein bindingto human CD36", ATHEROSCLER, 155(1), 2001, pp. 19-28

Abstract

Peroxynitrite-mediated oxidation may be an important physiological mechanism for oxidation of low density lipoprotein (LDL), however, the molecular basis for the interaction of peroxynitrite oxidized LDL (OxLDL) with scavenger receptors such as CD36, has not been characterized. In this study, we compared the biochemical characteristics and receptor binding of LDL that wasoxidized using: (1) CU2+, a Standard method of oxidizing LDL in vitro; and(2) 3-morpholinosydnonimine (SIN-1), a source of peroxynitrite. Both methods of oxidation caused an increase in electrophoretic migration of LDL, butgreater mobility was observed with Cu2+-OxLDL. In addition, greater fragmentation of apolipoprotein B was observed following CU2+ oxidation than after SIN-1 oxidation. The levels of lipid peroxides and thiobarbituric acid reactive substances were similar after 20 h of oxidation by both methods, although the time-course was distinct. CU2+ and SIN-1-OxLDL bound specificallyto the macrophage scavenger receptor CD36 with high affinity. Binding of the 20 h SIN-1 treated LDL to CD36 was comparable to a 4 h Cu2+ modified LDL. The binding of Cu2+ and SIN-1-OxLDL to CD36 was similar under different biochemical conditions and modifications of the receptor, suggesting that OxLDL particles, generated by either method, bind to the same domain of CD36. The results demonstrate that SIN-1 produced an oxidized LDL particle that binds specifically to CD36 and suggests that peroxynitrite OxLDL may represent a more physiologically relevant model than CU2+-OxLDL for studying the interactions of OxLDL with cells and lipoprotein receptors in vitro. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 10:27:24