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Titolo:
Major apolipoprotein B-100 mutations in lipoprotein metabolism and atherosclerosis
Autore:
Vrablik, M; Ceska, R; Horinek, A;
Indirizzi:
Charles Univ, Fac Med 1, Internal Dept 3, Prague 12821 2, Czech Republic Charles Univ Prague Czech Republic 12821 2 rague 12821 2, Czech Republic
Titolo Testata:
PHYSIOLOGICAL RESEARCH
fascicolo: 4, volume: 50, anno: 2001,
pagine: 337 - 343
SICI:
0862-8408(2001)50:4<337:MABMIL>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
FAMILIAL DEFECTIVE APOLIPOPROTEIN-B-100; LOW-DENSITY LIPOPROTEINS; RECEPTOR-BINDING DOMAIN; HAPLOTYPE ANALYSIS; B GENE; ARGININE(3500)->GLUTAMINE MUTATION; R3531C MUTATION; HEART-DISEASE; LDL RECEPTOR; HYPERCHOLESTEROLEMIA;
Keywords:
apolipoprotein B-100; mutations; hyperlipidemia; atherosclerosis;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Vrablik, M Charles Univ, Fac Med 1, Internal Dept 3, Nemocnice 1, Prague 12821 2, Czech Republic Charles Univ Nemocnice 1 Prague Czech Republic 12821 2 epublic
Citazione:
M. Vrablik et al., "Major apolipoprotein B-100 mutations in lipoprotein metabolism and atherosclerosis", PHYSL RES, 50(4), 2001, pp. 337-343

Abstract

Apolipoprotein (apo) B-100 is a key protein compound of plasma lipid metabolism. This protein, as a sole component of LDL particles, to a great extent controls the homeostasis of LDL cholesterol in the plasma. Therefore, this protein and its structural variants play an important role in developmentof hyperlipidemia and atherosclerosis. Intensive research into the structure and biological functions of apoB-100 has led to identification of its complete structure as well as the responsible binding sites. With the development of the methods of molecular biology, some structural variants of the apoB-100 protein that directly affect its binding properties have been described. These are mutations leading to amino acid substitution at positions 3500 (R3500Q and R3500W) and 3531 (R3531C) that have been shown to decrease the binding affinity of apoB-100 in vitro. However, only the former mutations have been unequivocally demonstrated to cause hyperlipidemia in vivo. This minireview is aimed to discuss the impact of apoB-100 and its structuralvariants on plasma lipid metabolism and development of hyperlipidemia.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 22:07:54