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Titolo:
Apolipoprotein E1 Baden (Arg(180)-> Cys) - A new apolipoprotein E variant associated with hypertriglyceridemia
Autore:
Hoffmann, MM; Scharnagl, H; Koster, W; Winkler, K; Wieland, H; Marz, W;
Indirizzi:
Univ Freiburg, Sch Med, Div Clin Chem, D-79106 Freiburg, Germany Univ Freiburg Freiburg Germany D-79106 n Chem, D-79106 Freiburg, Germany
Titolo Testata:
CLINICA CHIMICA ACTA
fascicolo: 1-2, volume: 303, anno: 2001,
pagine: 41 - 48
SICI:
0009-8981(200101)303:1-2<41:AEB(C->2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRIGLYCERIDE-RICH LIPOPROTEINS; LIPASE-MEDIATED LIPOLYSIS; RECEPTOR-BINDING ACTIVITY; III HYPERLIPOPROTEINEMIA; DOMAIN; HYPERLIPIDEMIA; ARGININE-61; SEQUENCE; GENE;
Keywords:
apolipoprotein E; DNA sequencing; hypertriglyceridemia; mutation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Hoffmann, MM Univ Freiburg, Sch Med, Div Clin Chem, Hugstetter Str 55, D-79106 Freiburg, Germany Univ Freiburg Hugstetter Str 55 Freiburg Germany D-79106 any
Citazione:
M.M. Hoffmann et al., "Apolipoprotein E1 Baden (Arg(180)-> Cys) - A new apolipoprotein E variant associated with hypertriglyceridemia", CLIN CHIM A, 303(1-2), 2001, pp. 41-48

Abstract

Apolipoprotein (apo) E mediates the removal of chylomicron and very low density lipoprotein remnants from plasma. It is polymorphic in sequence and the products of the three common alleles (epsilon2, epsilon3, epsilon4) differ from one another in their binding to lipoprotein receptors. ApoE2 is defective in binding and homozygosity for apoE2 is associated with type III hyperlipoproteinemia (HLP). Other rare isoforms of apoE have been found to beassociated either with dominant type III HLP or with the development of hypertriglyceridemia. We identified a 42 year-old hypertriglyceridemic woman with an apoE phenotype 3/1. Restriction isotyping using AflIII/HaeII resulted in an apparent apoE genotype 3/2, suggesting that the mutation occurred in an epsilon2 allele. DNA sequence analysis revealed a C-->T point mutation at the first position of the codon for amino acid residue 180 of the mature apoE. This predicted a change ARG(180)-->Cys. The mutation altered a recognition site for the endonuclease HaeII, which allowed us rapidly to screen for this mutation. In relatives of the proband, apoE1 Baden was consistently associated with hypertriglyceridemia. Similar to other apoE variants linked to hypertriglyeridemia, the Arg(180)-->Cys mutation is located within the lipid binding domain of apoE. We therefore suggest that apoE1 Baden maycause hypertrigylceridemia, possibly by inhibiting the hydrolysis of triglycerides associated with very low density lipoproteins. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/01/20 alle ore 06:45:27