Structural and functional properties of apolipoprotein A-I mutants.
J Atheroscler Thromb
; 7(2): 67-70, 2000.
Article
em En
| MEDLINE
| ID: mdl-11426584
ABSTRACT
Apolipoprotein (apo) A-I is composed of 243 amino acid residues that fold into amphipathic helixes, and plays a central role in the high density lipoprotein (HDL) metabolism. Familial apoA-I deficiency is a rare metabolic disorder of which three cases have been characterized at a molecular level in western Japan. However, in subjects with apoA-I deficiency, coronary artery disease was not always present. One apo A-I deficiency was compound heterozygous apoA-I mutant for a TATA box mutation and a structural nonsense mutation. To date, screening analysis in our laboratory has identified nine genetically-determined structural mutations of apo A-I. We have also characterized these apo A-I mutations, including apoA-I (Glu235del) Nichinan. Few structural mutations were associated with altered HDL cholesterol levels.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Apolipoproteína A-I
/
Mutação
Limite:
Female
/
Humans
/
Male
País/Região como assunto:
Asia
Idioma:
En
Revista:
J Atheroscler Thromb
Ano de publicação:
2000
Tipo de documento:
Article