title: Structural and functional properties of apolipoprotein A-I mutants.
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.
authors: Department of Internal Medicine, Fukuoka University School of Medicine, Japan. jsasaki@cis.fukuoka-u.ac.jp
authors: J
authors: J
authors: Sasaki
authors: A
authors: A
authors: Matsunaga
authors: W
authors: W
authors: Huang
authors: H
authors: H
authors: Han
authors: W
authors: W
authors: Li
authors: M
authors: M
authors: Kugi
authors: T
authors: T
authors: Koga
mesh_terms: D016632:Apolipoprotein A-I / Q000172:deficiency / Q000235:genetics* / Q000378:metabolism*; D005260:Female; D006579:Heterozygote; D006801:Humans; D007564:Japan; D008297:Male; D009154:Mutation; D016385:TATA Box
chemical_list: D016632:Apolipoprotein A-I