NDLI: Disruption of the C-terminal helix by single amino acid deletion is directly responsible for impaired cholesterol efflux ability of apolipoprotein A-I Nichinan.

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Disruption of the C-terminal helix by single amino acid deletion is directly responsible for impaired cholesterol efflux ability of apolipoprotein A-I Nichinan.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kono, Momoe Tanaka, Toshitaka Tanaka, Masafumi Vedhachalam, Charulatha Chetty, Palaniappan S. Nguyen, David Dhanasekaran, Padmaja Lund-Katz, Sissel Phillips, Michael C. Saito, Hiroyuki
Description	Country affiliation: Japan Author Affiliation: Kono M ( Department of Biophysical Chemistry, Kobe Pharmaceutical University, Kobe, Japan.)
Abstract	Apolipoprotein A-I (apoA-I) Nichinan, a naturally occurring variant with DeltaE235 in the C terminus, is associated with low plasma HDL levels. Here, we investigated the tertiary structure, lipid-binding properties, and ability to induce cellular cholesterol efflux of apoA-I Nichinan and its C-terminal peptide. Thermal and chemical denaturation experiments demonstrated that the DeltaE235 mutation decreased the protein stability compared with wild type (WT). ApoA-I Nichinan exhibited capabilities to bind to or solubilize lipid vesicles that are intermediate to that of WT and a L230P/L233P/Y236P variant in which the C-terminal alpha-helix folding is completely disrupted and forms relatively larger and unstable discoidal complexes, indicating that perturbation of the C-terminal alpha-helical structure by the DeltaE235 mutation leads to reduced lipid binding. Supporting this, apoA-I 209-241/DeltaE235 peptide showed significantly decreased ability to form alpha-helix both in the lipid-free and lipid-bound states, and reduced efficiency to solubilize vesicles. In addition, both apoA-I Nichinan and its C-terminal peptide exhibited reduced activity in ABCA1-mediated cellular cholesterol efflux. Thus, the disruption of the ability of the C-terminal region to form alpha-helix caused by the E235 deletion appears to be the important determinant of impaired lipid binding and cholesterol efflux ability and, consequently, the low plasma HDL levels of apoA-I Nichinan probands.
File Format	HTM / HTML
ISSN	00222275
e-ISSN	15397262
DOI	10.1194/jlr.M002113
Journal	The Journal of Lipid Research
Issue Number	4
Volume Number	51
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2010-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Biochemistry Apolipoprotein A-i Genetics Metabolism Cholesterol Atp Binding Cassette Transporter 1 Atp-binding Cassette Transporters Amino Acid Sequence Animals Chemistry Cell Line Circular Dichroism Cricetinae Hot Temperature Hydrophobic And Hydrophilic Interactions Mice Mutagenesis, Site-directed Mutant Proteins Peptide Fragments Protein Binding Protein Denaturation Protein Stability Protein Structure, Secondary Protein Structure, Tertiary Time Factors Unilamellar Liposomes Comparative Study Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Endocrinology

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Disruption of the C-terminal helix by single amino acid deletion is directly responsible for impaired cholesterol efflux ability of apolipoprotein A-I Nichinan

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Disruption of the C-terminal helix by single amino acid deletion is directly responsible for impaired cholesterol efflux ability of apolipoprotein A-I Nichinan.

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