Apolipoprotein A-V N-terminal Domain Lipid Interaction Properties in Vitro Explain the Hypertriglyceridemic Phenotype Associated with Natural Truncation Mutants

• Published in: The Journal of biological chemistry Vol. 284; no. 48; pp. 33369 - 33376
• Main Authors: Wong-Mauldin, Kasuen, Raussens, Vincent, Forte, Trudy M., Ryan, Robert O.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 27.11.2009; American Society for Biochemistry and Molecular Biology
• Subjects: Animals; Apolipoprotein A-V; Apolipoproteins - chemistry; Apolipoproteins - genetics; Apolipoproteins - metabolism; Apolipoproteins A - chemistry; Apolipoproteins A - genetics; Apolipoproteins A - metabolism; Binding Sites; Circular Dichroism; Humans; Hypertriglyceridemia - genetics; Hypertriglyceridemia - metabolism; Hypertriglyceridemia - pathology; Immunoblotting; Kinetics; Lipids and Lipoproteins: Metabolism, Regulation, and Signaling; Lipoproteins, HDL - blood; Lipoproteins, HDL - metabolism; Lipoproteins, VLDL - blood; Lipoproteins, VLDL - metabolism; Male; Mice; Mice, Knockout; Mutation; Phospholipids - metabolism; Protein Binding; Protein Structure, Secondary; Spectrometry, Fluorescence; Spectroscopy, Fourier Transform Infrared

The N-terminal 146 residues of apolipoprotein (apo) A-V adopt a helix bundle conformation in the absence of lipid. Because similarly sized truncation mutants in human subjects correlate with severe hypertriglyceridemia, the lipid binding properties of apoA-V(1–146) were studied. Upon incubation with...