Unsaturated long-chain fatty acids inhibit the binding of oxidized low-density lipoproteins to a model CD36. Issue 2 (1st February 2014)

• Record Type: Journal Article
• Authors: Takai, Marie; Kozai, Yuki; Tsuzuki, Satoshi; Matsuno, Yukari; Fujioka, Maiko; Kamei, Kozue; Inagaki, Hitomi; Eguchi, Ai; Matsumura, Shigenobu; Inoue, Kazuo; Fushiki, Tohru
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 78:Issue 2(2014)
• Page Start: 238
• Page End: 244
• Publication Date: 2014-02-01
• Subjects: binding inhibition -- CD36 -- long-chain fatty acids -- oxidized low-density lipoproteins -- synthetic peptide; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1080/09168451.2014.882750
• Languages: English
• ISSNs: 0916-8451

Abstract

Abstract: Transmembrane protein CD36 binds multiple ligands, including oxidized low-density lipoproteins (oxLDLs) and long-chain fatty acids (LCFAs). Our aim was to determine whether LCFAs compete with oxLDLs for binding to CD36. We addressed this issue by examining the inhibitory effect of LCFAs against the binding of Alexa-fluor-labeled oxLDLs (AFL-oxLDL) to a synthetic peptide representing the oxLDL-binding site on CD36 (3S-CD36150–168 ). All of the unsaturated LCFAs tested, inhibited the binding of AFL-oxLDL to 3S-CD36150–168, albeit to varying degrees. For instance, the concentrations required for 50% inhibition of binding for oleic, linoleic, and α-linolenic acids were 0.25, 0.97, and 1.2 mM, respectively. None of the saturated LCFAs tested (e.g. stearic acid) exhibited inhibitory effects. These results suggest that at least unsaturated LCFAs can compete with oxLDLs for binding to CD36. The study also provides information on the structural requirements of LCFAs for inhibition of oxLDLs–CD36 binding. Graphical abstract: : Unsaturated long-chain fatty acids but not saturated ones compete with Alexa-Fluor-labeled oxidized low-density lipoproteins for binding to a synthetic CD36 peptide.