Document Detail


A Synthetic Peptide-Based Assay System for Detecting Binding between CD36 and an Oxidized Low-Density Lipoprotein.
MedLine Citation:
PMID:  23291771     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
CD36 is an integral membrane protein that mediates the cellular uptake of oxidized low-density lipoprotein (oxLDL) through recognition of the oxidized glycerophospholipids (oxPLs) formed during LDL oxidation. We aimed to devise an assay system to detect binding between CD36 and oxLDL/oxPL without using recombinant proteins. A peptide corresponding to amino-acid residues 149-168 of mouse CD36 with biotin at its N-terminus (named biotin-CD36(149-168)) and variants of it were synthesized and immobilized onto streptavidin-coated plates. oxLDL labeled with Alexa-Fluor-488 bound specifically and saturably to immobilized biotin-CD36(149-168), but poorly or not at all to the variants, such as that with a scrambled amino-acid sequence. The binding of fluorescence-labeled oxLDL to biotin-CD36(149-168) was inhibited efficiently by an oxPL species, but not by a nonoxidized glycerophospholipid. This assay system using biotin-CD36(149-168) provides a convenient means not only of characterizing binding profiles between CD36 and oxLDL/oxPL but also of finding competitors for the binding.
Authors:
Satoshi Tsuzuki; Marie Takai; Yukari Matsuno; Yuki Kozai; Maiko Fujioka; Kozue Kamei; Hitomi Inagaki; Ai Eguchi; Shigenobu Matsumura; Kazuo Inoue; Tohru Fushiki
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-07
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  -     ISSN:  1347-6947     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-7     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University.
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