A Synthetic Peptide-Based Assay System for Detecting Binding between CD36 and an Oxidized Low-Density Lipoprotein

• TSUZUKI Satoshi

  Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

• TAKAI Marie

  Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

• MATSUNO Yukari

  Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

• KOZAI Yuki

  Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

• FUJIOKA Maiko

  Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

• KAMEI Kozue

  Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

• INAGAKI Hitomi

  Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

• EGUCHI Ai

  Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

• MATSUMURA Shigenobu

  Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

• INOUE Kazuo

  Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

• FUSHIKI Tohru

  Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

抄録

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.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 77 (1), 132-137, 2013

  公益社団法人 日本農芸化学会

キーワード

• CD36
• cell-free assay system
• oxidized low-density lipoprotein/oxidized glycerophospholipids
• specific binding
• synthetic peptide

詳細情報

• CRID: 1390282681455334272
• NII論文ID: 10031164702
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.120625
• COI: 1:STN:280:DC%2BC3s3ntVSqsQ%3D%3D
• ISSN: 13476947
• ISSN: 09168451
• NDL書誌ID: 024226651
• PubMed: 23291771
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I024226651
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.120625
• Web Site: https://search.jamas.or.jp/link/ui/2013228982
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
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