Anti-idiotypic monoclonal antibody recognizes a consensus recognition site for phosphatidylserine in phosphatidylserine-specific monoclonal antibody and protein kinase C

Farooq Reza, Koji Igarashi, Shigeru Tokita, Kenji Asai, Junken Aoki, Yoshinori Asaoka, Masato Umeda, Keizo Inoue

研究成果: Article査読

12 被引用数 (Scopus)

抄録

In order to elucidate the molecular mechanisms responsible for the specific lipid-protein interactions, we have undertaken structural and idiotypic analyses of a monoclonal antibody, PS4A7, which binds specifically to phosphatidylserine (PS). Here we showed that one of the anti-idiotypic monoclonal antibodies raised against PS4A7 cross-reacted extensively with protein kinase C (PKC) and inhibited the activation of the enzymatic activity. The binding of the anti-idiotypic antibody to PKC was inhibited specifically by PS, but not by other phospholipids including 1,2-diacyl-sn-glycero -3-phospho-d-serine or 1,2-diacyl-sn-glycero-3-phospho-l-homoserine. In contrast, the binding of the anti-idiotypic mAb to the enzyme was significantly enhanced in the presence of either diacylglycerol or sphingosine. These findings indicate that the PS-specific monoclonal antibody and PKC share a consensus structure which is responsible for the specific interaction with PS and both diacylglycerol and sphingosine may induce a similar conformational change which exposes the PS-specific binding site of the enzyme.

本文言語English
ページ(範囲)229-233
ページ数5
ジャーナルFEBS Letters
339
3
DOI
出版ステータスPublished - 1994 2 21

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

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