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

FEBS Letters

Umeda, Masato¹  Reza, Farooq¹  Asai, Kenji¹  Inoue, Keizo¹  Tokita, Shigeru¹  Igarashi, Koji¹  Asaoka, Yoshinori²  Aoki, Junken¹ 

[1] Department of Health Chemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan;Biosignal Research Center, Kobe University, Kobe 657, Japan

关键词: Lipid-protein interaction;    Phosphatidylserine;    Protein kinase C;    Anti-phospholipid antibody;    Anti-idiotypic antibody;    Diacylglycerol;    PKC;    protein kinase C;    PS;    phosphatidylserine;    mAb;    monoclonal antibody;    BSA;    bovine serum albumin;   

DOI  :  10.1016/0014-5793(94)80421-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown