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

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)229-233
Number of pages5
JournalFEBS Letters
Volume339
Issue number3
DOIs
Publication statusPublished - 1994 Feb 21

Keywords

  • Anti-idiotypic antibody
  • Anti-phospholipid antibody
  • Diacylglycerol
  • Lipid-protein interaction
  • Phosphatidylserine
  • Protein kinase C

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Anti-idiotypic monoclonal antibody recognizes a consensus recognition site for phosphatidylserine in phosphatidylserine-specific monoclonal antibody and protein kinase C'. Together they form a unique fingerprint.

Cite this