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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Reza F,Igarashi K,Tokita S,Asai K,Aoki J,Asaoka Y,Umeda M,Inoue Kdoi
10.1016/0014-5793(94)80421-4subject
Has Abstractpub_date
1994-02-21 00:00:00pages
229-33issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(94)80421-4journal_volume
339pub_type
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