FKBP, THE BINDING-PROTEIN FOR THE IMMUNOSUPPRESSIVE DRUG, FK-506, IS NOT AN INHIBITOR OF PROTEIN-KINASE-C ACTIVITY

被引：9

作者：

CRYAN, J ^{[1
]}

HUNG, SHY ^{[1
]}

WIEDERRECHT, G ^{[1
]}

SIGAL, NH ^{[1
]}

SIEKIERKA, JJ ^{[1
]}

机构：

[1] MERCK SHARP & DOHME LTD,DEPT IMMUNOL RES,POB 2000,W POINT,PA 19486

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 180卷 / 02期

关键词：

D O I：

10.1016/S0006-291X(05)81142-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recently, the amino acid sequence of a 12 Kd endogenous protein inhibitor of protein kinase C (PKC-I 2) has been shown to be identical to that of the 12 KDa receptor for the immunosuppressive drug, FK-506. In view of this observation we examined the effects of recombinant and native human FKBP on protein kinase C (PKC) activity. FKBP, at molar concentrations up to 1900-fold over that of PKC, failed to inhibit PKC phosphorylation of histone H1 and failed to block the auto-phosphorylation of PKC. Interestingly, FKBP is phosphorylated by PKC in these reactions. The phosphorylation of FKBP by PKC appears to be specific since the catalytic subunit of cAMP-dependent protein kinase fails to phosphorylate the binding protein. Our results fail to support a role for FKBP as an inhibitor of protein kinase C. © 1991 Academic Press, Inc.

引用

页码：846 / 852

页数：7

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