Effect of okadaic acid on protein phosphorylation patterns of chicken myogenic cells with special reference to creatine kinase

FEBS Letters

Skarli, M.¹  Wallimann, T.¹  Hemmer, W.¹  Perriard, J.-C.¹ 

[1]Institute for Cell Biology, ETH-Hönggerberg, CH-8093 Zürich, Switzerland

关键词: Phosphorylation of creatine kinase;    Okadaic acid;    Chicken;    Myogenic cell;    B- and M-CK;    refer to brain- and muscle-type creatine kinase isoenzymes;    respectively;    CaM-kinase;    Ca2+/calmodulin-de-pendent protein kinase;    DAG;    diacylglycerol;    dbcAMP;    di-butyryl-3'-5'-cAMP;    OA;    okadaic acid;    OAG;    1-oleoyl-2-acetyl-sn-glycerol;    PCr;    phosphocreatine;    PKA;    cyclic AMP-dependent protein kinase;    PKC;    protein kinase C;    PP1 and PP2A;    type 1 and type 2A phosphatase;    respectively;   

DOI  :  10.1016/0014-5793(93)81034-W

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Okadaic acid and other agents affecting cellular phosphorylation and dephosphorylation processes profoundly changed the phosphoprotein pattern of ³²P_ilabelled chicken embryonic skeletal muscle cells. The phosphorylation states of proteins in the lower molecular weight range were especially increased. Immunoprecipitation of cellular extracts with anti-creatine kinase antibodies enabled us to identify creatine kinase (CK) phosphoproteins. B-CK was phosphorylated after treating the cultures with 1-oleoyl-2-acetyl-sn-glycerol, dibutyryl-cAMP, okadaic acid and combinations thereof, but not with 1,2-dioleoyl-sn-glycerol. M-CK was also shown to be phosphorylated. The results indicated that in vivo, CK isoforms in muscle are subjected to control mediated by phosphorylation and dephosphorylation processes.

【 授权许可】

Unknown