Hemmer W, Skarli M, Perriard J C, Wallimann T
Institute for Cell Biology, ETH-Hönggerberg, Zürich, Switzerland.
FEBS Lett. 1993 Jul 19;327(1):35-40. doi: 10.1016/0014-5793(93)81034-w.
Okadaic acid and other agents affecting cellular phosphorylation and dephosphorylation processes profoundly changed the phosphoprotein pattern of 32Pi-labelled 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, okadiac 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.
冈田酸和其他影响细胞磷酸化和去磷酸化过程的试剂深刻改变了用³²Pi标记的鸡胚骨骼肌细胞的磷蛋白模式。较低分子量范围内蛋白质的磷酸化状态尤其增加。用抗肌酸激酶抗体对细胞提取物进行免疫沉淀，使我们能够鉴定肌酸激酶（CK）磷蛋白。在用1-油酰基-2-乙酰基-sn-甘油、二丁酰-cAMP、冈田酸及其组合处理培养物后，B-CK发生了磷酸化，但用1,2-二油酰基-sn-甘油处理则未发生磷酸化。M-CK也被证明发生了磷酸化。结果表明，在体内，肌肉中的CK同工型受到磷酸化和去磷酸化过程介导的调控。
