Effect of okadaic acid on protein phosphorylation patterns of chicken myogenic cells with special reference to creatine kinase.
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.
Institute for Cell Biology, ETH-Hönggerberg, Zürich, Switzerland.
W
W
Hemmer
M
M
Skarli
J C
JC
Perriard
T
T
Wallimann
D000595:Amino Acid Sequence; D000818:Animals; D002457:Cell Extracts; D002478:Cells, Cultured; D002642:Chick Embryo; D016384:Consensus Sequence; D003402:Creatine Kinase / Q000737:chemistry / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D004988:Ethers, Cyclic / Q000494:pharmacology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D019319:Okadaic Acid; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation / Q000187:drug effects; D011233:Precipitin Tests; D011493:Protein Kinase C / Q000737:chemistry
D002457:Cell Extracts; D004988:Ethers, Cyclic; D010750:Phosphoproteins; D019319:Okadaic Acid; D011493:Protein Kinase C; D003402:Creatine Kinase; D010749:Phosphoprotein Phosphatases