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Effect of okadaic acid on protein phosphorylation patterns of chicken myogenic cells with special reference to creatine kinase
Author(s) -
Hemmer W.,
Skarli M.,
Perriard J.-C.,
Wallimann T.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81034-w
Subject(s) - okadaic acid , dephosphorylation , phosphorylation , phosphoprotein , kinase , creatine kinase , skeletal muscle , biochemistry , immunoprecipitation , phosphatase , protein kinase a , protein phosphorylation , biology , microbiology and biotechnology , chemistry , endocrinology , gene
Okadaic acid and other agents affecting cellular phosphorylation and dephosphorylation processes profoundly changed the phosphoprotein pattern of 32 P i 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, 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.