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Phosphorylation of a gelatin‐binding protein from L6 myoblasts by protein kinase C
Author(s) -
Cates G.A.,
Litchfield D.W.,
Narindrasorasak S.,
Nandan D.,
Ball E.H.,
Sanwal B.D.
Publication year - 1987
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(87)81045-1
Subject(s) - phosphorylation , chemistry , gelatin , protein kinase a , cgmp dependent protein kinase , protein phosphorylation , microbiology and biotechnology , kinase , biochemistry , mitogen activated protein kinase kinase , biology
A gelatin‐binding glycoprotein from L6 rat myoblasts, designated gp46, was shown to be phosphorylated in vivo. This phosphorylation was increased slightly (18%) by phorbol ester treatment of L6 suggesting protein kinase C involvement. Purified gp46 could be phosphorylated in vitro with protein kinase C, but not by the catalytic subunit of cAMP‐dependent protein kinase. Comparison of the phosphotryptic peptide maps of in vitro and in vivo labeled gp46 suggested that in vivo phosphorylation of gp46 may be mediated by protein kinase C.