Phosphorylation of high molecular weight proteins in platelets treated with 12-O-tetradecanoylphorbol-13-acetate.
Changes in the phosphorylation of three high molecular weight cytoskeletal proteins in platelets (actin binding protein, platelet talin and myosin heavy chain) were investigated after treatment with a phorbol ester. All three showed rapid increases in phosphate incorporation, reaching near-maximal values within three minutes. Phosphopeptide maps of the proteins before and after phorbol treatment revealed a single new site in myosin heavy chain, two new peptides in actin binding protein, and multiple sites in talin. These results point to multiple cytoskeletal targets of protein kinase C and suggest complex mechanisms for reorganizing microfilaments.
Litchfield
D W
DW
Department of Biochemistry, University of Western Ontario, London, Canada.
Ball
E H
EH
D001792:Blood Platelets / Q000187:drug effects* / Q000378:metabolism; D001798:Blood Proteins / Q000378:metabolism*; D006801:Humans; D008840:Microfilament Proteins / Q000097:blood; D008970:Molecular Weight; D015879:Myosin Subfragments / Q000097:blood; D010449:Peptide Mapping; D010766:Phosphorylation; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D001798:Blood Proteins; D008840:Microfilament Proteins; D015879:Myosin Subfragments; D013755:Tetradecanoylphorbol Acetate