Altered kinase C function in transformed BALB/c3T3 cells.

H C Yang

doi:10.1016/0014-4827(89)90416-3

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Altered kinase C function in transformed BALB/c3T3 cells.

H C Yang

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Abstract

Comparative studies of kinase C function were performed in an untransformed (A31) and the benzo[a]pyrene (BPA31), dimethylbenz[a]anthracene (DA31), and Kirsten sarcoma virus (KA31) transformed BALB/c 3T3 mouse fibroblast cell lines. The 80-kDa kinase C dependent phosphoprotein (pp80), an in vivo marker of kinase C activity, was markedly decreased in the transformed cells although the amount of the 80-kDa substrate protein in the BPA31 cells was similar to that in the untransformed A31 cells. Total cell lysate kinase C levels were lower in the transformed cells but this difference could not account for the reduced pp80 phosphorylation. Increased affinity of kinase C for the membrane fraction in the BPA31 cells may account for decreased phosphorylation of pp80.

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Animals Cell Line, Transformed Fibroblasts Immunoassay Mice Mice, Inbred BALB C Mitosis Neoplasm Proteins Phosphoproteins Protein Kinase C Synaptosomes Tetradecanoylphorbol Acetate Tumor Cells, Cultured Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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H C Yang. 1989. Altered kinase C function in transformed BALB/c3T3 cells.. https://doi.org/10.1016/0014-4827(89)90416-3

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