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Protein kinase C levels and protein phosphorylation associated with inhibition of proliferation in a murine macrophage tumor

✍ Scribed by Nigel T. Goode; Ian R. Hart

Publisher: John Wiley and Sons
Year: 1990
Tongue: English
Weight: 867 KB
Volume: 142
Category: Article
ISSN: 0021-9541
DOI: 10.1002/jcp.1041420306

No coin nor oath required. For personal study only.

✦ Synopsis

Treatment of M5076 tumor cells with the phorbol esters 12-0-tetradecanoylphorbol 13-acetate (TPA) and phorbol 12,13 dibutyrate (PdBu) inhibited cellular proliferation, whereas 1,2-dioctanoyl-glycerol (DiC8) and 1 -0leoyl2-acetyl-glycerol (OAG) did not affect cell growth. Inhibition uf cellular proliferation in this cell line appears to be a consequence of protein kinase C (PKC) down-regulation since phorbol esters, but not a single application of diacylglycerols (DGs) downregulated cellular PKC levels. By repeated application of DGs, PKC down-regulation was achieved and correlated with inhibition of proliferation. Phorbol esterinduced PKC down-regulation wa5 reversible, upon removal of the phorbol ester, and the reappearance of PKC was associated with resumption of proliferation.

The mitogenic responsiveness of these cells to added serum depended upon cellular PKC levels. Phorbol esters also caused the phosphorylation of two proteins which were not phosphorylated in response to DG treatment. Inhibition of growth of M5076 cells appears to be associated with phosphorylation of two novel proteins and/or PKC down-regulation.

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