Phorbol esters have a dual action through protein kinase C in regulation of proliferation of FRTL‐5 cells

FEBS Letters

Miyai, Kiyoshi¹  Amino, Nobuyuki¹  Takada, Kaoru¹  Tetsumoto, Toru¹ 

[1] Department of Laboratory Medicine, Osaka University Medical School, 1-1-50 Fukushima, Fukushima-ku, Osaka 553, Japan

关键词: Cell proliferation;    Cell cycle;    Phorbol ester;    Protein kinase C;    (FRTL-5 cell);    PMA;    phorbol-12-myristate-13-acetate;    TSH;    thyrotropin;    Bt2cAMP;    dibutyryl cyclic AMP;    OAG;    1-oleoyl-2-acetylglycerol;    4α-PDD;    4α-phorbol-12;    13-didecanoate;    PIP2;    phosphatidylinositol 4;    5-bisphosphate;    IP3;    inositol 1;    4;    5-trisphosphate;    DAG;    diacylglycerol;    PDGF;    platelet-derived growth factor;   

DOI  :  10.1016/0014-5793(88)81292-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In quiescent rat thyroid (FRTL-5) cells, phorbol-12-myristate-13-acetate (PMA) inhibited DNA synthesis induced by a combination of insulin and thyrotropin (TSH) or dibutyryl cyclic AMP (Bt₂cAMP). This inhibitory effect of PMA was observed even when PMA was added after addition of these growth factors, and was maximal when PMA was added 2–4 h after the growth factors (late in the G₁-phase of the cell cycle). On the other hand, PMA alone induced DNA synthesis and also enhanced that induced by Bt₂cAMP or insulin in these quiescent cells. 1-Oleoyl-2-acetylglycerol mimicked these effects of PMA, but 4α-phorbol-12,13-didecanoate had no effect. These data demonstrate that in FRTL-5 cells protein kinase C has a stimulatory effect on the G₀ to G₁ transition and an inhibitory effect on the G₁ to S transition in the cell cycle.

【 授权许可】

Unknown