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Phorbol esters have a dual action through protein kinase C in regulation of proliferation of FRTL‐5 cells
Author(s) -
Takada Kaoru,
Amino Nobuyuki,
Tetsumoto Toru,
Miyai Kiyoshi
Publication year - 1988
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(88)81292-4
Subject(s) - protein kinase c , phorbol ester , chemistry , protein kinase a , microbiology and biotechnology , cell growth , dual (grammatical number) , kinase , biochemistry , biology , art , literature
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 (Bt 2 cAMP). 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 G 1 ‐phase of the cell cycle). On the other hand, PMA alone induced DNA synthesis and also enhanced that induced by Bt 2 cAMP 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 G 0 to G 1 transition and an inhibitory effect on the G 1 to S transition in the cell cycle.