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Phorbol ester stimulates the synthesis of sphingomyelin in NIH 3T3 cells A diminished response in cells transformed with human A‐ raf carrying retrovirus
Author(s) -
Kiss Zoltan,
Rapp Ulf R.,
Anderson Wayne B.
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)80372-7
Subject(s) - sphingomyelin , 3t3 cells , phosphatidylcholine , 12 o tetradecanoylphorbol 13 acetate , phorbol , chemistry , tetradecanoylphorbol acetate , stimulation , microbiology and biotechnology , signal transduction , choline , biochemistry , biology , phorbol ester , protein kinase c , phospholipid , endocrinology , transfection , gene , cholesterol , membrane
The tumor promoter 12‐ O ‐tetradecanoylphorbol‐13‐acetate (TPA) stimulated the synthesis of sphingomyelin (CerPCho) from a [ 14 C]choline‐labelled phosphatidylcholine (PtdCho) pool in NIH 3T3 cells. Maximal stimulation (68%) of CerP‐Cho synthesis, accompanied by an increase (38%) in its cellular content, required only 2 nM TPA. Higher concentrations of TPA (2–100 nM) had progressively less effect on CerPCho synthesis which correlated with increased hydrolysis of precursor PtdCho. In cells transformed with human or mouse A‐ raf carrying retroviruses TPA‐stimulated PtdCho hydrolysis, but not CerPCho synthesis, suggesting independent regulation of these processes by the TPA‐stimulated signal transduction system.