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The protein phosphatase inhibitor, okadaic acid, potentiates the stimulatory effect of phorbol ester on phosphatidylcholine synthesis, but not on phospholipid hydrolysis, in fibroblasts
Author(s) -
Kiss Zoltan
Publication year - 1992
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(92)81295-w
Subject(s) - okadaic acid , phosphatidylcholine , phospholipid , phorbol , chemistry , phosphatase , phosphorylation , biochemistry , hydrolysis , protein kinase c , membrane
The potent protein phosphatase inhibitor, okadaic acid, was used to determine the possible role of protein phosphorylation reaction(s) in phorbol ester‐induced synthesis and hydrolysis of phosphatidylcholine (PtdCho) in NIH 3T3 fibroblasts. Okadaic acid (2μM) was found to enhance the stimulatory effects of lower concentrations (2.5–25 nM) of phorbol 12‐myristate 13‐acetate (PMA) on PtdCho synthesis, but not an PtdCho hydrolysis, after treatments for 30–60 min. These data support a view that in fibroblasts PMA simulates only PtdCho synthesis, and not PtdCho hydrolysis, by a protein phosphorylation‐dependent mechanism.