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Tamoxifen stimulates phospholipase D activity by an estrogen receptor‐independent mechanism
Author(s) -
Kiss Zoltan
Publication year - 1994
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(94)01200-8
Subject(s) - phospholipase d , tamoxifen , estrogen receptor , antiestrogen , chemistry , phosphatidylethanolamine , phospholipid , phosphatidylcholine , stimulation , endocrinology , medicine , mechanism of action , estrogen , receptor , pharmacology , biochemistry , biology , cancer , signal transduction , breast cancer , in vitro , membrane
The effects of tamoxifen (TAM), a widely used agent in the treatment of breast cancer, were examined on phospholipase D (PLD)‐mediated phospholipid hydrolysis. In drug‐sensitive MCF‐7 human breast carcinoma cells TAM, similar to several well‐established activators of PLD, had no effect on phospholipid hydrolysis. In an estrogen receptor‐deficient multidrug‐resistant subline of MCF‐7 cells, TAM preferentially stimulated the hydrolysis of phosphatidylethanolamine; two‐fold stimulation required 2.5 or 5 μM TAM in the absence or presence of serum, respectively. In NIH 3T3 fibroblasts significant (4‐ to 4.8‐fold) stimulation of phosphatidylethanolamine and phosphatidylcholine hydrolysis in the presence of serum required 10 μM TAM. These data establish that TAM can stimulate PLD activity by an estrogen receptor‐independent mechanism.