Inhibition of protein kinase C by tamoxifen.
Article Details
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O'Brian CA, Liskamp RM, Solomon DH, Weinstein IB
Inhibition of protein kinase C by tamoxifen.
Cancer Res. 1985 Jun;45(6):2462-5.
- PubMed ID
- 3157445 [ View in PubMed]
- Abstract
The antiestrogen drug tamoxifen inhibits rat brain protein kinase C in vitro, whether the enzyme is activated by Ca2+ and phospholipid (50% inhibitory dose, 100 microM), 12-O-tetradecanoylphorbol-13-acetate and phospholipid (50% inhibitory dose, 40 microM), or teleocidin and phospholipid. Tamoxifen does not inhibit the Ca2+- and phospholipid-independent phosphorylation of protamine sulfate by protein kinase C, indicating that the drug does not interact with the active site of the enzyme. The binding of [3H]phorbol dibutyrate to high-affinity membrane receptors of cultured mouse fibroblast cells is inhibited by tamoxifen (50% inhibitory dose, 5 microM). Our findings suggest that the growth-inhibitory and cytotoxic effects of tamoxifen, which have been observed at microM concentrations of the drug, may be in part due to its effects on protein kinase C.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Tamoxifen Protein kinase C (Protein Group) Protein group Humans YesInhibitorDetails