Biochemical and Biophysical Research Communications
Regular ArticleRottlerin, a Novel Protein Kinase Inhibitor
Abstract
Rottlerin, a compound from Mallotus philippinensis, is shown to inhibit protein kinases with some specificity for PKC. To some extent, the novel inhibitor is able to differentiate between PKC isoenzymes, with IC50 values for PKCδ of 3-6 μM, PKCα,β,γ of 30-42 μM and PKCϵ,η,ζ of 80-100 μM. Inhibition of PKC appears, at least in part, to be due to a competition between rottlerin and ATP. Among the protein kinases tested, only CaM-kinase III is suppressed by rottlerin as effectively as PKCδ. The chemical structure of rottlerin might serve as a basis for the development of novel inhibitors with improved selectivity for a distinct PKC isoenzyme, such as PKCδ, or for CaM-kinase III.
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Rottlerin impairs early and late steps of Toxoplasma gondii infection in human trophoblast cells and villous explants
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Divergent roles of estrogen receptor subtypes in regulating estrogen-modulated colonic ion transports and epithelial repair
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Rottlerin renders a selective and highly potent CYP2C8 inhibition to impede EET formation for implication in cancer therapy
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Rottlerin promotes anti-metastatic events by ameliorating pharmacological parameters of paclitaxel: An in-vivo investigation in the orthotopic mouse model of breast cancer
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Transient receptor potential melastatin 7 and their modulators
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