Highly specific inhibitor of protein kinase C (IC50 = 50 nM); requires light for activation. At higher concentrations (100 nM or greater), it has been shown to inhibit cell proliferation and induce apoptosis in vitro.
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This compound is featured on the Phospholipase D and PKC pages of the Handbook of Receptor Classification and Signal Transduction. To browse other handbook pages, click here.
Potent and specific inhibitors of protein kinase C have been found in streptomyces and fungi: Staurosporine, an alkaloid from Streptomyces sp., is the most potent inhibitor of protein kinases with an IC50 in the nanomolar range. UCN-01 (7-hydroxy staurosporine), isolated
Annals of translational medicine, 10(3), 132-132 (2022-03-15)
The currently available treatment methods are ineffective in reducing mortality or improving outcomes in acute lung injury (ALI). The activation of protein kinase C alpha (PKCα) has recently been implicated in ALI development. We explored the potential therapeutic outcomes of
Protein kinase C (PKC) is a central component in signal transduction and growth control and might be an appropriate target for the chemotherapy of human brain tumors. This study demonstrates that the staurosporine derivative Ro 31-8220, a potent PKC inhibitor
Biochemical and biophysical research communications, 176(1), 288-293 (1991-04-15)
Calphostin C, a secondary metabolite of the fungus Cladosporium cladosporioides, inhibits protein kinase C by competing at the binding site for diacylglycerol and phorbol esters. Calphostin C is a polycyclic hydrocarbon with strong absorbance in the visible and ultraviolet ranges.
Biochemical and biophysical research communications, 159(2), 548-553 (1989-03-15)
Calphostin C (UCN-1028C), a newly isolated compound from Cladosporium cladosporioides, is a potent and specific inhibitor of protein kinase C, because it was 1000 times more inhibitory to protein kinase C (IC50, 0.05 microM) than other protein kinases such as
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