doi: 10.1016/0006-291x(91)90922-t.
Inhibition of protein kinase C by calphostin C is light-dependent
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- PMID: 1708246
- DOI: 10.1016/0006-291x(91)90922-t
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Inhibition of protein kinase C by calphostin C is light-dependent
Biochem Biophys Res Commun.
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Abstract
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. In characterizing the activity of this compound, we unexpectedly found that the inhibition of [3H]phorbol dibutyrate binding was dependent on exposure to light. Ordinary fluorescent light was sufficient for full activation. The inhibition of protein kinase C activity in cell-free systems and intact cells also required light. Light-dependent cytotoxicity was seen at concentrations about 5-fold higher than those inhibiting protein kinase C.
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