Home
Resources
Publications
Inhibition of Protein Kinase C by Calphostin C Is Light-Dependent

Inhibition of Protein Kinase C by Calphostin C Is Light-Dependent

R F Bruns, F D Miller, R L Merriman, J J Howbert, W F Heath, E Kobayashi, I Takahashi, T Tamaoki, H Nakano

Biochem Biophys Res Commun. 1991 Apr 15;176(1):288-93.

PMID: 1708246

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP121263192-A	Calphostin C from Cladosporium cladosporioides		121263-19-2	Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: