Abstract
The presence of tumor-promoting phorbol ester receptors in rat prostate was investigated by studying the binding of phorbol diester 12,13-dibutyrate (PDBu) in both soluble and particulate subcellular fractions. Binding of [ 3H]PDBu to the soluble fraction was optimal after the addition of phosphatidylserine (0.1 mg/ml) and Ca 2+ (1 mM). Both subcellular fractions exhibited a single class of PDBu receptor (K d between 97 and 128 nM) as shown by saturation binding experiments. Phorbol esters with tumor-promoting activity showed a higher affinity for these receptors than did endogenous ligands such as diacyglycerols whereas phorbol esters without tumor-promoting activity were ineffective even at concentrations as high as 1 μM. These properties are highly representative of protein kinase C activity.
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