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Membrane-phorbol ester interactions monitored by circular dichroism.

F Frézard·A Garnier-Suillerot·J Bolard·M Castagna
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Abstract

The interaction of phorbol 12,13-dibutyrate (PDBu), 12-O-retinoylphorbol 13-acetate (RPA) and 12-O-tetradecanoylphorbol 13-acetate (TPA) with L-alpha-phosphatidylserine-containing small unilamellar vesicles or erythrocyte ghosts was monitored by circular dichroism (CD). No change in the CD spectra of PDBu was observed upon binding, while RPA and TPA spectra were slowly affected by the interaction. The changes in RPA and TPA spectra were assigned to the embedding of these molecules in the membrane bilayers. In the presence of 10(8) cells/ml, after one minute incubation, about 2 to 5% of the amount of phorbol ester added is embedded in the membrane. It is suggested that either phorbol esters entering the membrane is not a prerequisite for protein kinase C activation or the amount of phorbol esters necessary to activate protein kinase C is very small.

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Circular DichroismEnzyme ActivationErythrocyte MembraneHumansLiposomesPhorbol 12,13-DibutyratePhorbol EstersPhosphatidylserinesProtein Kinase CSpectrum AnalysisTetradecanoylphorbol AcetateComparative StudyJournal ArticleResearch Support, Non-U.S. Gov't

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F Frézard, A Garnier-Suillerot, J Bolard, M Castagna. 1989-03-13. Membrane-phorbol ester interactions monitored by circular dichroism.. https://doi.org/10.1016/0005-2736(89)90251-4

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