Abstract

Abstract In order to study the signal transduction mechanism of human endothelial cells (EC), the regulation of superoxide anion (O 2 − ) release in EC has been investigated using the calcium ionophore A23187 and phorbol myristate acetate (PMA), a potential activator of the Ca 2+ activated, phospholipid‐dependent protein kinase, designated “protein kinase C.” PMA enhanced O 2 − release from EC, and this enhancement occurred regardless of the presence or absence of extracellular Ca 2+ . A similar increase was produced by A23187; omission of extracellular Ca 2+ prevented this increase. Simultaneous stimulation with PMA and A23187 produced a large increase in O 2 − release at submaximal concentrations of these agents, which, when added separately, caused minimal effects. These findings indicate that the activation of protein kinase C and mobilization of Ca 2+ evoked by PMA and A23187 respectively are synergistically effective for eliciting a full physiological response of EC in the generation and release of O 2 − .

Keywords

IonophoreProtein kinase CExtracellularCalciumSuperoxideChemistryActivator (genetics)PhorbolStimulationBiochemistryProtein kinase AKinaseBiophysicsEndocrinologyBiologyEnzymeReceptor

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Publication Info

Year
1986
Type
article
Volume
127
Issue
2
Pages
207-210
Citations
165
Access
Closed

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Tsukasa Matsubara, Morris Ziff (1986). Superoxide anion release by human endothelial cells: Synergism between a phorbol ester and a calcium ionophore. Journal of Cellular Physiology , 127 (2) , 207-210. https://doi.org/10.1002/jcp.1041270203

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DOI
10.1002/jcp.1041270203