In order to study the signal transduction mechanism of human endothelial cells (EC), the regulation of superoxide anion (02-)release in EC has been investigated using the calcium ionophore A23187 and phorbol myristate acetate (PMA), a potential activator of the Ca2+ activated, phospholipid-dependent
Bradykinin induces superoxide anion release from human endothelial cells
β Scribed by James A. Holland; Kirkwood A. Pritchard; Miguel A. Pappolla; Michael S. Wolin; Nancy J. Rogers; Michael B. Stemerman
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 541 KB
- Volume
- 143
- Category
- Article
- ISSN
- 0021-9541
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β¦ Synopsis
Abstract
The timeβdependent release of superoxide anion (O) from bradykinin (Bk)βstimulated human umbilical vein endothelial cells (EC) was measured as the superoxide dismutaseβinhibitable reduction of ferricytochrome C employing a novel application of microspectrophotometry. In the absence of Bk, O release by EC was not detectable. EC exposure to Bk (10^β6^ to 10^β5^ M) resulted in a rapid release of O. The release of O occurred within 5 minutes of exposure. O release was partially inhibited by indomethacin (63 Β± 6%), thus suggesting that arachidonic acid metabolism, through cyclooxygenase, contributes to EC O production. EC O release may be an important component in the pathophysiologic actions of Bk on vascular function.
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