Separation of different receptor-mediated effects of a prostaglandin H sub(2) analogue (U46619) on human platelets by means of human granulocytic elastase and chymotrypsin

Previous investigations indicated two classes of thromboxane A sub(2)/prostaglandin H sub(2) (TXA sub(2)/PGH sub(2)) receptors on human platelets and suggested that shape change and myosin light chain phosphorylation correlated with the occupancy of high affinity receptors while serotonin release wa...

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Veröffentlicht in:Biochemical pharmacology 1989-01, Vol.38 (19), p.3213-3217
Hauptverfasser: Lukasiewicz, H, Peng, Man-Ling, Morinelli, T A, Eckardt, A, Kirby, E P, Niewiarowski, S
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Sprache:eng
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Zusammenfassung:Previous investigations indicated two classes of thromboxane A sub(2)/prostaglandin H sub(2) (TXA sub(2)/PGH sub(2)) receptors on human platelets and suggested that shape change and myosin light chain phosphorylation correlated with the occupancy of high affinity receptors while serotonin release was related to a putative low affinity binding component. The current study shows that chymotrypsin destroyed three receptor-mediated responses of platelets to U46619 (a TXA sub(2)/PGH sub(2) agonist), i.e. shape change, myosin light chain phosphorylation and serotonin release. Human granulocyte elastase selectively inactivated platelet ability to release serotonin following stimulation with U46619, but it did not affect significantly shape change and myosin light chain phosphorylation. In conclusion, it is possible to separate different receptor-mediated effects of U46619 on human platelets by means of human granulocytic elastase and chymotrypsin.
ISSN:0006-2952