Detail of "64626-32-0"

Reference

Dihomogammalinolenic acid, but not eicosapentaenoic acid, activates washed human platelets

Dihomogammalinolenic acid, but not eicosapentaenoic acid, activates washed human platelets. Siess, Wolfgang; Siegel, Frances L.; Lapetina, Eduardo G. (Dep. Mol. Biol., Wellcome Res. Lab., Research Triangle Park, NC 27709, USA). Biochim. Biophys. Acta, 801(2), 265-76 (English) 1984. CODEN: BBACAQ. ISSN: 0006-3002. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Dihomo-g-linolenic acid (I) [1783-84-2] (2.5-20 mM) added to suspensions of washed human platelets induced platelet shape change and the formation of 1,2-diacylglycerol and phosphatidic acid, indicating the activation of phospholipase C [9001-86-9]. It also stimulated the phosphorylation of a 40 kilodalton protein, indicating the activation of protein kinase C [9026-43-1]. I was converted mainly to 12-hydroxyheptadecadienoic acid [74380-53-3] and to a smaller extent to prostaglandin E1 [745-65-3] and thromboxane B1 [64626-32-0]. Small quantities of the lipoxygenase product 12-hydroxyeicosatrienoic acid [93347-66-1] were also obsd. Indomethacin, by blocking platelet cyclooxygenase, prevented the activation of phospholipase C, protein kinase C, and platelet shape change induced by I. Compd. UK 38485, a specific thromboxane synthetase inhibitor, did not block platelet activation induced by I. Thus, endoperoxides derived from I, such as prostaglandin G1 or prostaglandin H1, may be responsible for the stimulation of phospholipase C and protein kinase C, and for the induction of platelet shape change. Eicosapentaenoic acid (II) [10417-94-4] did not activate platelets and was poorly metabolized by platelet cyclooxygenase and lipoxygenase. II was a better inhibitor of platelet activation induced by various agonists in washed platelets than I. I and II were, however, equally effective in inhibiting aggregation induced by collagen in platelet-rich plasma. Thus II might be a better antithrombotic agent than I.