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• W137310981 endingPage "164" @default.
• W137310981 startingPage "149" @default.
• W137310981 abstract "Blood platelets possess three types of secretory organelle, namely dense granules that contain serotonin (5-HT), ADP, ATP and Ca2+, α-granules that store a wide variety of proteins, including β-thromboglobulin (βTG), fibrinogen, thrombospondin and various growth factors, and lysosomes that contain acid hydrolases (Zucker and Nachmias, 1985). Secretion of the contents of platelet dense and α-granules in response to stimuli such as thrombin or thromboxane A2 plays an important role in both physiology and pathology, contributing to normal hemostasis and to the development of arterial thrombi. Many studies on the signal transduction pathways that initiate these secretory responses have emphasized the receptor and G protein-dependent activation of phosphoinositide-specific phospholipase C (PLC) and the consequent mobilization of Ga2+ ions by inositol 1,4,5-trisphosphate (IP3) and activation of protein kinase C (PKC) by 1,2-diacylglycerol (DAG) (Nishizuka, 1984; Siess, 1989). However, it is now clear that the process of platelet activation is much more complex than this, involving rapid parallel and sequential changes in the activities of several effector enzymes and ion channels, with many positive and negative feedback loops. As a result, the relative importance of Ca2+ ions and PKC, the contributions made by other factors, and the molecular mechanisms responsible for exocytosis of granule contents have proved difficult to analyse in intact platelets. Several groups have therefore used platelets permeabilized by saponin or by high-voltage electric discharges to study specific aspects of signal transduction and to identify factors involved in the secretion of granule constituents." @default.
• W137310981 created "2016-06-24" @default.
• W137310981 creator A5004394777 @default.
• W137310981 creator A5040132439 @default.
• W137310981 date "1993-01-01" @default.
• W137310981 modified "2023-10-15" @default.
• W137310981 title "Evidence That Activation of Phospholipase D can Mediate Secretion from Permeabilized Platelets" @default.
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• W137310981 doi "https://doi.org/10.1007/978-1-4615-2994-1_11" @default.
• W137310981 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8209783" @default.
• W137310981 hasPublicationYear "1993" @default.
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