This study demonstrates that thrombin can induce platelet activation independently of second messengers derived from phospholipase C-induced inositol phospholipid breakdown in permeabilized platelets.
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May indicate PLC-independent thrombin effects in platelets; leaves open relevance to intact human systems and clinical translation.
We have observed that the addition of Ca2+ to platelets, permeabilized with saponin, promotes a drastic dephosphorylation of proteins and polyphosphoinositides without inducing platelet responses. Subsequent addition of thrombin could promote secretion of serotonin and aggregation in the absence of phospholipase C-induced breakdown of the inositol phospholipids and protein phosphorylation. This information indicates that activation of saponized platelets by thrombin is independent of the formation of second messengers derived from the phospholipase C-induced breakdown of the inositol phospholipids. The implications of this result for intact platelets are discussed.
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Lapetina et al. (1985) studied this question.
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