Abstract: 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.

Thrombin induces serotonin secretion and aggregation independently of inositol phospholipid hydrolysis and protein phosphorylation in human platelets permeabilized with saponin / M. RUGGIERO;E. G. LAPETINA;J. SILIO. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - STAMPA. - 260(1985), pp. 7078-7083.

Thrombin induces serotonin secretion and aggregation independently of inositol phospholipid hydrolysis and protein phosphorylation in human platelets permeabilized with saponin

RUGGIERO, MARCO;
1985

Abstract

Abstract: 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.
260
7078
7083
M. RUGGIERO;E. G. LAPETINA;J. SILIO
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2158/9937
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