1,720,965 research outputs found
Cytoskeleton-dependent inhibition of the ADP-ribosyl cyclase activity of CD38 in thrombin-stimulated platelets
No full textAbstractStimulation of human platelets with thrombin caused a 42% inhibition of the ADP-ribosyl cyclase activity of membrane CD38. This effect was mediated by the activation of the platelet thrombin receptor rather than by proteolysis of CD38, and was not due to a different distribution of the synthesised nucleotide or to a reduced accessibility of CD38 to the substrate. The inhibitory effect of thrombin required actin polymerisation and was not observed when interaction of CD38 with the cytoskeleton was prevented by cytochalasin D. Finally, we analysed whether cADPR could play a role as a Ca2+-mobilising agent in human platelets. Using saponin-permeabilised cells, we found that unlike IP3, cADPR did not induce any release of Ca2+ from intracellular stores. These results indicate that the enzymatic activity of membrane CD38 can be modulated by platelet activation, and that the function of this glycoprotein is probably not related to Ca2+ mobilisation
Interaction of CD38 with the platelet cytoskeleton induced by thrombin and modulation of the ADP-ribosyl cyclase activity
No full textRegulation of CD38-mediated production of cADPR by platelet stimulation and cytoskeleton reorganization (PD633)
No full text
Concanavalin A-induced tyrosine phosphorylation of Syk, PLCgamma2 and FAK in platelets: role of glycoprotein IIb-IIIa
No full textClustering of integrin aIIb-b3 differently regulates tyrosine pohsphorylation of pp72syk, PLCg2 and p125FAK in Concanavalin A-stimulated platelets
No full textLysophosphatidic acid induces protein tyrosine phosphorylation in the absence of phospholipase C activation in human platelets
No full textLysophosphatidic acid induces protein tyrosine phosphorilation in the absence of phospholipase C activation in human platelets
No full text
- …
