Effect of protease inhibitors on TPA-induced platelet aggregation.
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The effect of protease inhibitors on TPA-induced aggregation was studied. Thiol protease inhibitors such as antipain, E-64 or leupeptin which were known to block the activity of neutral protease did not inhibit the aggregation and ATP release stimulated by TPA or by the combination of TPA and A23187 by which each dose neither platelet aggregation nor ATP release did induce. Nafamostat mesilate (FUT-175), a new synthetic serine protease inhibitor, blocked the aggregation and ATP release in the study using platelet rich plasma, but not the ATP release in that of washed platelet suspension, stimulated by TPA or the combination of TPA and A23187. The phosphorylation of platelet 40 K-dalton protein induced by TPA was not inhibited by this agent. To clarify the inhibitory effect on TPA aggregation, the change of Triton X-100 insoluble platelet cytoskeletons was investigated. Enhancement of incorporated myosin heavy chain and fibrinogen to cytoskeletons by TPA was suppressed by FUT-175. The 58 K-dalton and 53 K-dalton protein were insolubilised by this agent, the former was identified the fibrinogen derivatives by immunoblotting method. Permeability of FUT-175 to platelet plasma membrane was examined as anti-hydrolytic activity against trypsin recovered in cytosol fraction with tosyl L-lysine α-naphtyl ester as substrate. When platelets were incubated with 10-4M of FUT-175, about one tenth of the activity was recovered in cytosol fraction.These results suggest that some serine proteases play a role in the formation of contractile cytoskeletons.
- 一般社団法人 日本血栓止血学会の論文
一般社団法人 日本血栓止血学会 | 論文
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