Key result
Thrombin transiently elevated platelet phosphotyrosine content in intact human platelets, causing dramatic changes in tyrosine phosphorylation in three distinct temporal waves.
Why the study?
Does thrombin stimulation alter tyrosine-specific protein phosphorylation in intact human platelets?
Population
Intact human platelets
Comparison
Thrombin stimulation vs Unstimulated state (implied)
Design
Preclinical
Authors
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Thrombin-driven tyrosine phosphorylation may shape platelet signaling; leaves open any clinical relevance for antithrombotic targeting.
Does thrombin stimulation alter tyrosine-specific protein phosphorylation in intact human platelets?
This study demonstrates that thrombin regulates tyrosine-specific protein phosphorylation in human platelets, suggesting the involvement of tyrosine kinases in platelet signal transduction.
Ferrell et al. (1988) studied this question. Thrombin was evaluated on Tyrosine-specific protein phosphorylation. Thrombin transiently elevated platelet phosphotyrosine content in intact human platelets, causing dramatic changes in tyrosine phosphorylation in three distinct temporal waves.
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