apyrase and daidzein

apyrase has been researched along with daidzein* in 1 studies

Other Studies

1 other study(ies) available for apyrase and daidzein

Article	Year
The tyrosine kinase inhibitors, genistein and methyl 2,5-dihydroxycinnamate, inhibit the release of (3H)arachidonate from human platelets stimulated by thrombin or collagen. Thrombosis and haemostasis, 1994, Volume: 72, Issue:4 We have investigated the effects of the tyrosine kinase inhibitors, genistein and methyl 2,5-dihydroxycinnamate, on [3H]arachidonic acid release from human platelets. Both tyrosine kinase inhibitors blocked, in a dose-dependent manner, the release of arachidonic acid stimulated by thrombin or suspensions of collagen fibres. Blockade by the tyrosine kinase inhibitors occurred early in the arachidonate release time course. Both genistein and methyl 2,5-dihydroxycinnamate also inhibited tyrosine phosphorylation in platelets. The inhibitors were specific in that they did not affect protein kinase C activity, ATP levels or mobilization of Ca2+ from internal stores. These findings suggest a role for tyrosine kinase activity in the regulation of phospholipase A2 in platelets stimulated by the physiological ligands, thrombin and collagen. Topics: Adenosine Triphosphate; Apyrase; Arachidonic Acid; Blood Platelets; Calcium; Cinnamates; Collagen; Enzyme Activation; Genistein; Humans; Indomethacin; Isoflavones; Phosphorylation; Protein Kinase C; Protein Processing, Post-Translational; Protein-Tyrosine Kinases; Signal Transduction; Tetradecanoylphorbol Acetate; Thrombin	1994

Article

Year

The tyrosine kinase inhibitors, genistein and methyl 2,5-dihydroxycinnamate, inhibit the release of (3H)arachidonate from human platelets stimulated by thrombin or collagen.

Thrombosis and haemostasis, 1994, Volume: 72, Issue:4

We have investigated the effects of the tyrosine kinase inhibitors, genistein and methyl 2,5-dihydroxycinnamate, on [3H]arachidonic acid release from human platelets. Both tyrosine kinase inhibitors blocked, in a dose-dependent manner, the release of arachidonic acid stimulated by thrombin or suspensions of collagen fibres. Blockade by the tyrosine kinase inhibitors occurred early in the arachidonate release time course. Both genistein and methyl 2,5-dihydroxycinnamate also inhibited tyrosine phosphorylation in platelets. The inhibitors were specific in that they did not affect protein kinase C activity, ATP levels or mobilization of Ca2+ from internal stores. These findings suggest a role for tyrosine kinase activity in the regulation of phospholipase A2 in platelets stimulated by the physiological ligands, thrombin and collagen.

Topics: Adenosine Triphosphate; Apyrase; Arachidonic Acid; Blood Platelets; Calcium; Cinnamates; Collagen; Enzyme Activation; Genistein; Humans; Indomethacin; Isoflavones; Phosphorylation; Protein Kinase C; Protein Processing, Post-Translational; Protein-Tyrosine Kinases; Signal Transduction; Tetradecanoylphorbol Acetate; Thrombin

1994