Figure 3.
Figure 3. Platelet adhesion to dA1VWF induces tyrosine phosphorylation. Human platelets adherent to dA1VWF or incubated over a BSA matrix were lysed and analyzed by Western blotting as described in “Materials and methods.” (A) Platelets adherent to dA1VWF (dA1) or incubated over BSA for 10 or 20 minutes were lysed, and lysates were then probed with antiphosphotyrosine antibodies. Membranes were reprobed for Syk. (B) Platelets were allowed to adhere to dA1VWF with or without 5 μM PP2 or PP3. Then lysates (LYS) were immunoprecipitated with an antibody to ADAP and probed for phosphotyrosine. (C) The effect of PP2, EDTA, and 1 μM BAPTA-AM on tyrosine phosphorylation of ADAP. Data represent ADAP phosphotyrosine band intensities, determined by densitometry, and are expressed relative to results obtained in the absence of inhibitor. Data represent means ± SEM of 3 experiments.

Platelet adhesion to dA1VWF induces tyrosine phosphorylation. Human platelets adherent to dA1VWF or incubated over a BSA matrix were lysed and analyzed by Western blotting as described in “Materials and methods.” (A) Platelets adherent to dA1VWF (dA1) or incubated over BSA for 10 or 20 minutes were lysed, and lysates were then probed with antiphosphotyrosine antibodies. Membranes were reprobed for Syk. (B) Platelets were allowed to adhere to dA1VWF with or without 5 μM PP2 or PP3. Then lysates (LYS) were immunoprecipitated with an antibody to ADAP and probed for phosphotyrosine. (C) The effect of PP2, EDTA, and 1 μM BAPTA-AM on tyrosine phosphorylation of ADAP. Data represent ADAP phosphotyrosine band intensities, determined by densitometry, and are expressed relative to results obtained in the absence of inhibitor. Data represent means ± SEM of 3 experiments.

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