Fig. 3.
Fig. 3. Tyrosine phosphorylation in CRP-stimulated wild-type andfyn−/− platelets. / Murine platelets were treated with 1 mmol/L EGTA and 10 μmol/L indomethacin for these experiments. Antiphosphotyrosine immunoblots show that CRP (1.0 μg/mL)-induced tyrosine phosphorylation of FcRγ chain (A), Syk (B), LAT (C), and PLCγ2 (D) in wild-type andfyn−/− platelets. FcRγ chain was precipitated using GST fusion protein of the tandem SH2 domains of Syk. We were unable to obtain a reprobe for LAT from LAT immunoprecipitations because the antibody could not be readily used for Western blotting for murine platelets. The results are representative of 3 to 5 experiments. Wild-type and knockout samples were obtained from experiments run in parallel. Results shown in each panel in A are from samples resolved on the same gel and are from the same exposure on the same film. This also applies to B-D.

Tyrosine phosphorylation in CRP-stimulated wild-type andfyn−/−platelets.

Murine platelets were treated with 1 mmol/L EGTA and 10 μmol/L indomethacin for these experiments. Antiphosphotyrosine immunoblots show that CRP (1.0 μg/mL)-induced tyrosine phosphorylation of FcRγ chain (A), Syk (B), LAT (C), and PLCγ2 (D) in wild-type andfyn−/−platelets. FcRγ chain was precipitated using GST fusion protein of the tandem SH2 domains of Syk. We were unable to obtain a reprobe for LAT from LAT immunoprecipitations because the antibody could not be readily used for Western blotting for murine platelets. The results are representative of 3 to 5 experiments. Wild-type and knockout samples were obtained from experiments run in parallel. Results shown in each panel in A are from samples resolved on the same gel and are from the same exposure on the same film. This also applies to B-D.

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