Figure 7
Figure 7. LXR-β interacts with Syk, PLC-γ2, and PPAR-γ. Platelets (8 × 108 cells/mL) pretreated with GW3965 or 15d-PGJ2 (5-30μM) or DMSO (0.08% volume/volume) for 10 minutes and stimulated with collagen (50 μg/mL) for 90 seconds in the presence of ethyleneglycoltetraacetic acid (10μM), indomethacin (10μM), and apyrase (2 U/mL). LXR-β was immunoprecipitated from lysates separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotted with anti-Syk, anti-PLC-γ2 (A) or anti-PPAR-γ (B) antibodies. Membranes were stripped and reblotted for LXR-β. Band intensities were quantified from 3 separate experiments and normalized for LXR-β loading. Numerical data represent the percentage increase in the associations of LXR with Syk (Aii), PLC-γ2 (Aiii), or PPAR-γ (Bi), where 0% association was defined as the level of association in the untreated samples. *P < .05. **P < .01.

LXR-β interacts with Syk, PLC-γ2, and PPAR-γ. Platelets (8 × 108 cells/mL) pretreated with GW3965 or 15d-PGJ2 (5-30μM) or DMSO (0.08% volume/volume) for 10 minutes and stimulated with collagen (50 μg/mL) for 90 seconds in the presence of ethyleneglycoltetraacetic acid (10μM), indomethacin (10μM), and apyrase (2 U/mL). LXR-β was immunoprecipitated from lysates separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotted with anti-Syk, anti-PLC-γ2 (A) or anti-PPAR-γ (B) antibodies. Membranes were stripped and reblotted for LXR-β. Band intensities were quantified from 3 separate experiments and normalized for LXR-β loading. Numerical data represent the percentage increase in the associations of LXR with Syk (Aii), PLC-γ2 (Aiii), or PPAR-γ (Bi), where 0% association was defined as the level of association in the untreated samples. *P < .05. **P < .01.

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