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. 2010 Mar 19;9(7):1461–1475. doi: 10.1074/mcp.M900548-MCP200

Fig. 5.

Fig. 5.

Activation of caspase-3 in Dhcr7Δ3–5/Δ3–5 and Sc5d−/− embryonic brain tissues. A, representative regions from the 2-DE gels demonstrating differential expression of protein spot 39, which was subsequently identified as caspase-3 precursor. B, Western blot analysis of pooled protein samples (20 μg) with anti-caspase-3 showed increased cleaved caspase-3 in Dhcr7Δ3–5/Δ3–5 and Sc5d−/− brain tissues. C, Western blot analysis of caspase-3 from five independent Dhcr7+/+ or Dhcr7Δ3–5/Δ3–5 brain tissue protein samples (20 μg) confirmed increased cleaved caspase-3 (mean ± S.D.; n = 5; *, p < 0.05). D, Western blot analysis of caspase-3 from five independent Sc5d+/+ or Sc5d−/− brain tissue protein samples (20 μg) confirmed increased cleaved caspase-3 (mean ± S.D.; n = 5; **, p < 0.01). Band intensity was normalized to that of actin. Error bars indicate the S.D. calculated from five individual samples. E, Western blot analysis showed that cleaved caspase-3 increased both in DSF and in DRM of Dhcr7Δ3–5/Δ3–5 brain tissue. Transferrin receptor and clathrin heavy chain were used as marker proteins for DSF and DRM, respectively.

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