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. 2003 May 12;161(3):507–519. doi: 10.1083/jcb.200211104

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Copyright © 2003, The Rockefeller University Press

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Figure 3. — Increased Cn and mitochondrial stress induce nuclear Rel protein levels. Control C2C12 cells were transfected with Cn cDNA or treated with CCCP (25 μM for 2 h) in the presence or absence of added FK506 (10 nM). (A) Nuclear and postnuclear cell fractions (30 μg protein each) were subjected to immunoblot analysis with indicated antibodies. Values in parentheses under each panel show relative band intensities. YY1 and Na⁺/K⁺ ATPase antibodies were used to monitor protein loading and cross-contamination between the two subcellular fractions. (B–E) Gel mobility shift analysis with nuclear extracts from control or transfected C2C12 cells or mtDNA-depleted cells. In B, D, and E, NFκB consensus probe was used, whereas in C ZBP-89 DNA was used as a probe. In B, supershift with indicated antibody (1–2 μl antibody) was performed. Treatment with FK506 and CCCP were as in Fig. 2.

Figure 3. — Increased Cn and mitochondrial stress induce nuclear Rel protein levels. Control C2C12 cells were transfected with Cn cDNA or treated with CCCP (25 μM for 2 h) in the presence or absence of added FK506 (10 nM). (A) Nuclear and postnuclear cell fractions (30 μg protein each) were subjected to immunoblot analysis with indicated antibodies. Values in parentheses under each panel show relative band intensities. YY1 and Na⁺/K⁺ ATPase antibodies were used to monitor protein loading and cross-contamination between the two subcellular fractions. (B–E) Gel mobility shift analysis with nuclear extracts from control or transfected C2C12 cells or mtDNA-depleted cells. In B, D, and E, NFκB consensus probe was used, whereas in C ZBP-89 DNA was used as a probe. In B, supershift with indicated antibody (1–2 μl antibody) was performed. Treatment with FK506 and CCCP were as in Fig. 2.