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. Author manuscript; available in PMC: 2013 Oct 9.
Published in final edited form as: Biochim Biophys Acta. 2012 Feb 9;1823(4):889–899. doi: 10.1016/j.bbamcr.2012.01.017

Fig. 6.

Fig. 6

Role of HIF-1α for down-regulation of hMSH3 by hypoxia. A: Stabilization of the HIF-1α protein in SW620 and HCT116+5 cells by hypoxia. Cells were cultured for 0, 1, 2, and 3 days in hypoxia and the amount of HIF-1α was monitored by Western blot analysis with anti HIF-1α antibody. α-Tubulin was used as a loading control. B: HIF-1α knockdown by siRNA. Cells were transfected with a negative control (ctr) oligomer or an HIF-1α siRNA (HIF) oligomer and cultured under hypoxia for the indicated days. The amount of HIF-1α was compared between hypoxic cells transfected with a negative control (ctr) oligomer and the HIF-1α siRNA (HIF) oligomer after normalization by α-tubulin signals. C: Effect of HIF-1α knockdown on hypoxia-induced down-regulation of hMSH3 mRNA. HCT116+5 and SW620 transfected with a negative control (ctr) oligomer (open bars) and an HIF-1α specific siRNA oligomer (closed bars) were cultured in hypoxia for the indicated number of days. The amount of hMSH3 mRNA was compared between the cells transfected with ctr and HIF siRNA. *, P<0.01; **, P<0.05. D: Effect of HIF-1α knockdown on hypoxia-induced down-regulation of hMSH3 protein. HCT116+5 and SW620 transfected with a negative control (ctr) oligomer (open bars) and an HIF-1α specific siRNA oligomer (closed bars) were cultured in hypoxia for the indicated number of days. The amount of hMSH3 was compared between hypoxic cells transfected with a negative control (ctr) oligomer and the HIF-1α siRNA (HIF) oligomer after normalization by α-tubulin signals.