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. 2009 Aug 19;10:79. doi: 10.1186/1471-2350-10-79

Figure 1.

Figure 1

The effect of the p.P582S mutation on the binding affinity of the HIF-1α to hypoxia responsive element (HRE) in SK-N-FI cells. A. Schematic description of pHRE vector, which is a modified pGL3-Control plasmid, containing five HIF-1α binding sites (HRE) in front of the SV40 promoter and the luciferase reporter gene. B. No significant difference could be detected between the transcriptional activities of the pHRE constructs co-transfected with either wild type or p.P582S mutant HIF-1α, neither in normoxic nor under hypoxic conditions. Luciferase activity was normalized to the β-galactosidase activity. Data are presented as fold increments over the normoxic pGL3-Control activity and shown as mean ± SD. Results of a representative experiment are shown as measured in triplicates. Similar data were obtained from three independent transfection experiments.