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Papers In Press, published online ahead of print August 16, 2003
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Surgery Dept., Uniformed Services University, School of Medicine, Bethesda, MD 20814
Corresponding Author: ishechter{at}usuhs.mil
The mRNA level for cytosolic NADP-dependent isocitrate dehydrogenase (IDH1) increases 2.3 fold, and enzyme activity of NADP-isocitrate dehydrogenase 63%, in sterol-deprived HepG2 cells. mRNA levels of the NADP- and NAD-dependent mitochondial enzymes show limited or lack of regulation under the same conditions. Nucleotide sequences that are required, and sufficient, for the sterol-regulation of transcription are located within a 67 bp region of an IDH1-secreted alkaline phosphatase (SEAP) promoter-reporter gene. The IDH1 promoter is fully activated by the expression of SREBP-1a in the cells and, to a lesser degree, by SREBP-2. 5'-end truncation of 23 bp containing a CAAT and a GC-Box results in a 6.5% residual activity. The promoter region involved in the activation by the SREBPs is located at nucleotides -44 to -25. Mutagenesis analysis identified within this region the IDH1-SRE sequence element GTGGGCTGAG, which binds the SREBPs. Similar to the promoter activation, electrophoretic mobility-shift of probes containing the IDH1-SRE element exhibit preferential binding to SREBP-1a, as compared to SREBP-2. These results indicate that IDH1 activity is coordinately regulated with the cholesterol and fatty acid biosynthetic pathways and suggest it to be the source for the cytosolic NADPH required by these pathways.
Revised on August 8, 2003
Accepted on August 16, 2003
IDH1 gene transcription is sterol-regulated and activated by SREBP-1a and SREBP-2 in human hepatoma HepG2 cells: Evidence that IDH1 may regulate lipogenesis in hepatic cells
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