Role of Sp1 in Transcriptional Activation of Human Nitric Oxide Synthase Type III Gene
Copyright policy )Role of Sp1 in Transcriptional Activation of Human Nitric Oxide Synthase Type III Gene
Endothelial nitric oxide synthase (eNOS or NOS-III) is constitutively expressed. To elucidate the mechanism by which the basal expression of NOS-III gene is activated, we constructed in a luciferase vector, pXP1, serial 5'-deletion mutants of a 1.3-kb 5'-flanking fragment and transiently expressed them in cultured human endothelial cells. The promotor activity was detected in the -198/+22 region which contains several putative Sp1 binding sites. DNase I footprinting assays coupled with gel shift assays revealed the GC box(-104/-90) to be the Sp1 binding site. Site-directed mutation of 4 crucial bases in this site reduced the promotor activity by > 90%. These findings provide strong evidence that binding of Sp1 or closely related protein to this site is required for the activation of basal NOS-III transcription.
- The University of Texas at Austin United States
- The University of Texas Health Science Center at Houston United States
Umbilical Veins, Base Sequence, Transcription, Genetic, Sp1 Transcription Factor, Recombinant Fusion Proteins, Molecular Sequence Data, Transfection, beta-Galactosidase, Polymerase Chain Reaction, Gene Expression Regulation, Mutagenesis, Site-Directed, Deoxyribonuclease I, Humans, Amino Acid Oxidoreductases, Endothelium, Vascular, Nitric Oxide Synthase, Luciferases, Cells, Cultured
Umbilical Veins, Base Sequence, Transcription, Genetic, Sp1 Transcription Factor, Recombinant Fusion Proteins, Molecular Sequence Data, Transfection, beta-Galactosidase, Polymerase Chain Reaction, Gene Expression Regulation, Mutagenesis, Site-Directed, Deoxyribonuclease I, Humans, Amino Acid Oxidoreductases, Endothelium, Vascular, Nitric Oxide Synthase, Luciferases, Cells, Cultured
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