Role of Sp1 in transcriptional activation of human nitric oxide synthase type III gene

Biochemical and Biophysical Research Communications
J L TangK K Wu

Abstract

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.

Citations

Jun 17, 2008·American Journal of Physiology. Lung Cellular and Molecular Physiology·Sanjiv KumarStephen M Black
Nov 11, 1999·Proceedings of the National Academy of Sciences of the United States of America·T WallerathU Förstermann
Apr 29, 1999·Proceedings of the National Academy of Sciences of the United States of America·X M XuK K Wu
Jan 15, 2008·American Journal of Physiology. Lung Cellular and Molecular Physiology·Neetu SudStephen M Black
Dec 13, 2006·Biochemical and Biophysical Research Communications·Ji-Eun OhEun Seong Hwang
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