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J Biol Chem, Vol. 274, Issue 5, 3076-3093, January 29, 1999
From the Renal Division and Department of Medicine, St. Michael's
Hospital and University of Toronto, Toronto,
Ontario M5S 1A8, Canada
Understanding transcription initiation of the
endothelial nitric-oxide synthase (eNOS) gene appears pivotal to
gaining a comprehensive view of NO biology in the blood vessel wall.
The present study therefore focused upon a detailed dissection of the
functionally important cis-DNA elements and the multiprotein complexes
implicated in the cooperative control of constitutive expression of the
human eNOS gene in vascular endothelium. Two tightly clustered
cis-regulatory regions were identified in the proximal enhancer of the
TATA-less eNOS promoter using deletion analysis and linker-scanning
mutagenesis: positive regulatory domains I (
104/95 relative to
transcription initiation) and II (144/115). Analysis of
trans-factor binding and functional expression studies revealed a
surprising degree of cooperativity and complexity. The nucleoprotein
complexes that form upon these regions in endothelial cells contained
Ets family members, Sp1, variants of Sp3, MAZ, and YY1. Functional
domain studies in Drosophila Schneider cells and
endothelial cells revealed examples of positive and negative
protein-protein cooperativity involving Sp1, variants of Sp3, Ets-1,
Elf-1, and MAZ. Therefore, multiprotein complexes are formed on the
activator recognition sites within this 50-base pair region of the
human eNOS promoter in vascular endothelium.
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