Regulation of Endothelial Nitric Oxide Synthase Activity and Gene Expression

@article{Wu2002RegulationOE,
  title={Regulation of Endothelial Nitric Oxide Synthase Activity and Gene Expression},
  author={Kenneth K. Wu},
  journal={Annals of the New York Academy of Sciences},
  year={2002},
  volume={962}
}
  • K. Wu
  • Published 1 May 2002
  • Biology
  • Annals of the New York Academy of Sciences
Abstract: Endothelial nitric oxide synthase (eNOS) is constitutively expressed in endothelial cells lining the blood vessel and the heart. It plays a major role in vascular and tissue protection. Its activity is tightly controlled by an intramolecular autoinhibitory element that hinders calmodulin binding. This molecular hindrance is removed by elevated intracellular calcium levels. The catalytic activity of eNOS is augmented by phosphorylation of a C‐terminal serine residue (Ser‐1177 of human… 

Downregulation of human endothelial nitric oxide synthase promoter activity by p38 mitogen-activated protein kinase activation.

TLDR
The findings strongly suggest that the activation of the p38 MAPK signaling pathway may be implicated in the downregulation of human eNOS promoter activity.

Transcriptional and posttranscriptional regulation of endothelial nitric oxide synthase expression.

  • C. Searles
  • Biology
    American journal of physiology. Cell physiology
  • 2006
The ability of the endothelium to produce nitric oxide is essential to maintenance of vascular homeostasis; disturbance of this ability is a major contributor to the pathogenesis of vascular disease.

Lysophosphatidylcholine up-regulates human endothelial nitric oxide synthase gene transactivity by c-Jun N-terminal kinase signalling pathway

TLDR
It was observed by electrophoretic mobility shift assay that LPC stimulated both SP1 and AP1 DNA binding activity to go up, and using decoy oligonucleotides proved that SP1 was necessary for maintaining the basal or stimulated trans activity, whereas AP1 contributed mainly to the increase of the stimulated transactivity.

Serine 1179 Phosphorylation of Endothelial Nitric Oxide Synthase Increases Superoxide Generation and Alters Cofactor Regulation

TLDR
It is demonstrated that eNOS serine 1179 phosphorylation, in addition to enhancing NO production, also profoundly affects superoxide generation: S1179osphorylation increases superoxide production while decreasing sensitivity to the inhibitory effect of BH4 on this activity.

Betulinic Acid Increases eNOS Phosphorylation and NO Synthesis via the Calcium-Signaling Pathway.

TLDR
Results indicate that BA activates eNOS phosphorylation and NO synthesis via the Ca(2+)/CaMKII and Ca( 2+)/ CaMKK/AMPK pathways, which provide further insight into the eN OS signaling pathways involved in the antiatherosclerosis effects of BA.

Progesterone promotes endothelial nitric oxide synthase expression through enhancing nuclear progesterone receptor-SP1 formation.

TLDR
Progesterone modulates eNOS expression through promoting PR-A-SP1 complex formation and progesterone antagonist attenuates eNos expression leading to the loss of vascular relaxation.

Long‐term up‐regulation of eNOS and improvement of endothelial function by inhibition of the ubiquitin–proteasome pathway

  • V. StanglM. Lorenz K. Stangl
  • Biology, Chemistry
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 2004
TLDR
Results indicate that low‐dose proteasome inhibition enhances eNOS expression and activity, and improves endothelial function, as evidenced by accumulation of poly‐ubiquitinylated proteins and by measuring proteasomal activity in cell extracts.

16K-prolactin inhibits activation of endothelial nitric oxide synthase, intracellular calcium mobilization, and endothelium-dependent vasorelaxation.

TLDR
16K-PRL can block the Ca(2+)-mediated activation of eNOS by three different vasoactive substances, and this action results in the inhibition of both angiogenesis and vasorelaxation.
...

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TLDR
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