41 research outputs found
Oxidation-reduction midpoint potentials of the molybdenum center in spinach NADH:nitrate reductase
AbstractOxidation-reduction midpoint potentials for the molybdenum center in assimilatory NADH:nitrate reductase isolated from spinach (Spinacia oleracea) have been determined at pH 7.0 in the presence of dye mediators using EPR spectroscopy to monitor formation of Mo(V). Values for the Mo(VI)/Mo(V) and Mo(V)/Mo(IV) couples were determined to be −8 and −42 mV, respectively
Polynucleotides targeted against the extended 5′-UTR region of argininosuccinate synthase and uses thereof
The present invention is based in part on the discovery that the upstream open reading frame (uORF) in the extended 5′-untranslated region (5′-UTR) argininosuccinate synthase (AS) mRNA species is functional, and when functional, limits overall AS expression as well as nitric oxide (NO) production. Thus, the extended 5′-UTR AS mRNA species is a mechanism for regulating AS expression and NO production, and provides a target for the treatment of pathophysiological conditions associated with vascular endothelial dysfunction and characterized by impairment of NO production, such as heart failure, hypertension, hypercholesterolemia, atherosclerosis, and diabetes
Author Correction: Transcript expression-aware annotation improves rare variant interpretation
In this Article, author Marquis P. Vawter was missing from the Genome Aggregation Database Consortium list. They are associated with the affiliation: ‘Department of Psychiatry & Human Behavior, University of California Irvine, Irvine, CA, USA’, and contributed to the generation of the primary data incorporated into the gnomAD resource. The original Article has been corrected online
Stimulation of Receptor-Mediated Nitric Oxide Production by Vanadate
Abstract
—Nitric oxide (NO) production by endothelial cells in response to bradykinin (Bk) treatment was markedly and synergistically enhanced by cotreatment with sodium orthovanadate (vanadate), a phosphotyrosine phosphatase inhibitor. This enhancement was blocked by tyrosine kinase inhibitors. Calcium ionophore– (A23187) activated production of NO was also enhanced by cotreatment with vanadate. No significant changes were found in total endothelial NO synthase (eNOS) protein or in eNOS distribution between membrane (caveolae) and cytosolic fractions in response to the various treatments. Vanadate had no direct effect on eNOS activity, and lysates prepared from cells treated with vanadate showed little change in specific activity of eNOS. Western blots of immunoprecipitated eNOS showed the presence of a major tyrosine-phosphorylated protein band at a mass corresponding to ≈125 kDa and 2 minor bands corresponding to ≈105 and 75 kDa after treatment with vanadate/Bk. No tyrosine phosphorylation of eNOS after treatment with vanadate/Bk was observed. Geldanamycin, an inhibitor of heat shock protein 90, also inhibited the enhancement of NO production by vanadate/Bk or vanadate/A23187, and there was an increase in the amount of heat shock protein 90 that coimmunoprecipitated with eNOS after treatment with vanadate/Bk. These results show that there is a clear link between tyrosine phosphorylation and stimulation of eNO production, which does not appear to involve direct modification of eNOS, changes in eNOS levels, or compartmentation, but rather appears to be due to changes in proteins associating with eNOS, thereby enhancing the state of activation of eNOS.
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