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Possible Interaction: Nitric Oxide and Ascorbate



Research Papers that Mention the Interaction

Asc may increase NO bioavailability by a number of mechanisms involving BH₄ and eNOS.
Ascorbate (Asc) has been shown to increase nitric oxide (NO) bioavailability and thereby improve endothelial function in patients showing signs of endothelial dysfunction.
In this review, we discuss the putative mechanisms by which Asc may increase NO bioavailability through its interactions with BH₄ and eNOS.
Nitric oxide : biology and chemistry  •  2014  |  View Paper
Notably, ascorbate has been proposed to enhance myeloperoxidase-catalyzed NO consumption by forming NO-consuming substrate radicals.
Free radical biology & medicine  •  2014  |  View Paper
Ascorbate also regulates nitric oxide concentration by releasing nitric oxide from adducts and by acting through tetrahydrobiopterin (BH4) to stimulate endothelial nitric oxide synthase (eNOS).
Sub-cellular biochemistry  •  2012  |  View Paper
Pharmacologic studies reveal that vitamin C (as ascorbate ), at supraphysiologic doses, significantly affects the bioavailability of nitric oxide during acute inflammation, including inhibiting nitric oxide synthetase induction.
Critical care medicine  •  2007  |  View Paper
In addition, L-arginine, the substrate for NO synthesis, and the anti-oxidants ascorbate and α-tocopherol, are able to increase NO synthesis and bioavailability respectively.
Expert opinion on pharmacotherapy  •  2001  |  View Paper
In this review, multiple mechanisms are considered that might account for the ability of ascorbate to preserve NO.
Free radical biology & medicine  •  2000  |  View Paper
Both DHA and ascorbate free radical AFR ), the intermediate between ASC and DHA, enhanced NO oxidation to nitrite, but not nitrate; nor did either oxidize nitrite to nitrate.
Biochemistry  •  2008  |  View Paper
Nitric oxide predictably inhibited both endothelial nitric oxide synthase and glyceraldehyde 3-phosphate dehydrogenase, and ascorbate partially prevented inhibition of the latter enzyme.
Archives of biochemistry and biophysics  •  2004  |  View Paper
By exposing cells to ascorbate , we induced release of NO from the S-nitroso groups, resulting in HS degradation and unloading of the sequestered polyamines as well as nuclear targeting of the deglycanated Gpc-1 protein.
Journal of Biological Chemistry  •  2003  |  View Paper
Combined experiments encompassing direct stimulus with NO and inhibitors of glutamate uptake and nNOS provided additional evidence supporting the modulator role of NO in the release of ascorbate to the extracellular space.
Brain Research Bulletin  •  2015  |  View Paper
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