Bioconversion of L-arginine into nitric oxide. Nitric Oxide and Arginine Connection.

The bioconversion of L-arginine in the nitric oxide pathway results in one molecule of NO and one of L-citrulline.

This reaction is mediated by the enzyme endothelial nitric oxide synthase (eNOS), which uses ascorbic acid and tetrahydrobiopterin as cofactors. This enzyme is inhibited by hypercholesterolemia, oxidative stress, and asymmetrical dimethylarginine (ADMA).

ADMA is a methylated isomer of L-arginine derived from protein. L-arginine residues in proteins can become methylated; then the protein is hydrolyzed, releasing ADMA. ADMA is a competitive inhibitor of eNOS activity, as it binds to the L-arginine binding site on the enzyme, preventing L-arginine binding.

High levels of ADMA have been positively correlated with inhibited endothelial function and an increased risk of cardiovascular disease, including acute coronary events. It also appears the well-documented correlation between homocysteine and cardiovascular disease might be mediated by ADMA. High levels of ADMA can occur due to poor liver or kidney function, and there may be a genetic component as well.

Whatever the reason for elevated ADMA, increasing the L-arginine/ADMA ratio by supplementation with L-arginine overwhelms the inhibitory effect of ADMA on eNOS and subsequently improves NO production and endothelial function,iv Research does suggest vitamin A might lower ADMA, and antioxidants appear to increase the metabolism of ADMA by dehydro-dimethylarginine hydrolase (DDAH), the rate-limiting enzyme responsible for hepatic degradation of ADMA.

Furthermore, folic acid, vitamin B6, and vitamin B12 lower homocysteine levels, which can decrease ADMA, and it is possible that ADMA levels might decrease if poor kidney or liver function is reversed. However, the most reliable method of improving the L-arginine/ADMA ratio is by L-arginine supplementation.
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