Inhibition of L-Arginine Metabolizing Enzymes by L-Arginine-Derived Advanced Glycation End Products
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Nω-Carboxymethyl-arginine (CMA), Nω-carboxyethyl-arginine (CEA) and Nδ-(5-hydro-5-methyl-4-imidazolon-2-yl)-ornithine (MG-H1) have been identified as L-arginine-derived advanced glycation end products (AGEs) formed by non-enzymatic reactions between reducing sugars such as glucose and amino groups in proteins. These AGEs are structurally analogous to endogenous inhibitors of nitric oxide synthases (NOS) including NG-monomethyl-L-arginine (L-NMMA) and asymmetric NG,NG-dimethyl-L-arginine (ADMA). Increased plasma levels of these NOS inhibitors, and thus impaired generation of NO in vivo has been associated with the pathogenesis of vascular complications such as kidney failure and atherosclerosis. For these reasons we examined whether L-arginine-derived AGEs inhibit the activities of three L-arginine metabolizing enzymes including three isoforms of NOS (endothelium, neuronal and inducible NOS), dimethylarginine dimethylaminohydrolase (DDAH) that catalyzes the hydrolytic degradation of L-NMMA and ADMA to L-citrulline, and arginase that modulates intracellular L-arginine bioavailability. We found that AGEs inhibited the in vitro activities of endothelium type NOS weakly (IC50 values of CMA, CEA and MG-H1 were 830, 3870 and 1280 μM, respectively) and were also potential endogenous inhibitors for arginase (IC50 values of CMA and CML were 1470 and 1060 μM), but were poor inhibitors for DDAH. These results suggest that the tested L-arginine- and L-lysine-derived AGEs appear not to impair NO biosynthesis directly.
- 日本酸化ストレス学会 JCBN事務局の論文
日本酸化ストレス学会 JCBN事務局 | 論文
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