Clitoris NO—Arginine Yes

The Durk Pearson & Sandy Shaw®
Life Extension NewsTM
Volume 6 No. 3 • June 2003

Clitoris NO—Arginine Yes

“The localization of NO synthase in human clitoral corpus cavernosum [the homologous female tissue to male penile corpus cavernosum] may . . . implicate arginase as a regulator of arginine bioavailability in this tissue . . . .”1 It also implicates nitric oxide as a mediator of clitoral erection. Arginine may be processed by the arginase or nitric oxide synthase pathways: it is converted to citrulline and nitric oxide by nitric oxide synthase, and it is converted to ornithine and urea by the arginase pathway. The latter is part of the ammonia detoxifying process. The paper cited here found data supporting the hypothesis that arginase bioavailability appears to limit NO biosynthesis by removing available arginine from use by the NO synthase. This can be overcome by adequate supplies of extracellular (but not intracellular) arginine.

The authors also note that an additional factor in the use of arginine is the presence and compartmentalization of endogenous competitive inhibitors such as NG-methyl-L-arginine and NG,NG-dimethyl-L-arginine, which can be displaced from the NO synthase active site by highly effective concentrations of substrate (arginine).

  1. Kim et al. Probing erectile function: S-(2-boronoethyl)-L-cysteine binds to arginase in a transition state analogue and enhances smooth muscle relaxation in human penile corpus cavernosum. Biochemistry 40:2678-88 (2001). Thanks for the paper, Will.

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