Sandbox Reserved 322: Difference between revisions
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==='''Arginase and the Physiology of Sexual Arousal'''=== | ==='''Arginase and the Physiology of Sexual Arousal'''=== | ||
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[[Image:Arginine_catabloism_by_arginase_and_NO_synthase.jpg|thumb| | [[Image:Arginine_catabloism_by_arginase_and_NO_synthase.jpg|thumb|left|300px|Figure 4: Chemical reaction of arginine, illustrating how arginase and NO synthase compete for arginine<ref name="c"/>.]] | ||
Female sexual arousal disorder is defined as an inability to achieve or maintain sufficient sexual excitement, including clitoral erection and genital engorgement, and it is a physiologically analogous to male erectile dysfunction, which is defined as a deficiency in genital blood circulation which compromises the hemodynamic of erectons<ref name="c"/>. Nitric oxide (NO) is the principle mediator of erectile functions and governs nonadrenergic, noncholinergic neurotransmission in penile corpus cavernosum smooth muscle<ref name="c"/>. NO cause’s rapid relaxation of smooth muscle tissue and thereby facilitates the engorgement of the corpus cavernosum<ref name="c"/>. Thus, NO synthase is a critical enzyme in the physiology of sexual arousal<ref name="c"/>. Also, human arginase II is a critical enzyme in the physiology of sexual arousal, due to the fact it coexpressed with NO synthase in smooth muscle tissue<ref name="c"/>. Given that hAII and NO synthase compete for the same substrate L-arginine as shown in figure 4, arginase appears to attenuate NO synthase activity and NO-dependent smooth muscle relaxation by depleting the substrate pool of L-arginine that would be available to NO synthase<ref name="c"/>. In addition arginase is inhibited by the boronic acid inhibitor (<scene name='Sandbox_Reserved_322/Abh/1'>ABH</scene>), which maintains L-arginine concentrations, which in turn enhances NO synthase activity and NO-dependent smooth muscle relaxation in tissue<ref name="c"/>. Thus over expression of human arginase II contributes to erectile dysfunction, and human penile arginase is a potential target for the treatment of male sexual dysfunction<ref name="c"/>. | Female sexual arousal disorder is defined as an inability to achieve or maintain sufficient sexual excitement, including clitoral erection and genital engorgement, and it is a physiologically analogous to male erectile dysfunction, which is defined as a deficiency in genital blood circulation which compromises the hemodynamic of erectons<ref name="c"/>. Nitric oxide (NO) is the principle mediator of erectile functions and governs nonadrenergic, noncholinergic neurotransmission in penile corpus cavernosum smooth muscle<ref name="c"/>. NO cause’s rapid relaxation of smooth muscle tissue and thereby facilitates the engorgement of the corpus cavernosum<ref name="c"/>. Thus, NO synthase is a critical enzyme in the physiology of sexual arousal<ref name="c"/>. Also, human arginase II is a critical enzyme in the physiology of sexual arousal, due to the fact it coexpressed with NO synthase in smooth muscle tissue<ref name="c"/>. Given that hAII and NO synthase compete for the same substrate L-arginine as shown in figure 4, arginase appears to attenuate NO synthase activity and NO-dependent smooth muscle relaxation by depleting the substrate pool of L-arginine that would be available to NO synthase<ref name="c"/>. In addition arginase is inhibited by the boronic acid inhibitor (<scene name='Sandbox_Reserved_322/Abh/1'>ABH</scene>), which maintains L-arginine concentrations, which in turn enhances NO synthase activity and NO-dependent smooth muscle relaxation in tissue<ref name="c"/>. Thus over expression of human arginase II contributes to erectile dysfunction, and human penile arginase is a potential target for the treatment of male sexual dysfunction<ref name="c"/>. | ||