Effects of kyotorphin (l-tyrosyl-l-arginine) on [H]N-nitro-l-arginine binding to neuronal nitric oxide synthase in rat brain期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

Effects of kyotorphin (l-tyrosyl-l-arginine) on [H]N-nitro-l-arginine binding to neuronal nitric oxide synthase in rat brain

Authors:	Takashi Arima Yoshihisa Kitamura Tadashi Nishiya Takashi Taniguchi Hiroshi Takagi Yasuyuki Nomura

Affiliation:	^aDepartment of Pharmacology, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060, Japan;^bDepartment of Neurobiology, Kyoto Pharmaceutical University, Kyoto 607, Japan;^cDepartment of Pharmacology, Faculty of Pharmaceutical Sciences, Kinki University, Higashi-Osaka 577, Japan;^dDepartment of Neuroscience, Research Institute for Oriental Medicine, Toyama Medical and Pharmaceutical University, Toyama 930-01, Japan

Abstract:	Full-size image -Tyrosyl- Full-size image -arginine (kyotorphin) is known as an endogenous analgesic neuropeptide. We examined whether kyotorphin and other arginine-containing neuropeptides were endogenous substrates for neuronal nitric oxide synthase (NOS) in the rat brain. Cytosol fractions of the rat cerebellum contained higher concentrations of neuronal NOS (nNOS) than endothelial NOS. In rat cerebellar cytosol, the binding activity of [³H]N^G-nitro- Full-size image -arginine (NNA) was inhibited equally by Full-size image -arginine ( Full-size image -Arg), kyotorphin, and Full-size image -leucyl- Full-size image -Arg (a kyotorphin receptor antagonist). Binding activities were inhibited to lesser degrees by fibronectin active fragments, bradykinin, and dynorphin A, but were not inhibited by Full-size image -tyrosyl- Full-size image -Arg or substance P. Interestingly, the inhibition of [³H]NNA binding by kyotorphin was attenuated by inhibitors of kyotorphin-hydrolyzing peptidases (KTPases) such as bestatin and arphamenine B. These results suggest that kyotorphin is degraded to Full-size image -Arg by KTPases, which in turn may act as substrate for nNOS.

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