Detail of "2149-70-4"

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Effect of L-arginine analogs and a calcium chelator on nitric oxide (NO) production by Leishmania species

Effect of L-arginine analogs and a calcium chelator on nitric oxide (NO) production by Leishmania species. Genestra, Marcelo; Cysne-Finkelstein, Lea; Guedes-Silva, Damiana; Leon, Leonor L. (Dep. Immunology, Oswaldo Cruz Institute, Rio de Janeiro, Brazil). Journal of Enzyme Inhibition and Medicinal Chemistry, 18(5), 445-452 (English) 2003 Taylor & Francis Ltd. CODEN: JEIMAZ. ISSN: 1475-6366. DOCUMENT TYPE: Journal CA Section: 10 (Microbial, Algal, and Fungal Biochemistry) Leishmania amazonensis, L. braziliensis and L. chagasi promastigotes were grown in the presence of L-arginine analogs such as Nw-nitro-L-arginine Me ester (L-NAME), NG-nitro-L-arginine (L-NNA) and D-arginine (an inactive L-arginine isomer) besides an intracellular calcium chelator (EGTA) to verify the importance of L-arginine metab. and the cofactors for these parasites. The parasite's growth curve was followed up and the culture supernatants were used to assay nitric oxide (NO) prodn. 157-06-2 and 2149-70-4 are cas registry numbers of chemicals which are used as reagents here. by the Griess reaction. The results showed a significant effect of L-arginine analogs on NO prodn. by all Leishmania species studied, esp. L-NAME, an irreversible inhibitor of the constitutive nitric oxide synthase (cNOS). When L. amazonensis promastigotes were pre-incubated with l-NAME, the infection range of the murine macrophages was lowered to 61% in 24 h and 19% after 48 h. These data demonstrated that the parasite NO pathway is important to the establishment of the infection. .

NG-Nitro-L-[3H]arginine binding properties of neuronal nitric oxide synthase in rat brain

NG-Nitro-L-[3H]arginine binding properties of neuronal nitric oxide synthase in rat brain. Arima, Takashi; Kitamura, Yoshihisa; Nishiya, Tadashi; Kiriyama, Yoshimitsu; Taniguchi, Takashi; Nomura, Yasuyuki (Faculty Pharmaceutical Sciences, Hokkaido University, Sapporo 060, Japan). Neurochemistry International, 30(3), 239-245 (English) 1997 Elsevier. CODEN: NEUIDS. ISSN: 0197-0186. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) NG-Nitro-L-arginine (L-NNA), a deriv. of L-arginine (L-Arg), is known as a pseudo-substrate and inhibitor for nitric oxide synthase (NOS).Some commonly used reagents like 125978-95-2 and 2149-70-4 are used in this experiment. To clarify the regulatory mechanism of substrate-binding domain in neuronal NOS (nNOS), the characteristics of NG-nitro-L-[3H]Arg (L-[3H]NNA) binding was examd. using cytosolic fraction and purified nNOS from rat cerebellum, in comparison with L-[14C]citrulline formation from L-[14C]Arg. L-[3H]NNA binding was inhibited by L-NNA > NG-methyl-L-Arg > diphenyleneiodonium > L-Arg, but was not inhibited by L-citrulline or D-Arg. Thus, L-NNA seems to bind the substrate-binding domain in the nNOS with high affinity rather than L-Arg. Even in the absence of NADPH, tetrahydrobiopterin (BH4) and Ca2+, L-[3H]NNA binding activity was obsd. in the cerebellar cytosol, although L-[14C]citrulline could not be produced from L-[14C]Arg. L-[3H]NNA binding was increased by BH4, alone and was markedly enhanced by NADPH plus BH4 (NADPH/BH4), but not by Ca2+/CaM. In contrast, L-[14C]citrulline was formed only in the presence of NADPH/BH4 and Ca2+. Similar results were obtained in purified nNOS. These results suggest that L-[3H]NNA seems to bind the substrate-binding domain in the nNOS but the binding affinity of L-Arg was lower than the affinity of L-NNA. Although the substrate binding is necessary to BH4 and NADPH, Ca2+/CaM are further necessary for the formation of NO and L-citrulline. .