Identification of a specific amino acid cluster in the calmodulin-binding domain of the neuronal nitric oxide synthase

AbstractThe calmodulin (CaM) binding domain of rat neuronal nitric oxide synthase (nNOS) was analyzed using 3 synthetic peptides corresponding to different regions of the middle portion of the enzyme. One corresponding to nNOS 732–754 gave complete inhibition of NOS enzyme activity with an IC50 of about 1 μM. Kinetic analysis indicated that the inhibition was not competitive with respect to l-arginine and the peptide produced a Ca2+ dependent, electrophoretic mobility shift of CaM on 1 M urea gels. A specific hydrophobic/basic amino acid cluster in the rat nNOS sequence, Lys732LysLeu, that was critical for its CaM binding was also identified in this study.© 1997 Federation of European Biochemical Societes

酵母細胞の耐塩性に関する研究

第1章 耐塩性酵母Zygosaccharomyces rouxiiの脂質組成に及ぼす食塩の影響 第2章 耐塩性酵母Zosaccharomyces rouxii細胞のリノール酸合成に及ぼす食塩の影響 第3章 好塩性酵母Candida versatilisの脂質組成に及ぼす食塩の影響 第4章 酵母細胞の易熱性抗原タンパク質TLAa及びTLAbの同定 第5章 酵母細胞の易熱性抗原タンパク質TLAaとTLAbのストレスに対する応答 第6章 耐塩性酵母Zygosaccharomyces rouxiiの生育に及ぼす薬剤の効果 第7章 耐塩性酵母Zygosaccharomyces rouxii細胞膜に局在するプロトンATPaseの性質 第8章 耐塩性酵母Zygosaccharomyces rouxii細胞膜プロトンATPase遺伝子のクローニングと解析Made available in DSpace on 2012-06-28T07:06:43Z (GMT). No. of bitstreams: 2 watanabe1.pdf: 10927213 bytes, checksum: 96b779a1d36541707abad7fddfc73d17 (MD5) watanabe2.pdf: 11491080 bytes, checksum: 7d7f1d07ff3565ad551cce8c5c5c352a (MD5) Previous issue date: 1991-09-27主1-参

Effects of cold exposure on metabolites in brown adipose tissue of rats

Brown adipose tissue (BAT) plays an important role in regulation of energy expenditure while adapting to a cold environment. BAT thermogenesis depends on uncoupling protein 1 (UCP1), which is expressed in the inner mitochondrial membranes of BAT. Gene expression profiles induced by cold exposure in BAT have been studied, but the metabolomic biological pathway that contributes to the activation of thermogenesis in BAT remains unclear. In this study, we comprehensively compared the relative levels of metabolites between the BAT of rats kept at room temperature (22 °C) and of those exposed to a cold temperature (4 °C) for 48 h using capillary electrophoresis (CE) time-of-flight mass spectrometry (TOFMS) and liquid chromatography (LC)-TOFMS. We identified 218 metabolites (137 cations and 81 anions) by CE-TOFMS and detected 81 metabolites (47 positive and 34 negative) by LC-TOFMS in BAT. We found that cold exposure highly influenced the BAT metabolome. We showed that the cold environment lead to lower levels of glycolysis and gluconeogenesis intermediates and higher levels of the tricarboxylic acid (TCA) cycle metabolites, fatty acids, and acyl-carnitine metabolites than control conditions in the BAT of rats. These results indicate that glycolysis and β-oxidation of fatty acids in BAT are positive biological pathways that contribute to the activation of thermogenesis by cold exposure, thereby facilitating the generation of heat by UCP1. These data provide useful information for understanding the basal metabolic functions of BAT thermogenesis in rats in response to cold exposure

Iron Chelation Therapy with Deferasirox Results in Improvement of Liver Enzyme Level in Patients with Iron Overload-Associated Liver Dysfunction

Iron chelation therapy (ICT) has been applied for the patients with iron overload-associated liver dysfunction since it is one of the causes of death in patients with intractable hematological diseases requiring multiple red blood cell transfusions. Recently, deferasirox (DSX), a novel, once-daily oral iron chelator, was demonstrated to have similar efficacy to the conventional continuous infusion of deferoxamine on a decrease in serum ferritin (SF) level in heavily transfused patients. We show three cases of transfusion-mediated iron-overloaded patients with an elevated serum alanine aminotransaminase (ALT). All three patients who received the ICT with DSX showed a decrease in ALT level in association with a decrease in SF level. It is suggested that DSX therapy could be considered to expect the improvement of liver damage for iron-overloaded patients with an abnormal ALT level