1999 Fiscal Year Final Research Report Summary
Extensive research on D-amino acids present in mammals
| Project/Area Number |
10309005
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
広領域
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| Research Institution | The Universityof Tokyo |
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Principal Investigator |
IMAI Kazuhiro Graduate School of Pharmaceutical Sciences, The Univ. of Tokyo Professor, 大学院・薬学系研究科, 教授 (50012620)
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| Co-Investigator(Kenkyū-buntansha) |
ESAKI Nobuyosi Institute for Chemical Research, Kyoto Univ., Professor, 化学研究所, 教授 (50135597)
ASANO Yasuhisa Biotechnology Research Center, Toyama Prefectural Univ., Professor, 薬学部, 教授 (00222589)
TOYOOKA Tosimasa School of Pharmaceutical Sciences, Univ. of Shizuoka, Professor, 薬学部, 教授 (40183496)
NAGATA Yoko Faculty of Science, Himeji Institute of Technology, Associate professor, 理学部, 助教授 (00164442)
MISONO Haruo Faculty of Agriculture, Kochi Univ., Professor, 農学部, 教授 (30027073)
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| Project Period (FY) |
1998 – 1999
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| Keywords | D-amino acid / mammals / biosynthesis / racemase / oxidase / bacteria / dehydrogenase / labeling reagent |
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| Research Abstract |
Toyo'oka applied a method a method he developed to the determination of D, L-amino acids in food and biosamples. Nagata isolated D-alanine dehydrogenase from Pyrobaculum islandicum. Misono cloned glutamate racemase and determined the sequence of the enzyme. Asano cloned D-amino acid amide specific amidase from O. anthropi and investigated its relation to the function. Esaki analyzed the gene of amino acid rasemase obtained from Saccharomyces cerevisiae and Schizosaccharomyces pombe. Horiike demonstrated a reverse localization of D-serine and D-amino acid oxidase in the mammals brain. Ymada suggested that a membrane dipeptidase might be useful for the diagnosis of kidney disease. Hashimoto suggested a probable uptake of D-serine into a cell by a stimulation of depolarization. Nishikawa proposed a possible binding of endogenous D-serine with an another site in addition to NMDA glycine binding site. Imai demonstrated the emergence of glutamate transporter at the same site of existence of endogenous D-aspartate. Kagawa isolated a specific degradation enzyme of a D-aspartate containing peptide. Iwatsubo Identified an essential functional domain of presenilin as the most C-terminal amino acid for the enhancement of A β 42 production. Fujii proposed a stereospecific structure for the reverse reaction of aspartate in α A-chrystallin.
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[Publications] Jin, D., Nagakura, K., Murofushi, S., Miyahara, T., Toyo'oka, T.: "Total Resolution of 17 DL-Amino Acids Labeled with a Fluorescent Chiral Reagent, R(-)-4-(3-Isothiocyanatopyrrolidin-1-yl)-7-(N, N-dimethylaminosulfonyl)-2, 1, 3-benzoxadiazole, by High-performance Liquid Chromatograpyh."J. Chromatogr. A. 822. 215-224 (1998)
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「研究成果報告書概要(欧文)」より
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[Publications] Nagata, Y., Tanaka, K., Iida, T., Kera, Y., Yamada, R., Nakajima, Y., Fujiwara, T., Fukumori, Y., Ymamanaka, T., Koga, Y., Tsuji, S., and Kawaguchi, K.: "Occurrence of D-amino acids in a fewarchaea and dehydrogenase activities in hyperthermophile pyrobaculum islandicum."Biochimi. Biophys. Acta. 1435. 160-166 (1999)
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[Publications] Fukumura, Y., Kera, Y., Oshitani, S., Ushijima, Y., Kobayashi, I., Liu, Z., Watanabe, T., Yamada, R., Kikuchi, H., Kawazu, S. and Yabuuchi, M.: "Behavior of urinary dipeptidase in patiens with hronic renal failure."Ann. Clin. Biochem.. 36. 221-225 (1999)
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「研究成果報告書概要(欧文)」より
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[Publications] Cha Seung Hun, Hasegawa, K. Kawabata, T., Kato, M., Shimokawa, T., and Kagawa, Y.: "Increased uncoupling protein 2 mRNA in white adipose tissue, and decrease in leptin viscera; fat, blood glucose and cholesterol in KK-Ay mice fed with eicosapentaenoic and docosahexaenoic acids in addition to linoleicacid."Biochem. Biophys. Res. Commun.. 259. 85-90 (1999)
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[Publications] Tomita, T, Takikawa, R, Koyama, A, Morohashi, Y, Takasugi, N, Saido, TC, Maruyama, K, and Iwatsubo, T: "C terminus of presenilin is required for overproduction of amyloidogenic Ab42 through stabilization and endoproteolysis of presenilin."J. Neurosci. 19. 10627-10634 (1999)
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