1989 Fiscal Year Final Research Report Summary
Post-translational modification of protein and its cell-biochemical significance
| Project/Area Number |
62304034
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| Research Category |
Grant-in-Aid for Co-operative Research (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
General medical chemistry
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| Research Institution | Yamagata University |
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Principal Investigator |
TUBOI Syozo Yamagata University, Biochemistry Professor, 医学部, 教授 (70004554)
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| Co-Investigator(Kenkyū-buntansha) |
OMURA Tsuneo Kyushu University, Biochemistry, Professor, 大学院医学系, 教授 (80029933)
MAIKITA Akira Hokkaido University, Biochemistry Professor, 医学部, 教授 (60004561)
KATUNUMA Nobuhiko Tokushima University, Biochemistry Professor, 酵素科学センター, 教授 (50035375)
TSUIKI Shigeru Tohoku University, Biochemistry, Professor, 抗酸菌病研究所, 教授 (90006065)
KATO Keitaro Kyushu University, Biochemistry, Professor, 薬学部, 教授 (70037571)
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| Project Period (FY) |
1987 – 1989
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| Keywords | modification of lysosomal enzymes / cystatin beta / protein disulfide isomerase / Cu, Zn-Superoxide dismutase / glycation / protein carboxymethyltransfer se / 酸性フォスファタ-ゼ / 蛋白質カルボキシメチル転移酵素 |
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| Research Abstract |
Kato, Makita and Tsuiki studied on three kinds of lysosomal enzymes and reported as follows: Acid phosphatase was changed its localization by the modification of its c-terminal sequence (Kato), the post-translocational modification of beta-glucronidase was greatly influenced with the oncogenic transformation of cell (Makita), the membrane-associated sialidase which decreased in hepatoma cells was its type II of two isozymes (Tsuiki). Katunuma reported the complete structure of an endogenous inhibitor (Cystatin beta) which is specific to the lysosomal cysteine proteases and the molecular mechanism of the inhibition to these proteases by Cystatin beta that the proteases were modified with glutathione forming mixed disulfide with enzyme protein. Tashiro showed that the localization of protein disulfide isomerase was determined by the differential cleavage of an oligo-peptide in its C-terminal portion. Taniguchi reported that in a patient of diabetes mellitus, Cu, Zn-superoxide dismutase i
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n red blood cell was glycated with twice fold magnitude of the reaction velocity comparing with that of normal one and analyzed the molecular mechanism of the inactivation of Cu, Zn-superoxide dismutase by glycation. Horiuchi suggested the existence of the receptor which specifically binds the proteins glycated during his studies on the receptor of proteins modified by acetylation. Omura purified the processing enzyme for the mitochondrial protein precursor from rat liver and obtained its homogeneous preparation. He also determined its primary structure, then analyzed the molecular mechanism of processing of mitochondrial protein precursor using the purified processing enzyme. Saheki analyzed the structure of E_2 in pyruvate dehydrogenase complex and tried to clarify the mechanism of covalent bond between E_2 protein and lipoic acid. Tuboi studied on protein carboxymethyltransferase in rat brain and found that this enzyme has two types, the cytosolic and membrane bound types. The primary structure of the cytosolic type was determined by analysis of its cDNA, and that of the membrane bound type are now investigating. He is intending to clarify the mechanism of their localization from their primary structures and their physiological significances on intra-cellular metabolism of proteins. Less
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