1986 Fiscal Year Final Research Report Summary
Biological significance of proteolysis and its regulation
| Project/Area Number |
60304094
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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 |
代謝生物化学
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| Research Institution | Nagoya City University Medical School |
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Principal Investigator |
SASAKI Makoto Nagoya City University Medical School, 医学部, 教授 (10080003)
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| Co-Investigator(Kenkyū-buntansha) |
SUZUKI Koichi The Tokyo Metropolitan Institute of Medical Science, 部長 (80011948)
TAKAHASHI Kenji University of Tokyo, Faculty of Science, 理学部, 教授 (70011533)
ICHIHARA Akira University of Tokushima, School of Medicine, 医学部, 教授 (20035405)
MURACHI Takashi Kyoto University, Faculty of Medicine, 医学部, 教授 (10089104)
IWANAGA Sadaaki Kyushu University, Faculty of Science, 理学部, 教授 (90029942)
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| Project Period (FY) |
1985 – 1986
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| Keywords | Proteolysis / Proteinase inhibitor / Kininogen / Calpain / Calpastatin / Cathepsin / Signal peptidase / プロティナーゼの活性制御 |
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| Research Abstract |
This Grant-in-Aid for Co-operative Research (Project NO. 60304094) facilitated the study on "Biological significance of Proteolysis and its Regulation" during the last 2 years. The study was carried out under 3 subgroups:
1. Proteolysis and activation mechanism of bioactive proteins.
2. Intracellular proteolysis and its regulation, and
3. Proteolysis of cell surface proteins and cell division.
Subgroup 1 studied limited proteolysis and the change in inhibitory capacity for cysteine proteinases, a new activation mechanism of prothrombin, structure and substrate specificity of signalpeptidase for prepepsinogen, and activation mechanism of tyrosine monooxygenase by calpain.
Subgroup 2 concerned sequence study and activation mechanism of calpains, tissue distribution and physiological function of prolylendopeptidase, reversible regulation of cystatin- <BETA> inhibitory activity by interaction with glutathione, and chymotryptic-like enzyme associated with Fc receptor stimulation to polymorphoneuclear lcucocytes.
Subgroup 3 studied a membrane bound protease and its contribution to the cell division of primary cultured-liver cells, and a fibronection proteolytic enzyme which increases in virus-transformed liver cells.
These works were carried out centering on the biological events on proteolysis and its regulation mechanism. The results were published in total of ca. 70 original papers and 10 review articles.
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Research Products
(14 results)
