| Project/Area Number |
08672129
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Functional basic dentistry
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| Research Institution | THE UNIVERSITY OF TOKUSHIMA,SCHOOL OF DENTISTRY |
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Principal Investigator |
HOSOI Kazuo The University of Tokushima, School of Dentistry, Professor, 歯学部, 教授 (10049413)
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| Co-Investigator(Kenkyū-buntansha) |
MATSUMOTO Takuya The University of Tokushima, School of Dentistry, Research associate, 歯学部, 助手 (90284299)
AKAMATSU Tetsuya The University of Tokushima, School of Dentistry, Research associate, 歯学部, 助手 (80294700)
KIKKAWA Yamato The University of Tokushima, School of Dentistry, Research associate, 歯学部, 助手 (20274227)
KANAMORI Norio The University of Tokushima, School of Dentistry, Associate Professor, 歯学部, 助教授 (90064865)
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| Project Period (FY) |
1996 – 1997
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| Project Status |
Completed (Fiscal Year 1997)
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| Budget Amount *help |
¥2,500,000 (Direct Cost: ¥2,500,000)
Fiscal Year 1997: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1996: ¥1,500,000 (Direct Cost: ¥1,500,000)
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| Keywords | Tissue kallikrein family / Proreninn converting enzyme / True tissue kallikrein / Submandibular gland / Mouse / Processing enzyme / 組織カリクレイン / プロレニン / プロセッシング / 成長因子 |
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| Research Abstract |
1. Four tissue kallikrein family enzymes (mK1, mK9, mK13, mK22) were prepared from mouse submandibular gland. mK13 was ientified to be a prorenin converting enzyme. mK9, a binding protein for EGF,was found to have an activity to hydrolyze prorenin to give an active renin. Acting on prorenin, mK22 (beta-NGF endopeptidase) gave two products renin and arginyl renin. On the other hand, mK1, a true kallikrein did not process renin at all. The results suggest that tissue kallikrein family enzyme bearing higher kinin-releasing activity have lower prorenin-converting activity and vice versa. These enzymes may possibly have a physiologic role in the tissue rein-angiotensin system
2. From the submandibular gland of DBA/2N mice, and enzyme of tissue kallikrein family was purified and sequenced. A cDNA of this enzyme was also cloned and nucleotide sequence was determined. The enzyme was highly homologous to mK13/mK26, a prorenin converting enzyme (PRECE). It actually had the activity to give renin from its precursor prorenin. The presence and absence of the present enzyme and mK13/mK26 in DBA/2N and ICR mice suggested that the purified enzyme is an allozyme of PRECE (PRECE^b).
3. Anti-mK1 antiserum specific to, its antigen was prepared by absorption of antiserum with purified tissue kallikrein enzymes. Immunohistochemical localization of mK1 was then invetigated using the specific antiserum. mK1 localized in the secretory granules of segregated number of granular convoluted tublar cells (GCT cellls). Such mosaic staining pattern was seen in both males and females. The cell type that shows possitive reaction was different between males and females ; slender GCT cells were stained in males whereas typical pyramydal cells were stained in females. About 5% of GCT cells in males were immunoreactive for mK1, whereas 65% of these segments were positive in females.
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