1988 Fiscal Year Final Research Report Summary
Study on brain proteases functioning in degradation of neuropeptides
| Project/Area Number |
62480447
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
物質生物化学
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| Research Institution | Hokkaido University |
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Principal Investigator |
ISHII Shin-ichi Faculty of Pharmaceutical Sciences, Hokkaido University, 薬学部, 教授 (90001031)
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| Project Period (FY) |
1987 – 1988
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| Keywords | Neuropeptide / Neuropeptidase / Substance P / Dynorphin / LHRH (luteinizing-hormone releasing hormone) / Neuron / Glia / エンドペプチダーゼー24.11 |
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| Research Abstract |
The physiological action of neuropeptides at the synapse is terminated through enzymatic degradation by membrane-bound proteases. We have purified membrane-bound proteases functioning in degradation of three neuropeptides, substance P, dynorphin, and LHRH (luteininzing-hormone releasing hormone).
1. A novel substance-P-degrading endopeptidase has been purified from rat brain and characterized as a metallo-protease whose activity was not inhibited by phosphoramidon. Its properties well corresponded to those proposed in the degradation by neuroblastoma cells and neuronal cells cultured from fetal brain. In contrast, the degradation by glioma cells and glial cells cultured from fetal brain was inhibited by phosphoramidon, suggesting the involvement of endopeptidase-24.11. The degrading enzyme has been purified from glioma cells and characterized as endopeptidase-24.11.
2. A dynorphin-degrading trypsin-like enzyme and two dynorphin-degrading cysteine proteases have been purified from neuroblastoma cells. Their properties well correponded to those proposed in the degradation by the cells. One of the cysteine proteases shows strict specificity toward paired basic amino acid residues.
3. LHRH fragment (1-5)-generating enzyme as well as angiotensin-converting enzyme has been purified from neuroblastoma cells. The former enzyme has been characterized as a mataloprotease whose sulfhydryl groups seem to be essential for the maintenance of the full activity.
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Research Products
(11 results)
