Molecular biological investigation of novel serine protease from rat pancreas, and its significance as a biological marker of pancreatic disease
| Project/Area Number |
12670508
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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 |
Gastroenterology
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| Research Institution | Kyoto Prefectural University of Medicine |
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Principal Investigator |
KATAOKA Keisho Kyoto Prefectural University of Medicine, the tided department of internal medicine, Leaner, 医学部, 講師 (70185792)
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| Project Period (FY) |
2000 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥3,800,000 (Direct Cost: ¥3,800,000)
Fiscal Year 2002: ¥200,000 (Direct Cost: ¥200,000)
Fiscal Year 2001: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 2000: ¥3,100,000 (Direct Cost: ¥3,100,000)
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| Keywords | chymopasin / serine protease / pancreatic enzyme / recombinant protein / substrate specificity / ELISA / Chymopasin / Serine protease / Chymotrypsin like enzyme-1 |
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| Research Abstract |
A novel serine protease specific to rat pancreas was cloned and designated chymopasin. The open reading frame of rat chymopasin consisted of 792 bp encoding 264 amino acid residues. The deduced amino acid sequence contained the essential catalytic triad characteristic of the serine protease family. The amino acid sequence of rat chymopasin showed 54.5% identity to rat chymotrypsin B. northern blot analysis showed that the transcript was strongly evpressed in the pancrreas. In situ hybridization with digoxigenin labeled Crna probe showed that the positive signals were observed in the acinar cells, but not in the islet or duct cells. Chymopasin protein was detected in the pancreas homogenate and bile-pancreatic juice. Further, Caerulein stimulated the secretion of rat chymopasin into bile-pancreatic juice. These results suggested that rat chymopasin might be a digestive enzyme secreted from the acinar cells. From the enzyme assay using synthetic subsrates, the purified recombinant chymopasin expressed in escherichi coil showed chymotrypsin like activity. In addition, rat recombinant chymopasin showed fibrinolytic and gelatinolytic activity. These results suggested a role in the pathogenesis of pancreatic damage. Rat chymopasin may be a potentially new biological marker for the evaluation of the pancreatic diseases in rat models
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Report
(4 results)
Research Products
(16 results)
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[Publications] Sogame Y, Kataoka K, Kato M, Sakagami J, Osawa S, Takatera A, Mitsuyoshi M, Usui N, Mitsui S, Yamaguchi N.: "Molecular cloning and characterization of chymopasin, a novel serine protease from rat pancreas"Pancreas. 25・4. 378-386 (2002)
Description
「研究成果報告書概要(和文)」より
Related Report
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[Publications] Sogame Y, Kataoka K, Kato M, Sakagami J, Osawa S, Takatera A, Mitsuyoshi M, Usui N, Mitsui S, Yamaguchi N.: "Molecular cloning and characterization of chymopasin, a novel serine protease from rat pancreas"Pancreas. 25・4. 378-386 (2002)
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