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Cloning and Subcellular Localization of GalNAc Transferase

Research Project

Project/Area Number 08044299
Research Category

Grant-in-Aid for international Scientific Research

Allocation TypeSingle-year Grants
SectionJoint Research
Research InstitutionKochi Medical School

Principal Investigator

NISHIMORI Isao  Kochi Medical School, Research Associate, 医学部, 助手 (30237747)

Co-Investigator(Kenkyū-buntansha) MORITA Masanori  Kochi Medical School, Research Associate, 医学部, 助手 (30191034)
ENZAN Hideaki  Kochi Medical School, Professor, 医学部, 教授 (00034645)
HOLLINGSWORT マイケル A  ネブラスカ州立大学メディカルセンター, エプリー癌研究所, 助教授
HOLLINGSWORTH Michacl A  University of Nebraska Medical Center, Eppley Cancer Institute, Associate Profes
HOLLINGSWORT マイケルエイ  ネプラスカ州立大学メディカルセンター, エプリー癌研究所, 助教授
Project Period (FY) 1996
Project Status Completed (Fiscal Year 1996)
Budget Amount *help
¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1996: ¥1,000,000 (Direct Cost: ¥1,000,000)
KeywordsGlycosyltransferase / Immunohistochemistry / N-acetylgalactosamine / cDNA / Pancreas cancer / Monoclonal antibody / Gastric cancer / Colon cancer / 免疫組織科学 / 膵臓
Research Abstract

1. We have obtained a cDNA clone of the human homologue of the UDP-N-acctylgalactosamine : polypeptide N-acetylgalactosaminyltransferase (GalNAc transferase). AcDNA sequence for human GalNAc transferase showed high homology with its bovine homelogue and was identical to human isozyme Tlthat was recently reported.
2. Twenty-three residues peptide was synthesized based on the obtained cDNA sequence and a mouse monoclonal antibody to the peptide (GNT-1) was successfully produced.
3. GNT-1 reacted with ductal epithelial cells of the exocrine organs including pancreas, salivary gland, bronchial gland, and mammary gland. Oherewise, GNT-1 had no reactivity with mucus cells of salivary gland and stomach. These results suggest that ductal epithelial cells and mucus cells have different types of GalNAc transferase. It was noteworthy that parietal cells of stomach and a large number of cells in Langerhans islands of pancreas showed nice reactivity with GNT-1, suggesting these cells produce O-glycosylated protein except for mucin.
4. Western immunoblotting with GNT-1 showed that the expression of GalNAc transferase T1 varies not only among organ types and cell type, but also according to cell differentiation.
5.Based on the results deceribed above, we plan to study the expression of GalNAc transferase T1 in various kinds of gastrointstinal disease and produce a monoclonal antibody to GalNAc transferase T2

Report

(2 results)
  • 1996 Annual Research Report   Final Research Report Summary
  • Research Products

    (3 results)

All Other

All Publications (3 results)

  • [Publications] Nishimori,Isao: "A monoclonal antibody against human UDP-GalNAc : polypeptide N-acetyl-galactosaminyltransferase and its reactivity with pancreatic and colon tumor cells." Gastroenterology. 110. A568- (1996)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Nishimori I,Kohsaki T,Morita M,Akizawa Y,Sano S,Onishi S,Hollingsworth MA.: "A monoclonal antibody against human UDP-GalNAc : polypeptide N-acetylgalactosaminyltransferase and its reactivity with pancreatic and colon tumor cells." Gastroenterology. 110. A568 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Nishimori I: "A monoclonal antibody against human UDP-GalNAc : polypeptide N-acetylgalactosaminyltransferase and its reactivity with pancreatic and colon tumor cells." Gastroenterology. 110. A568- (1996)

    • Related Report
      1996 Annual Research Report

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Published: 1996-04-01   Modified: 2016-04-21  

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