| Project/Area Number |
05670486
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Gastroenterology
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| Research Institution | Kochi Medical School |
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Principal Investigator |
OKAZAKI Kazuichi Kochi Medical School, 医学部, 講師 (70145126)
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| Co-Investigator(Kenkyū-buntansha) |
MORITA Masanori Kochi Medical School, 医学部, 助手 (30191034)
NISHIMORI Isao Kochi Medical School, 医学部, 助手 (30237747)
YOKOYAMA Yuichi Kochi Medical School, 医学部, 助手 (30243843)
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| Project Period (FY) |
1993 – 1994
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| Project Status |
Completed (Fiscal Year 1994)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1994: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1993: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | cancer / mucin / stomach |
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| Research Abstract |
Abstract : We have previously studied the biosynthesis and secretion of mucin in the normal human stomach and reported that the tetramer of the 60-kDa subunit of mucin core protein was synthesized and highly glycosylated, and that only high molecular weight mucin was secreted. In this study, we investigated the mucin-related products of a gastric cancer cell line (Hs746T). Analysis of intracellular and extracellular products immunoprecipitated with an anti-apomucin monoclonal antibody revealed that a ll0-kDa protein, the dimer of the 55-kDa subunit, was synthesized and secreted. Tunicamycin treatment inhibited the secretion of the ll0-kDa protein. These findings suggest that N-glycosylation may be involved in the secretory mechanism of the mucin-related product.
charides, and some of these antigens have been used as tumor markers.^<3-7> Low molecular weight mucin-related products, as well as high molecular weight ones, can be detected in the serum of cancer patients.^<H-11> However, very little is known about the intracellular transport and secretory mechanisms of mucin-related products. In the present study. we examined this mechanism in a human gastric carcinoma cell line (Hs746T) and compared it to that in the normal gastric mucosa. After pulse-labeling with [^<35>S] methionine and chase incubation, we analyzed the intracellular and extracellular products with an anti-carboxyl terminal of the apomucin monoclonal anti-body.
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