| Project/Area Number |
08672552
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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 |
Biological pharmacy
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| Research Institution | National Institute of Infectious Diseases, Tokyo, Japan. |
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Principal Investigator |
KITAGAWA Takayuki NATIONAL INSTITUTE OF INFECTIOUS DESEASES (NIID), DEPARTMENT OF BIOCHEMISTRY AND CELL BIOLOGY,LABORATORY CHIEF, 細胞化学部, 室長 (80092188)
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| Co-Investigator(Kenkyū-buntansha) |
IWAZAKI Ayano NIID,JAPAN,Res.Associate, 細胞化学部, 協力研究員
SUZUKI Toshikazu Yokohama City Univ., Res.Associate, 生物研究所, 助手 (70270527)
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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 |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1997: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1996: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | GLUCOSE TRANSPORTER / N-LINKED GLYCOPROTEIN / TUMOR SUPPRESSOR / HUMAN TUMOR CELLS / CAVEOLIN / MEMBRANE PROTEINS / グルコース輸送タンパク質 / 11番染色体 |
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| Research Abstract |
Glucose uptake in mammalian cells is mediated by an integral membrane protein, glucose transporter, which is an N-linked glycoprotein with molecular mass of about 50 kDa. We have previously demonstrated a tumor-associated glycosylation change in glucose transporter-1 (GLUT1) with increased affinity to D-glucose in human cell hybrids between a cervical carcinoma HeLa and normal fibroblasts, whose tumorigenicity is under the control of a putative tumor suppressor in chromosome 11. In this study, we demonstrated this glycosylation change in GLUT1 in gamma-ray-induced tumorigenic mutants (GIMs) isolated from CGL1 cells as expressing a tumor-associated surface antigen, intestinal alkaline phosphatase. In contrast, GLUT1 in the gamma-irradiated nontumorigenic control cells (CONs) did not show this alteration. In accordance with this glycosylation change, affinity to 2-deoxyglucose in the GIM clone was increased by about 2-fold when compared to the nontumorigenic CON clone. These results further suggest a close correlation between the glycosylation change in GLUT1 with increased affinity to D-glucose and tumorigenicity of these human cell hybrids. We also found that the expression of caveolin, a principal protein component of caveolae structure in the plasma membrane, is greatly reduced in tumorigenic HeLa cell hybrids. Genetic linkage between these membrane changes and a putative tumor suppressor gene is under investigation.
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