Project/Area Number |
04671384
|
Research Category |
Grant-in-Aid for General Scientific Research (C)
|
Allocation Type | Single-year Grants |
Research Field |
Biological pharmacy
|
Research Institution | NATIONAL INSTITUTE OF HEALTH |
Principal Investigator |
KITAGAWA Takayuki NATIONAL INSTITUTE OF HEALTH, DEPARTMENT OF BIOCHEMISTRY AND CELL BIOLOGY, LABORATORY CHIEF, 細胞化学部, 室長 (80092188)
|
Co-Investigator(Kenkyū-buntansha) |
MASUMI Atsuko INVESTIGATOR, DEPARTMENT OF SAFETY RESEARCH ON BIOLOGICS, 安全性研究部, 研究員 (70165728)
AKAMATSU Yuzuru DIRECTOR, DEPARTMENT OF BIOCHEMISTRY AND CELL BIOLOTY, 細胞化学部, 部長 (00072900)
|
Project Period (FY) |
1992 – 1993
|
Project Status |
Completed (Fiscal Year 1993)
|
Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1993: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1992: ¥1,300,000 (Direct Cost: ¥1,300,000)
|
Keywords | GLUCOSE TRANSPORT / GLUT1 PROTEIN / GLYCOSYLATION / GROWTH FACTORS / TGF geta / HUMAN TUMOR CELLS / TUMOR SUPPRESSOR GENE / グルコース輸送活性 / N-結合型糖鎖修飾 / TGFbeta / ヒトがん病態 / 糖輸送 / 糖輸送タンパク質 / 細胞増殖因子 / TGF-β / マウス線維芽細胞 |
Research Abstract |
GLUT1, a 55 kDa glycoprotein glucose transporter present in the plasma membranes of braink erythrocytes and several fibroblasts, mediates glucose uptake of memmalian cells in a facilitative diffusion manner. In the present studies we observed that the expression of GLUT1 mRNA and protein in the mouse 3T3 fibroblasts were stimulated by an active growth factor TGF-beta1. TGF-beta1 also modulated the glycosylation of the GLUT1 protein, which resulted in the expression of a larger 65 kDa GLUT1 with a higher affinity for D-glucose. Studies with glycosidases and lectins indicated that the asparagine-loinked oligosaccharides of the GLUT1 protein were altered by TGF-beta1 leading to more branched and/or repeated polylactosamine chains. Modulation of the GLUT1 glycosylation with the increased affinity for D-glucose was also found in malignant human cell lines and this was strongly associated with an unidentified tumor suppressor gene present in the human chromosome11. Futher studies on the analysis of the modulated glycosylation of the GLUT1 protein and on the tumor suppressor function are in progress.
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