• Search Research Projects
  • Search Researchers
  • How to Use
  1. Back to previous page

MOLECULAR MECHANISMS FOR REGULATION OF MAMMALIAN GLUCOSE TRANSPORTER EXPRESSION AND ITS FUNCTION

Research Project

Project/Area Number 06672225
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field Biological pharmacy
Research InstitutionNATIONAL INSTITUTE OF HEALTH,JAPAN

Principal Investigator

KITAGAWA Takayuki  DEPARTMENT OF BIOCHEMISTRY AND CELL BIOLOGY,NATIONAL INSTITUTE OF HEALTH,LABORATORY CHIEF, 細胞化学部, 室長 (80092188)

Co-Investigator(Kenkyū-buntansha) YAMAKAWA Yoshio  NATL INST HEALTH,of JAPAN,Chief Investigator, 細胞化学部, 主任研究官 (50100102)
KITAGAWA Takayuki  NATL INST HEALTH,of JAPAN,Laboratory Chief (80092188)
Project Period (FY) 1994 – 1995
Project Status Completed (Fiscal Year 1995)
Budget Amount *help
¥2,300,000 (Direct Cost: ¥2,300,000)
Fiscal Year 1995: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1994: ¥1,400,000 (Direct Cost: ¥1,400,000)
KeywordsGLUCOSE TRANSPORTER / N-LINKED GLYCOPROTEIN / TUMOR SUPPRESSOR / HUMAN TUMOR CELLS / CA VEOLIN / MEMBRANE PROTEINS / グルコース輸送 / ヒトがん細胞
Research Abstract

Glucose uptake in mammalian cells is mediated by an integral membrane protein called as a glucose transporter which is an N-linked glycoprotein with molecular mass of about 50 kDa.We have previously demonstrated that glucose uptake in mammalian cells is regulated by growth factors-dependent expression of a brain-type glucose transporter GLUT1 as well as its glycosylation change which modulates affinity to D-glucose.In the present research we have studied changes in GLUT1 expression in human tumor cells using human cell hybrids which have provied an evidence that the tumorigenicity of a cervical carcinoma HeLa is under the control of a putative tumor suppressor in chromosome 11, and found a tumor-associated glycosylation change in GLUT1.
An non-tumorigenic HeLa x fibroblast cell hybrid expressed the 50-55 kDa GLUT1, whereas in a tumorigenic segregant, GLUT1 glycosylation was altered and its molecular mass was about 70 kDa.Further studies on the oligosaccharides revealed that this glycosylation change in GLUT1 was mainly due to the increase in N-acetyl-lactosamine repeats in the oligosaccharides.In accordance with altered glycosylation, affinity for 2-deoxyglucose in the tumorigenic hybrid cells increased 2-fold, but there was little change in the Vmax.These results suggest that there may be a functional role for the modulation of GLUT glycosylation in the tumorigenic behavior of human tumor cells.
Subsequent studies on these human cell hybrids indicated that expression of another integral membrane protein caveolin, which is a major component of a caveolae structure in the plasma membrane, decreased in a tumorigenic hybrid cells.Further studies on the role of this caveolin expression in tumorigenicity and tumor suppressor function of HeLa cells are carried out.

Report

(3 results)
  • 1995 Annual Research Report   Final Research Report Summary
  • 1994 Annual Research Report
  • Research Products

    (4 results)

All Other

All Publications (4 results)

  • [Publications] A. Masumi, Y. Akamatsu and Takayuki Kitagawa: "Alteration by transforming growth factor-β1 of asparagine-linked sugar chains in glucose transporter protein in Swiss 3T3 cells." Biochimica et Biophysica Acta. 1221. 330-338 (1994)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] Takayuki Kitagawa, et al.,: "A tumor associated glycosylation chang in the glucose transporter GLUT1 controlled by tumor suppressor function in human cell hybrids." Journal of Cell Science. 108. 3735-3743 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1995 Final Research Report Summary
  • [Publications] T. Kitagawa,et al.: "Atumor-associated glycosylation chanqe in the qlucose transporter GLUT1 controlled by tumor suppressor function in human cell hybrids" J. Cell Sci.108. 3735-3743 (1995)

    • Related Report
      1995 Annual Research Report
  • [Publications] A.Masumi,Y.Akamatsu & T.Kitagawa: "Alteration by TGF-β1 of asparagine-linked sugar chains in glucose transporter protein in Swiss 3T3 cells." Biochim.Biophys.Acta,. 1221. 330-338 (1994)

    • Related Report
      1994 Annual Research Report

URL: 

Published: 1994-04-01   Modified: 2016-04-21  

Information User Guide FAQ News Terms of Use Attribution of KAKENHI

Powered by NII kakenhi