Loss of a Putative Tumor Suppressor Locus after Gamma-Ray-Induced Neoplastic Transformation of HeLa × Skin Fibroblast Human Cell Hybrids

1995 ◽  
Vol 143 (1) ◽  
pp. 34 ◽  
Author(s):  
Marc S. Mendonca ◽  
Clare L. Fasching ◽  
Eri S. Srivatsan ◽  
Eric J. Stanbridge ◽  
J. Leslie Redpath
Keyword(s):  
Tumor Suppressor ◽  
Human Cell ◽  
Skin Fibroblast ◽  
Gamma Ray ◽  
Neoplastic Transformation ◽  
Cell Hybrids ◽  
Putative Tumor Suppressor

Loss of Suppressor Loci on Chromosomes 11 and 14 May Be Required for Radiation-Induced Neoplastic Transformation of HeLa × Skin Fibroblast Human Cell Hybrids

1998 ◽  
Vol 149 (3) ◽  
pp. 246 ◽  
Author(s):  
Marc S. Mendonca ◽  
Kelly Howard ◽  
Clare L. Fasching ◽  
Daphne L. Farrington ◽  
Lael A. Desmond ◽  
...  
Keyword(s):  
Human Cell ◽  
Skin Fibroblast ◽  
Neoplastic Transformation ◽  
Cell Hybrids ◽  
Radiation Induced

A tumor-associated glycosylation change in the glucose transporter GLUT1 controlled by tumor suppressor function in human cell hybrids

1995 ◽  
Vol 108 (12) ◽  
pp. 3735-3743 ◽  
Author(s):  
T. Kitagawa ◽  
Y. Tsuruhara ◽  
M. Hayashi ◽  
T. Endo ◽  
E.J. Stanbridge
Keyword(s):  
Tumor Suppressor ◽  
Human Cell ◽  
Hela Cells ◽  
Glucose Transporter ◽  
Tumor Suppressor Function ◽  
Cell Hybrids ◽  
Putative Tumor Suppressor ◽  
Glycosylation Change ◽  
Glucose Transporter Glut1 ◽  
Transporter Glut1

Studies of human cell hybrids have provided evidence that the tumorigenicity of a cervical carcinoma (HeLa) is under the control of a putative tumor suppressor on chromosome 11. Using these human cell hybrids, we found a tumor-associated glycosylation change in the glucose transporter GLUT1, which is an N-linked glycoprotein at the plasma membrane. The non-tumorigenic HeLa × fibroblast cell hybrid CGL1 and the normal diploid fibroblast WI38 expressed the 50–55 kDa GLUT1, whereas in a tumorigenic segregant hybrid, CGL4, as well as in parental HeLa cells, GLUT1 glycosylation was altered and its molecular mass was about 70 kDa. However, the altered GLUT1 glycosylation was not observed in SV40-transformed WI38 cells, suggesting a correlation between this glycosylation change and a putative tumor suppressor function. Further investigations using glycosidases, glycosylation inhibitors and lectin-affinity chromatography demonstrated that the tumor-associated glycosylation change in GLUT1 was mainly due to the increase in N-acetyl-lactosamine repeats in the N-linked oligosaccharides. In accordance with the altered glycosylation, affinity for 2-deoxyglucose in the tumorigenic CGL4 cells increased 2-fold, but there was little change in the Vmax. These results suggest there may be a functional role for the modulation by glycosylation of GLUT1 in the tumorigenic behavior of CGL4 and HeLa cells.

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