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Volume 272, Number 14, Issue of April 4, 1997 pp. 9275-9279
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Gene Transfection-mediated Overexpression of 1,4-N-Acetylglucosamine Bisecting Oligosaccharides in Glioma Cell Line U373 MG Inhibits Epidermal Growth Factor Receptor Function

(Received for publication, December 17, 1996, and in revised form, February 10, 1997)

From the Brain Tumor Research Program, Children's Memorial Hospital, Chicago Institute for Neurosurgery and Neuroresearch, Chicago, Illinois 60614 and the ^§ Osaka University Medical School, Osaka 565, Japan

N-linked oligosaccharides appear to be important for the function of the epidermal growth factor (EGF) receptor. In a previous study (Rebbaa, A., Yamamoto, H., Moskal, J. R., and Bremer, E. G. (1996) J. Neurochem. 67, 2265-2272), we showed that binding of the erythroagglutinating phytohemagglutin lectin from Phaseolus vulgaris to the bisecting structures on the EGF receptor from U373 MG glioma cells blocked EGF binding and receptor autophosphorylation. In this study we examined the consequences of overexpression of the bisecting structure on the EGF receptor by gene transfection of U373 MG cells with the N-acetylglucosaminyltransferase III (GnT-III). This modification leads to a significant decrease in EGF binding and EGF receptor autophosphorylation. In addition, the cellular response to EGF was found to be altered. Proliferation of U373 MG cells in serum-free medium is inhibited by EGF. In contrast, proliferation of the GnT-III-transfected cells was stimulated by EGF. These data demonstrate that changes in EGF receptor glycosylation by GnT-III transfection reduces the number of the active receptors in U373 MG cells and that this change results in change in the cellular response to EGF.

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