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[Cancer Research 51, 1294-1299, February 15, 1991]
© 1991 American Association for Cancer Research

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Upregulation of Epidermal Growth Factor Receptor Induced by {alpha}-Interferon in Human Epidermoid Cancer Cells1

Alfredo Budillon2, Pierosandro Tagliaferri, Michele Caraglia, Maria Rosaria Torrisi, Nicola Normanno, Stefano Iacobelli, Giovannella Palmieri, Maria Patrizia Stoppelli, Luigi Frati and Angelo Raffaele Bianco

Cattedra di Oncologia Medica, II Facoltà di Medicina, Università di Napoli, Napoli [A. B., P. T., M. C., N. N., G. P., A. R. B.]; Dipartimento di Medicina Sperimentale, Università La Sapienza, Roma [M. R. T., L. F.]; Cattedra di Oncologia Clinica, Università G. D'Annunzio, Chieti [S. I.]; and Istituto Internazionale di Genetica e Biofisica, Napoli [M. P. S.]; Italy

Unregulated or increased expression of epidermal growth factor receptor (EGF-R) is a common event in neoplastic transformation; modulation of such a receptor by physiological agents could be, therefore, of clinical interest. We have studied the binding ability, the availability at cell surface, and the synthesis of EGF-R in the A431 and KB human epidermoid cancer cell lines after treatment with recombinant {alpha}-interferon (IFN-{alpha}). After 48 h of treatment, IFN-{alpha} induces, in both cell lines, growth inhibition and enhances class I major histocompatibility HLA complex expression, which is a common marker of IFN action. [125I]EGF total binding assessed after 48 h of treatment with IFN-{alpha} shows a dose-dependent upregulation of EGF-R binding capacity. Saturation plots of the binding data show that IFN-{alpha} treatment does not dramatically alter the affinity of the EGF-R and indicate that IFN-{alpha} only increases the number of low affinity receptors. We show that this effect is due to a specific increase in the synthesis of the receptor protein, as assessed by immunoprecipitation of [35S]methionine-labeled cell extracts. Electron microscopy analysis has confirmed an increase of EGF-R proteins at cell surface without major changes in the morphology of the cells. Taken together, these results indicate that IFN-{alpha} consistently induces both the binding capacity and the synthesis of EGF-R in human epidermoid cancer cells and suggest the use of such a mechanism for new anticancer therapies.

1 Supported by the Italian Association for Cancer Research (AIRC).

2 To whom requests for reprints should be addressed, at Cattedra di Oncologia Medica, II Facoltà di Medicina, Università di Napoli, via S. Pansini 5, 80131, Napoli, Italy.

Received 8/ 9/90. Accepted 11/30/90.




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HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
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Molecular Cancer Research Cancer Prevention Research
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Copyright © 1991 by the American Association for Cancer Research.