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Epidermal Growth Factor Inhibits the Proliferation of a Human Endometrial Carcinoma Cell Line^*

Departments of Medicine, Unversity of Arizona College of Medicine Tucson, Arizona 85724
Obstetrics and Gynecology, Unversity of Arizona College of Medicine Tucson, Arizona 85724

Address all correspondence and requests for reprints to: Dr. Murray Korc, Department of Medicine, University of Arizona College of Medicine, Tucson, Arizona 85724.

Specific epidermal growth factor (EGF) receptors were measured in RL95-2 human endometrial carcinoma cells. At 37 C, binding of ¹²⁵I-labeled EGF was associated with marked ligand internalization. Maximal cell surface binding occurred within 10 min. Bound [¹²⁵I]EGF was partially degraded to low mol wt products, and this degradation was blocked by the lysosomotropic compound ammonium chloride. At 4 C, maximal cell surface binding occurred at 3 h. Scatchard analysis of data obtained after 3 h at 4 C revealed a single order of binding sites with a K_d of 1.8 nM and approximately 150,000 surface receptors/cell. EGF, at a concentration of 0.83 nM, inhibited the proliferation of RL95-2 cells. Inhibition was reversible and was associated with morphological changes leading to a fusiform appearance of the growth-arrested cells. These findings indicate that RL95-2 human endometrial carcinoma cells bind, internalize, and degrade EGF in a manner similar to that described for other target cells for EGF action. The ability of EGF to inhibit the growth of RL95-2 cells supports the hypothesis that this type of inhibition is dependent on postreceptor events, rather than on the presence of an overabundance of EGF receptors.

^* This work was supported in part by NIH Grants AM-32561 (to M.K.) and CA-40162 (to M.K.).

Received October 10, 1985.

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