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Epidermal Growth Factor Binding and Protein Kinase C Activities in Human Breast Cancer Cell Lines: Possible Quantitative Relationship¹

Laboratory of Biochemistry-Endocrinology, Department of Research, and Department of Gynecology and Obstetrics, University Clinic Medical School, CH-4031 Basel, Switzerland

Quantitative polyacrylamide gel electrophoresis analysis of Ca²⁺, phospholipid-dependent protein kinase (PKC) of human mammary tumor cell lines (MCF-7, ZR-75, T-47-D, MDA-MB-231, BT-20, and HBL-100) revealed that 80% of the total cellular PKC resided in the cytosol. The tumor cells with no detectable levels of estrogen receptors (MDA-MB-231, HBL-100, and BT-20 cells) exhibited significantly larger (P < 0.001) cytosolic PKC activities than those cells that contained estrogen receptors (MCF-7, T-47-D, and ZR-75 cells). In addition, in estrogen receptor-negative cell lines, relatively high levels of specific low-affinity (appearent K_d = 700 pM) epidermal growth factor (EGF) binding activities were found as compared with estrogen receptor-positive cells with significantly (P < 0.001) lower levels of specific high-affinity (apparent K_d = 90 pM) EGT binding. A significant positive correlation (P < 0.01) was observed between the number of EGF receptor (R_s = 0.50) and/or the EGF receptor dissociation constants (R_s = 0.78) with the cytosolic PKC activity levels. These data indicate that, in human breast cancer cells, a positive relationship may exist between PKC activity, estrogen, and EGF receptors.

¹ This work was supported in part by the Swiss Cancer League, Grant FOR-249.AK.83(6), and by the Swiss National Science Foundation, Grant 3.409.0.83, as well as by CIBA-GEIGY Ltd., Basel, Switzerland.

² To whom requests for reprints should be addressed at Universitäts-Frauenklinik, Laboratorien, CH-4031 Basel, Switzerland.

Received 5/14/85. Revised 9/12/85. Revised 1/31/86. Accepted 2/11/86.

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