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Journal of Clinical Endocrinology & Metabolism, Vol 60, 1243-1249, Copyright © 1985 by Endocrine Society
ARTICLES |
WE Simon, VG Pahnke and F Holzel
This study demonstrates the specific binding of human (h) PRL to mammary carcinoma cells of the newly established line EFM-19. Under saturating conditions, [125I]hPRL bound to these cells with high affinity (Ka = 4.3 X 10(10) M-1) and low capacity (4080 binding sites/cell). In serum-free medium, stimulation of cell proliferation by PRL was found, suggesting a biological role in the growth of human breast cancer. hPRL was more effective in binding to and promoting the growth of EFM-19 cells than ovine PRL or other lactogenic hormones. Up- and down-regulation of [125I]hPRL binding occurred after pretreatment of EFM-19 cell cultures with subphysiological or higher hPRL concentrations, respectively. Physiological concentrations of 17 beta- estradiol or dihydrotestosterone increased the cellular capacity of hPRL binding. Pharmacological concentrations of dihydrotestosterone or physiological concentrations of progesterone reduced the binding of [125I]hPRL. The results provide evidence for complex regulatory mechanisms of PRL binding by human mammary carcinoma cells involving steroid hormones.
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