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Department of Biochemistry, Boston University School of Medicine Boston, Massachusetts 02118
Address requests for reprints to: Dr. Abdulmaged Traish, Department of Biochemistry, Boston University, 80 East Concord Street, Boston, Massachusetts 02118.
Abstract
Prostatic membranes contain high affinity [dissociation constant (KD) = 1.16 nM], saturable binding sites for [125I]iodo-epidermal growth factor (EGF). The binding of [125I] iodo-EGF is specific since it is displaced by excess EGF but not by insulin, fibroblast growth factor, platelet-derived growth factor, or multiplication-stimulating activity. Affinity labeling with [125I]iodo-EGF and subsequent cross-linking with disuccinimidyl suberate demonstrated the specific binding of [125I]iodo-EGF to a macromolecule with a mol wt of 170,000. Castration of mature rats resulted in a 3- to 6-fold increase in [125I]iodo-EGF binding, while treatment of 7-day castrated rats with 5
-dihydrotestosterone decreased the number of binding sites. Administration of estrogen or progesterone produced a slight decrease in EGF binding sites but not nearly to the extent observed with 5-dihydrotestosterone, suggesting that the observed effect is androgen specific. These results demonstrate that rat prostate contains specific binding sites for EGF and that their level is modulated by androgens. (Endocrinobgy 121:1461–1467,1987)
Footnotes
* This investigation was supported by PHS grant CA-28856 awarded by the National Cancer Institute, DHHS. This is publication 134 from the Hubert H. Humphrey Cancer Research Center of Boston University.
Received January 27, 1987.
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