PROSTATIC EPIDERMAL GROWTH-FACTOR RECEPTORS AND THEIR REGULATION BY ANDROGENS
PROSTATIC EPIDERMAL GROWTH-FACTOR RECEPTORS AND THEIR REGULATION BY ANDROGENS
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DOI:
10.1210/endo-121-4-1461
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发表时间:
1987-10-01
期刊:
影响因子:
4.8
通讯作者:
WOTIZ, HH
中科院分区:
文献类型:
--
作者:
TRAISH, AM;WOTIZ, HH
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.alpha.-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.alpha.-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.