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
WOTIZ, HH
中科院分区:
医学2区
文献类型:
--
作者:
TRAISH, AM;WOTIZ, HH

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前列腺膜含有高亲和力[解离常数(KD)= 1.16 nM],[125 I]碘-表皮生长因子(EGF)的可饱和结合位点。[125 I]碘-EGF的结合是特异性的,因为它被过量的EGF取代,但不被胰岛素、成纤维细胞生长因子、血小板衍生生长因子或增殖刺激活性取代。亲和标记与[125 I]碘-EGF和随后的交联与disuccinimidyl辛二酸证明了特异性结合的[125 I]碘-EGF的大分子与分子量为170,000。成熟大鼠的去势导致[125 I]碘-EGF结合增加3至6倍,而用5 α-碘-EGF处理7天的去势大鼠,双氢睾酮减少结合位点的数目。雌激素或孕酮的给药使EGF结合位点略有减少,但没有达到用5 α-EGF所观察到的程度。这表明观察到的作用是雄激素特异性的。这些结果表明,大鼠前列腺含有EGF的特异性结合位点,其水平受雄激素调节。
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.