激素依赖性和非依赖性大鼠乳腺肿瘤细胞质中camp解离动力学。

F Y Tang, K Skerrett, D Heiman, N Ballatori
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引用次数: 5

摘要

比较了7,12 -二甲基苯(α)蒽诱导的具有不同激素反应性的大鼠乳腺肿瘤细胞溶胶的camp解离动力学。在22℃,pH 4.5, 1微米cAMP条件下,激素依赖性乳腺肿瘤表现出单相解离速率,速率常数为k-1 = 0.06 min-1。而非激素依赖型乳腺肿瘤呈现双相解离曲线,速率常数分别为k-1 = 0.47和k-2 = 0.06 min-1。cAMP的结合完全可逆;放射性标记配体被1mM的非放射性cAMP完全解离;经葡聚糖包被炭吸附后,结合蛋白可以重新结合到原来的结合水平。乳腺细胞质对cAMP表现出特异性结合,可被cGMP部分取代,但不能被ATP、ADP、AMP或腺苷取代。在孵育过程中,受体失活可以忽略不计。在22℃、pH 4.5、1微米cAMP (k+1 = 5-7 × 10(5)M-1 min-1)条件下,两种乳腺组织细胞质的关联率相似。这些数据表明乳腺组织的cAMP解离率为2。激素依赖型乳腺肿瘤具有高亲和力结合位点(k-1/k+1 = 0.07微米)的解离常数,而激素非依赖型乳腺肿瘤具有高亲和力(k-1/k+1 = 0.07微米)和低亲和力位点(k-1/k+1 = 0.05微米)的解离常数。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
CAMP-dissociation kinetics in hormone-dependent and -independent rat mammary tumor cytosols.

Cytosols from 7, 12-dimethylbenz (alpha) anthracene-induced rat mammary tumors which exhibit different hormone-responsiveness were compared with respect to their cAMP-dissociation kinetics. At 22 degree C, pH 4.5, 1 micrometer cAMP, hormone-dependent mammary tumors exhibited monophasic dissociation rates with a rate constant of k-1 = 0.06 min-1. In contrast, hormone-independent mammary tumors exhibited biphasic dissociation curves with rate constants of k-1 = 0.47 and k-2 = 0.06 min-1. The binding of cAMP was completely reversible; radio-labeled ligand was completely dissociated by 1mM nonradioactive cAMP; the binding protein could be reassociated to its original binding level after dextran-coated charcoal adsorption. The mammary cytosols exhibited specific binding for cAMP which could be displaced partially by cGMP but not by ATP, ADP, AMP, or adenosine. Receptor inactivation during the course of incubation was negligible. Both mammary tissue cytosols exhibited similar association rates at 22 degree C, pH 4.5, 1 micrometer cAMP (k+1 = 5-7 x 10(5)M-1 min-1). These data indicate that mammary tissues exhibit 2 cAMP dissociation rates. Hormone-dependent mammary tumors exhibit a dissociation constant of a high affinity binding site (k-1/k+1 = 0.07 micrometer) whereas hormone-independent mammary tumors exhibit dissociation constants of one high affinity (k-1/k+1 = 0.07 micrometer) and a second low affinity site (k-1/k+1 = 0.05 micrometer).

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