Pettersson K, Vanharanta R, Söderholm J, Punnonen R, Lövgren T
J Steroid Biochem. 1982 Mar;16(3):369-72. doi: 10.1016/0022-4731(82)90047-4.
When small amounts of trypsin were added to prelabelled estrogen receptors in 24 human breast cancer cytosols there was a substantial increase in the binding capacity [79 +/- 11 (SE)%]. At the same time the affinity of the hormone receptor interaction was maintained at a very high level or even increased. This finding is discussed in relation to previous results where a diisopropylfluorophosphate (DFP) inhibitable protease activity was shown to cause a similar augmentation of estrogen binding sites in human myometrial cytosols. Addition of sodiummolybdate at or immediately after homogenization led to a similar increase in estrogen binding sites. Because these two effects were not additive we propose that the limited trypsin treatment reactivates the binding sites previously inactivated through a mechanism which can be inhibited by sodiummolybdate.
当向24份人乳腺癌细胞溶质中预先标记的雌激素受体添加少量胰蛋白酶时，结合能力显著增加[79±11(标准误)%]。与此同时，激素受体相互作用的亲和力维持在非常高的水平，甚至有所增加。结合之前的研究结果对这一发现进行了讨论，在之前的研究中，二异丙基氟磷酸酯（DFP）可抑制的蛋白酶活性被证明可导致人子宫肌层细胞溶质中雌激素结合位点出现类似的增加。在匀浆时或匀浆后立即添加钼酸钠会导致雌激素结合位点出现类似的增加。由于这两种效应并非相加关系，我们提出有限的胰蛋白酶处理可通过一种能被钼酸钠抑制的机制使先前失活的结合位点重新激活。
