Biological thiols elicit prolactin proteolysis by glandular kallikrein and permit regulation by biochemical pathways linked to redox control.
Biological thiols elicit prolactin proteolysis by glandular kallikrein and permit regulation by biochemical pathways linked to redox control.
复制标题
生物硫醇通过腺激肽释放酶引起催乳素蛋白水解，并允许通过与氧化还原控制相关的生化途径进行调节。
DOI：
10.1021/bi00245a002
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发表时间：
1991
期刊：
影响因子：
2.9
通讯作者：
Powers,CA
中科院分区：
文献类型：
--
作者：
Hatala,MA;DiPippo,VA;Powers,CA
纽约医学院药学系，Valhalla, New York 10595摘要：大鼠腺激肽酶（GK）是一种胰蛋白酶样丝氨酸蛋白酶，可在体外将大鼠泌乳素（PRL）裂解为体内可检测的新形式，可能具有生理意义。GK对PRL的蛋白水解依赖于硫醇，硫醇作用于PRL使分子重新折叠成新的构象，即GK底物。本研究比较了几种天然硫醇和合成硫醇诱导GK水解PRL蛋白的能力。将大鼠PRL与大鼠GK在各种硫醇和0.5% Triton X-100的存在下孵育，以增强硫醇诱导的蛋白水解。凝胶电泳分析了还原和非还原条件下的裂解情况。在Triton X-100存在下，所有的低分子量硫醇都能被GK诱导裂解PRL。效价顺序为二硫苏糖醇、巯基乙醇、硫辛酸、半胱胺
Department of Pharmacology, New YorkMedical College, Valhalla, New York 10595 Received February 4, 1991; Revised Manuscript Received May 22, 1991 abstract: Rat glandular kallikrein (GK), a trypsin-like serine protease, cleaves rat prolactin (PRL) in vitro to novel forms detectable in vivo and likely to be of physiological significance. PRL proteolysis by GK is thiol-dependent, with thiols acting upon PRL to refold the molecule into novel conformationsthat are GK substrates. This study compared several natural and synthetic thiolsfor their ability to elicit PRL proteolysis by GK. Rat PRL was incubated with rat GK in the presence of various thiols and 0.5% Triton X-100, which enhances thiol-elicited proteolysis. Cleavage was analyzed by gel electrophoresis under reducing and nonreducing conditions. In the presence of Triton X-100, all low molecular weight thiols elicited PRL cleavage by GK. The order of potency was dithiothreitol> mercaptoethanol> lipoic acid> cysteamine