RLIP76催化谷胱甘肽共轭物的ATP依赖性转运的功能重建。
Functional reconstitution of RLIP76 catalyzing ATP-dependent transport of glutathione-conjugates.
作者信息
Singhal Sharad S, Sehrawat Archana, Mehta Amee, Sahu Mukesh, Awasthi Sanjay
机构信息
Department of Molecular Biology and Immunology, University of North Texas Health Science Center, Fort Worth, TX 76107-2699, USA.
出版信息
Int J Oncol. 2009 Jan;34(1):191-9.
Abstract
RLIP76, a stress-responsive, multi-functional protein with multi-specific transport activity towards glutathione-conjugates (GS-E) and chemotherapeutic agents is frequently overexpressed in malignant cells. Our recent studies suggest that it plays a prominent anti-apoptotic role selectively in cancer cells. The present studies were performed to compare RLIP76 activity towards glutathione-conjugates in recombinant and K562 human erythroleukemia cells. The purity and identity of recombinant and K562 RLIP76 was established by SDS-PAGE and Western blot analysis. These studies confirmed the origin of the 38 kDa protein, previously referred to as DNP-SG ATPase, from RLIP76. Comparison of ATPase activity and transport kinetics for DNP-SG and GS-HNE between recombinant vs. K562 RLIP76 revealed higher specific activity of ATPase and transport for recombinant purified RLIP76, indicating that additional factors present in recombinant purified RLIP76 can modulate its transport activity.
摘要
RLIP76是一种应激反应性多功能蛋白，对谷胱甘肽结合物（GS-E）和化疗药物具有多特异性转运活性，在恶性细胞中经常过度表达。我们最近的研究表明，它在癌细胞中选择性地发挥着突出的抗凋亡作用。本研究旨在比较重组细胞和K562人红白血病细胞中RLIP76对谷胱甘肽结合物的活性。通过SDS-PAGE和蛋白质免疫印迹分析确定了重组RLIP76和K562 RLIP76的纯度和特性。这些研究证实了先前称为DNP-SG ATP酶的38 kDa蛋白源自RLIP76。重组RLIP76与K562 RLIP76之间DNP-SG和GS-HNE的ATP酶活性及转运动力学比较显示，重组纯化的RLIP76具有更高的ATP酶比活性和转运活性，表明重组纯化的RLIP76中存在的其他因子可调节其转运活性。
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