Transport of glutathione transferase-fold structured proteins into living cells
Transport of glutathione transferase-fold structured proteins into living cells
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DOI：
10.1016/j.bbamem.2008.10.018
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发表时间：
2009-03-01
影响因子：
3.4
通讯作者：
Casarotto, Marco G.
中科院分区：
文献类型：
--
作者：
Morris, Melanie J.;Craig, Scott J.;Casarotto, Marco G.
谷氨酸转移酶是传统上已知有助于第11阶段解毒反应的酶家族。然而，日本血吸虫谷胱甘肽转移酶（Sj.GST 26）的一个新特性涉及其从外部介质易位到各种不同的细胞类型。在这里，我们探讨了这类蛋白质进入细胞的效率和机制。使用流式细胞术和共聚焦显微镜，我们已经研究了在各种条件下Sj.GST 26内化到活细胞中，这些条件旨在阐明细胞摄取的模式。我们的研究结果表明，Sj.GST26可以有效地进入细胞，通过能量依赖性事件，涉及内吞作用。更具体地说，发现Sj.GST 26与细胞内的转铁蛋白共定位，表明内吞过程涉及网格蛋白包被的凹坑。还对GST结构超家族中其他类别的蛋白质的细胞内化进行了全面研究。这些实验表明，“GST折叠”结构基序影响细胞摄取，这提出了一个新的一瞥到一个未知的方面GST功能。(C)2008 Elsevier B.V.保留所有权利。
Glutathione transferases are a family of enzymes that are traditionally known to contribute to the phase 11 class of detoxification reactions. However, a novel property of the Schistosoma japonicum glutathione transferase (Sj.GST26) involves its translocation from the external medium into a variety of different cell types. Here we explore the efficiency and mechanism of cell entry for this class of protein. Using flow cytometry and confocal microscopy, we have examined the internalisation of Sj.GST26 into live cells under a variety of conditions designed to shed light on the mode of cellular uptake. Our results show that Sj.GST26 can effectively enter cells through an energy-dependent event involving endocytosis. More specifically, Sj.GST26 was found to colocalise with transferrin within the cell indicating that the endocytosis process involves clathrin-coated pits. A comprehensive study into the cellular internalisation of proteins from other classes within the GST structural superfamily has also been conducted. These experiments suggest that the 'GST-fold' structural motif influences cellular uptake, which presents a novel glimpse into an unknown aspect of GST function. (C) 2008 Elsevier B.V. All rights reserved.