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首页> 外文期刊>Biochemistry >Reversible change in thiol redox status of the insulin receptor alpha-subunit in intact cells.
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Reversible change in thiol redox status of the insulin receptor alpha-subunit in intact cells.

机译：完整细胞中胰岛素受体α-亚基的巯基氧化还原状态的可逆变化。

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In this study, we used maleimidobutyrylbiocytin to examine possible alteration that may occur in the redox state of the insulin receptor (IR) sulfhydryl groups in response to reduced glutathione (GSH) or N-acetyl-L-cysteine (NAC). Short-term treatment of intact cells expressing large numbers of IR with GSH or NAC led to a rapid and reversible reduction of IR alpha-subunit disulfides, without affecting the receptor beta-subunit thiol reactivity. The overall integrity of the oligomeric structure of IR was maintained, indicating that neither class I nor class II disulfides were targeted by these agents. Similar findings were obtained in cells transfected with IR mutants lacking cysteine524, one of the class I disulfides that link the two IR alpha-subunits. Membrane-associated thiols did not participate in GSH- or NAC-mediated reduction of IR alpha-subunit disulfides. No difference in insulin binding was observed in GSH-treated cells; however, ligand-mediated increases in IR autophosphorylation, tyrosine phosphorylation of cellular substrates, and dual phosphorylation of the downstream target mitogen-activated protein kinase were inhibited at concentrations of GSH (10 mM or greater) that yielded a significant increase in IR alpha-subunit thiol reactivity. GSH did not affect IR signaling in the absence of insulin. Our results provide the first evidence that the IR alpha-subunit contains a select group of disulfides whose redox status can be rapidly altered by the reducing agents GSH and NAC.
机译：在这项研究中，我们使用了马来酰亚胺基丁酰生物胞素来检查响应还原型谷胱甘肽（GSH）或N-乙酰基-L-半胱氨酸（NAC）而在胰岛素受体（IR）巯基的氧化还原状态中可能发生的变化。用GSH或NAC短期处理表达大量IR的完整细胞会导致IRα-亚基二硫键快速且可逆地降低，而不会影响受体β-亚基硫醇反应性。 IR的寡聚结构的整体完整性得以维持，表明这些试剂既不靶向I类也不适用II类二硫化物。在用缺少半胱氨酸524（连接两个IRα亚基的I类二硫键之一）的IR突变体转染的细胞中获得了类似的发现。膜相关的硫醇不参与GSH或NAC介导的IRα亚基二硫化物的还原。在经GSH处理的细胞中未观察到胰岛素结合的差异。但是，在GSH（10 mM或更高）的浓度下，配体介导的IR自磷酸化，细胞底物酪氨酸磷酸化和下游靶丝裂原活化蛋白激酶的双重磷酸化增加受到抑制，从而导致IRα亚基显着增加。硫醇反应性。在没有胰岛素的情况下，GSH不会影响IR信号传导。我们的结果提供了第一个证据，表明IRα亚基包含一组选定的二硫键，其氧化还原状态可以通过还原剂GSH和NAC迅速改变。

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