Laboratory of Molecular Biology, Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University Kyoto, Japan.
Front Pharmacol. 2011 Oct 13;2:58. doi: 10.3389/fphar.2011.00058. eCollection 2011.
Proteins are capable of sensing the redox status of cells. Cysteine residues, which react with oxidants, reductants, and electrophiles, have been increasingly recognized as the mediators of this redox sensitivity. Cation channels encoded by the transient receptor potential (trp) gene superfamily are characterized by a wide variety of activation triggers that act from outside and inside the cell. Recent studies have revealed that a class of TRP channels is sensitive to changes in redox status and is notably susceptible to modifications of cysteine residues, such as oxidation, electrophilic reaction, and S-nitrosylation of sulfhydryls. In this review, we focus on TRP channels, which directly sense redox status, and discuss the biological significance of cysteine modifications and the consequences of this chemical reaction for physiological responses.
蛋白质能够感知细胞的氧化还原状态。半胱氨酸残基与氧化剂、还原剂和亲电试剂反应,已被越来越多地认为是这种氧化还原敏感性的介质。瞬时受体电位 (TRP) 基因超家族编码的阳离子通道的特点是具有多种多样的激活触发因素,这些触发因素来自细胞内外。最近的研究表明,一类 TRP 通道对氧化还原状态的变化敏感,并且特别容易受到半胱氨酸残基修饰的影响,例如氧化、亲电反应和巯基的 S-亚硝基化。在这篇综述中,我们重点介绍直接感知氧化还原状态的 TRP 通道,并讨论半胱氨酸修饰的生物学意义以及这种化学反应对生理反应的后果。