通过热休克蛋白90、细胞血红素、可溶性鸟苷酸环化酶激动剂和一氧化氮对可溶性鸟苷酸环化酶的调节：新途径与临床前景
Regulation of sGC via hsp90, Cellular Heme, sGC Agonists, and NO: New Pathways and Clinical Perspectives.
作者信息
Ghosh Arnab, Stuehr Dennis J
机构信息
Department of Pathobiology, Lerner Research Institute , Cleveland Clinic, Cleveland, Ohio.
出版信息
Antioxid Redox Signal. 2017 Feb 1;26(4):182-190. doi: 10.1089/ars.2016.6690. Epub 2016 May 2.
Abstract
SIGNIFICANCE
Soluble guanylate cyclase (sGC) is an intracellular enzyme that plays a primary role in sensing nitric oxide (NO) and transducing its multiple signaling effects in mammals. Recent Advances: The chaperone heat shock protein 90 (hsp90) associates with signaling proteins in cells, including sGC, where it helps to drive heme insertion into the sGC-β1 subunit. This allows sGC-β1 to associate with a partner sGC-α1 subunit and mature into an NO-responsive active form.
CRITICAL ISSUES
In this article, we review evidence to date regarding the mechanisms that modulate sGC activity by a pathway where binding of hsp90 or sGC agonist to heme-free sGC dictates the assembly and fate of an active sGC heterodimer, both by NO and heme-dependent or heme-independent pathways.
FUTURE DIRECTIONS
We discuss some therapeutic implications of the NO-sGC-hsp90 nexus and its potential as a marker of inflammatory disease. Antioxid. Redox Signal. 26, 182-190.
摘要
意义
可溶性鸟苷酸环化酶（sGC）是一种细胞内酶，在哺乳动物中感知一氧化氮（NO）并传导其多种信号效应方面发挥主要作用。
最新进展
伴侣热休克蛋白90（hsp90）与细胞中的信号蛋白相关联，包括sGC，它在其中帮助将血红素插入sGC-β1亚基。这使得sGC-β1能够与伴侣sGC-α1亚基结合并成熟为对NO有反应的活性形式。
关键问题
在本文中，我们综述了迄今为止关于通过hsp90或sGC激动剂与无血红素sGC结合决定活性sGC异二聚体的组装和命运的途径来调节sGC活性的机制的证据，该途径通过NO和血红素依赖性或血红素非依赖性途径。
未来方向
我们讨论了NO-sGC-hsp90关系的一些治疗意义及其作为炎症性疾病标志物的潜力。《抗氧化剂与氧化还原信号》26，182 - 190。
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