North Shore Heart Research Group, Kolling Institute, University of Sydney, NSW 2006, Australia.
Trends Cardiovasc Med. 2010 Apr;20(3):85-90. doi: 10.1016/j.tcm.2010.06.002.
Reminiscent of phosphorylation, cellular signaling can induce reversible forms of oxidative modification of proteins with an impact on their function. Redox signaling can be coupled to cell membrane receptors for hormones and be a physiologic means of regulating protein function, whereas pathologic increases in oxidative stress may induce disease processes. Here we review the role of reversible oxidative modification of proteins in the regulation of their function with particular emphasis on the cardiac Na(+)-K(+) pump. We describe how protein-kinase-dependent activation of redox signaling, mediated by angiotensin receptors and β adrenergic receptors, induces glutathionylation of an identified cysteine residue in the β(1) subunit of the α/β pump heterodimer; and we discuss how this may link neurohormonal abnormalities, increased oxidative stress, and cardiac myocyte Na(+) dysregulation and heart failure with important implications for treatment.
类似于磷酸化作用，细胞信号转导可以诱导蛋白质发生氧化修饰的可逆形式，从而影响其功能。氧化还原信号可以与激素的细胞膜受体偶联，并成为调节蛋白质功能的生理手段，而病理性氧化应激的增加可能会诱导疾病过程。在这里，我们回顾了蛋白质的可逆氧化修饰在调节其功能中的作用，特别强调了心脏 Na(+)-K(+)泵。我们描述了蛋白激酶依赖性的氧化还原信号转导的激活，这种激活由血管紧张素受体和β肾上腺素能受体介导，可诱导α/β泵异二聚体β(1)亚基中一个特定半胱氨酸残基的谷胱甘肽化；我们还讨论了这如何将神经激素异常、氧化应激增加和心肌细胞 Na(+)失调与心力衰竭联系起来，这对治疗具有重要意义。
