Description
Title: S-Denitrosylation: A Glutathione and Redoxin Systems Crosstalk
Abstract: Proteins become S-nitrosylated as a result of derivatizing cysteine thiols with nitric oxide (NO), and this process is frequently linked to disease and protein dysfunction. Along with other genetic and epigenetic factors, aberrant S-nitrosylation has quickly emerged as a major contributor to a variety of metabolic, respiratory, and cardiac disorders, with a focus on cancer and neurodegeneration. In comparison to other covalently modified versions of the same set of proteins, the S-nitrosoproteome—a term used to refer to the diverse and dynamic repertoire of S-nitrosylated proteins—is relatively understudied in the field of redox biochemistry. The enormous clinical significance of S-nitrosylation in the etiology of diseases is gradually coming to light as a result of advanced research, which is also creating new opportunities for early diagnosis that take advantage of this phenomenon. Years of rife speculation have focused on the identification of particular substrates and other candidate denitrosylases, subcellular localization of both substrates and denitrosylases, the location of susceptible thiols, mechanisms of S-denitrosylation under basal and stimulus-dependent conditions, impact on protein conformation, and many other topics since the discovery of the two robust and highly conserved S-nitrosoglutathione reductase and thioredoxin systems However, more recent discoveries in the rapidly developing field of redox biology point to clear research gaps in understanding the critical interaction between the major denitrosylase/redoxin systems. To develop a theory that could help predict the degree of cell survival under high oxidative/nitrosative stress while taking into account the existence of alternative and compensatory regulatory mechanisms, it is crucial to first understand the significance of the functional overlap of the glutaredoxin, glutathione, and thioredoxin systems and to look at their complementary roles as denitrosylases and antioxidant enzymatic defense systems. With the help of numerous denitrosylases and antioxidants working together, the robust cellular redox regulation system is maintained. This review aims to identify significant knowledge gaps in this system.
Keywords: antioxidant systems; glutaredoxin; glutathione; glutathione peroxidase; glutathione reductase; glutathione transferase; glutathionylation; nitric oxide; nitric oxide synthases; nitro-oxidative stress; oxidoreductases; peroxiredoxin; thioredoxin; thioredoxin reductase; thioredoxin interacting protein; thioredoxin-related protein 14; reactive oxygen species; reactive nitrogen species; redox homeostasis; redundancy; S-(de)nitrosylation; S-nitrosoglutathione; S-nitrosoproteins; thiol disulfides
Paper Quality: SCOPUS / Web of Science Level Research Paper
Subject: Biology
Writer Experience: 20+ Years
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