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Protein S- Glutathionylation Translates a Regulatory Switch for Health and Disease

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Glutathionylation is a process where cysteine residues in proteins form disulfide bonds due to various cellular conditions. Oxidative or nitrosative stress induce post-translational modifications and may alter protein functions from maintaining the 3D structure of proteins, protecting further oxidation of ...

Glutathionylation is a process where cysteine residues in proteins form disulfide bonds due to various cellular conditions. Oxidative or nitrosative stress induce post-translational modifications and may alter protein functions from maintaining the 3D structure of proteins, protecting further oxidation of thiols to a level of biomarker in a disease state, drug therapeutic advancements and beyond. Several studies reported that progression in the glutathionylation process of specific proteins in disease conditions such as diabetes, cardiovascular, lung and neurodegenerative disease might be the cause for the disease severity. In vascular diseases, including hypertension (HTN) and atherosclerosis, endothelial dysfunction occurs secondary to altered function of endothelial NO synthase (eNOS).

However, questions remain regarding the mechanism by which this occurs and how it can be reversed. A novel redox-regulated pathway was recently identified through which eNOS is uncoupled due to S-glutathionylation; however, its role in human vascular disease remains unknown. On one hand, quantification of S-glutathionylation of target proteins with important functional consequences is a promising biomarker for vascular disease progression. On the other hand, there are methodology challenges in the quantitation of a specific protein glutathionylation due to method limitations and the availability of specific antibodies for detecting glutathionylated proteins.

The key to identify the glutathionylated proteins in the preclinical and clinical setting is an improved understanding of the mechanism involved and development of effective biomarkers and therapeutic targets. We invite investigators to contribute research articles, as well as review articles that will stimulate the continuing efforts to understand the molecular physiology and pathology underlying the glutathionylation process, and the development of strategies to treat these conditions. We are particularly interested in articles describing the mechanistic role for protein glutathionylation characterization, quantitation and new insights into the physiology and pathophysiology outcomes using animal & human models; current concepts in nutrition and drug therapy strategies.
Potential Research Topics include:
• S-glutathionylation as a biomarker of oxidative stress
• Molecular mechanisms and clinical significance of protein S-glutathionylation
• S-glutathionylation of eNOS: a major cause for reduced nitric oxide availability in vascular diseases
• Generation of vasodilator molecule through protein S- glutathionylation
• S-glutathionylation and failing heart: Redox regulation perspective
• Redox regulation in cardiac physiology and pathophysiology
• Physiology and Pathophysiology of Glutathionylation Process
• Glutathionylation of proteins in cellular physiology and pathophysiology
• Challenges in the detection of protein glutathionylation, and its importance as a diagnostic tool; and multiple functions of protein glutathionylation
• Protein sensitivity to glutathionylation process and disease progression
• The role of S-glutathionylation of proteins in cardiovascular diseases
• Elucidating the mechanisms of S-glutathionylation of elastin proteins and its effects on protein elasticity
• Glutathionylation of proteins and signaling mechanisms as molecular chaperones and signal regulators
• Novel regulators of S-glutathionylation of proteins during oxidative stress


Keywords: Vasculature, Protein S-Glutathionylation, Health & Disease, Nitric oxide, tetrahydrobiopterin


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