S-glutathionylation, friend or foe in cardiovascular health and disease

Rashdan, Nabil A.; Shrestha, Bandana; Pattillo, Christopher B.

doi:10.1016/j.redox.2020.101693

Cited by 30 publications

(19 citation statements)

References 212 publications

(148 reference statements)

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“…These extreme conditions are rare in vivo. Therefore, for most proteins, the spontaneous formation of Pr-SSG—as a result of the exchange of Pr-SH and GSSG—is not common and, as a rule, takes place under pathological conditions [ 30 ]. In addition, a variant of thiol-disulfide exchange between Pr-SH and a protein which is already S-glutathionylated (Pr′-SSG) is possible:

…”

Section: Glutathione and Protein S-glutathionylationmentioning

confidence: 99%

Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation

Калинина

Novichkova

2021

Molecules

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S-glutathionylation and S-nitrosylation are reversible post-translational modifications on the cysteine thiol groups of proteins, which occur in cells under physiological conditions and oxidative/nitrosative stress both spontaneously and enzymatically. They are important for the regulation of the functional activity of proteins and intracellular processes. Connecting link and “switch” functions between S-glutathionylation and S-nitrosylation may be performed by GSNO, the generation of which depends on the GSH content, the GSH/GSSG ratio, and the cellular redox state. An important role in the regulation of these processes is played by Trx family enzymes (Trx, Grx, PDI), the activity of which is determined by the cellular redox status and depends on the GSH/GSSG ratio. In this review, we analyze data concerning the role of GSH/GSSG in the modulation of S-glutathionylation and S-nitrosylation and their relationship for the maintenance of cell viability.

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…”

Section: Glutathione and Protein S-glutathionylationmentioning

confidence: 99%

Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation

Калинина

Novichkova

2021

Molecules

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“…The metabolic cofactor glutathione (GSH) is considered the most abundant endogenous antioxidant (discovered more than 10 decades ago) that plays an important role in detoxification of reactions in CCs [ 72 ]. This is a tripeptide that is biosynthesized in two key steps.…”

Section: Antioxidants (Aos)mentioning

confidence: 99%

Comprehensive Review of Methodology to Detect Reactive Oxygen Species (ROS) in Mammalian Species and Establish Its Relationship with Antioxidants and Cancer

et al. 2021

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Evidence suggests that reactive oxygen species (ROS) mediate tissue homeostasis, cellular signaling, differentiation, and survival. ROS and antioxidants exert both beneficial and harmful effects on cancer. ROS at different concentrations exhibit different functions. This creates necessity to understand the relation between ROS, antioxidants, and cancer, and methods for detection of ROS. This review highlights various sources and types of ROS, their tumorigenic and tumor prevention effects; types of antioxidants, their tumorigenic and tumor prevention effects; and abnormal ROS detoxification in cancer; and methods to measure ROS. We conclude that improving genetic screening methods and bringing higher clarity in determination of enzymatic pathways and scale-up in cancer models profiling, using omics technology, would support in-depth understanding of antioxidant pathways and ROS complexities. Although numerous methods for ROS detection are developing very rapidly, yet further modifications are required to minimize the limitations associated with currently available methods.

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“…Glrx reverses S-glutathionylation of GAPDH and plays a role in the key step of apoptosis signal transduction, thus participating in regulating apoptosis [ 40 ]. Moreover, eNOS is regulated by direct S-glutathionylation in the endothelial cells [ 41 ]. NO reacts with superoxide to form peroxynitrite, which activates S-glutathionylation in Cys674 to regulate SERCA2 activity and vascular smooth muscle function [ 42 ].…”

Section: Ptms In Heart Developmentmentioning

confidence: 99%

Role of Posttranslational Modifications of Proteins in Cardiovascular Disease

Liu

Zhang

Wen

et al. 2022

Oxidative Medicine and Cellular Longevity

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Cardiovascular disease (CVD) has become a leading cause of mortality and morbidity globally, making it an urgent concern. Although some studies have been performed on CVD, its molecular mechanism remains largely unknown for all types of CVD. However, recent in vivo and in vitro studies have successfully identified the important roles of posttranslational modifications (PTMs) in various diseases, including CVD. Protein modification, also known as PTMs, refers to the chemical modification of specific amino acid residues after protein biosynthesis, which is a key process that can influence the activity or expression level of proteins. Studies on PTMs have contributed directly to improving the therapeutic strategies for CVD. In this review, we examined recent progress on PTMs and highlighted their importance in both physiological and pathological conditions of the cardiovascular system. Overall, the findings of this review contribute to the understanding of PTMs and their potential roles in the treatment of CVD.

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S-glutathionylation, friend or foe in cardiovascular health and disease

Cited by 30 publications

References 212 publications

Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation

Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation

Comprehensive Review of Methodology to Detect Reactive Oxygen Species (ROS) in Mammalian Species and Establish Its Relationship with Antioxidants and Cancer

Role of Posttranslational Modifications of Proteins in Cardiovascular Disease

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