AI Article Synopsis

  • * Glutathionylation helps protect proteins from permanent damage caused by oxidation, and several enzymes, like glutathione transferases, are involved in this process.
  • * The paper explores the regulation of glutathione levels, identifies glutathionylated proteins, and reviews recent findings on the role of glutathionylation in lung diseases such as idiopathic pulmonary fibrosis, asthma, and chronic obstructive pulmonary disease.

Article Abstract

Glutathione is a major redox buffer, reaching millimolar concentrations within cells and high micromolar concentrations in airways. While glutathione has been traditionally known as an antioxidant defense mechanism that protects the lung tissue from oxidative stress, glutathione more recently has become recognized for its ability to become covalently conjugated to reactive cysteines within proteins, a modification known as glutathionylation (or glutathiolation or protein mixed disulfide). glutathionylation has the potential to change the structure and function of the target protein, owing to its size (the addition of three amino acids) and charge (glutamic acid). glutathionylation also protects proteins from irreversible oxidation, allowing them to be enzymatically regenerated. Numerous enzymes have been identified to catalyze the glutathionylation/deglutathionylation reactions, including glutathione transferases and glutaredoxins. Although protein glutathionylation has been implicated in numerous biological processes, glutathionylated proteomes have largely remained unknown. In this paper, we focus on the pathways that regulate GSH homeostasis, glutathionylated proteins, and glutaredoxins, and we review methods required toward identification of glutathionylated proteomes. Finally, we present the latest findings on the role of glutathionylation/glutaredoxins in various lung diseases: idiopathic pulmonary fibrosis, asthma, and chronic obstructive pulmonary disease.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7052607PMC
http://dx.doi.org/10.1152/ajpcell.00410.2019DOI Listing

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