Dysregulation of the glutaredoxin/S-glutathionylation redox axis in lung diseases.

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 S-glutathionylation (or S-glutathiolation or protein mixed disulfide). S-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). S-glutathionylation also protects proteins from irreversible oxidation, allowing them to be en

SUBMITTER: Chia SB 

PROVIDER: S-EPMC7052607 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature