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Role of Glutaredoxin-1 and Glutathionylation in Cardiovascular Diseases.
- Source :
-
International journal of molecular sciences [Int J Mol Sci] 2020 Sep 16; Vol. 21 (18). Date of Electronic Publication: 2020 Sep 16. - Publication Year :
- 2020
-
Abstract
- Cardiovascular diseases are the leading cause of death worldwide, and as rates continue to increase, discovering mechanisms and therapeutic targets become increasingly important. An underlying cause of most cardiovascular diseases is believed to be excess reactive oxygen or nitrogen species. Glutathione, the most abundant cellular antioxidant, plays an important role in the body's reaction to oxidative stress by forming reversible disulfide bridges with a variety of proteins, termed glutathionylation (GSylation). GSylation can alter the activity, function, and structure of proteins, making it a major regulator of cellular processes. Glutathione-protein mixed disulfide bonds are regulated by glutaredoxins (Glrxs), thioltransferase members of the thioredoxin family. Glrxs reduce GSylated proteins and make them available for another redox signaling cycle. Glrxs and GSylation play an important role in cardiovascular diseases, such as myocardial ischemia and reperfusion, cardiac hypertrophy, peripheral arterial disease, and atherosclerosis. This review primarily concerns the role of GSylation and Glrxs, particularly glutaredoxin-1 (Glrx), in cardiovascular diseases and the potential of Glrx as therapeutic agents.
- Subjects :
- Animals
Antioxidants metabolism
Cardiovascular Diseases drug therapy
Cysteine analogs & derivatives
Cysteine chemistry
Cysteine metabolism
Disulfides metabolism
Endothelial Cells metabolism
Glucose metabolism
Glutaredoxins deficiency
Glutaredoxins therapeutic use
Homeostasis
Humans
Lipid Metabolism physiology
Mice
Mice, Knockout
Myocytes, Cardiac metabolism
Oxidation-Reduction
Oxidative Stress
Reactive Nitrogen Species metabolism
Reactive Oxygen Species metabolism
Cardiovascular Diseases metabolism
Glutaredoxins physiology
Glutathione metabolism
Protein Processing, Post-Translational
Subjects
Details
- Language :
- English
- ISSN :
- 1422-0067
- Volume :
- 21
- Issue :
- 18
- Database :
- MEDLINE
- Journal :
- International journal of molecular sciences
- Publication Type :
- Academic Journal
- Accession number :
- 32948023
- Full Text :
- https://doi.org/10.3390/ijms21186803