Interacting with thioredoxin-1-disease or no disease?
Summary of "Interacting with thioredoxin-1-disease or no disease?"
Abstract Significance: Many cardiovascular disorders are accompanied by a deregulated cellular redox balance resulting in elevated levels of intracellular reactive oxygen species (ROS). One major antioxidative cellular molecule is thioredoxin-1 (Trx-1). Its indispensability is demonstrated by the embryonic lethality of Trx-1 deficient mice. Trx-1 is ubiquitously expressed in cells and has numerous, diverse functions. It not only reduces oxidized proteins or, together with peroxiredoxins, detoxifies H(2)O(2), but also binds to several proteins and thereby regulates their functions. The interaction partners of Trx-1 differ depending on its localization in the cytosol or in the nucleus. Recent Advances/Critical Issues: Over the past decade it has become clear that Trx-1 is not only critical for tumor functions, which has resulted in therapeutic approaches targeting this protein, but also essential for proper functions of the vasculature and the heart. Changes in post-translational modifications of Trx-1 or in its interactions with other proteins can lead to a switch from a physiologic state of cells and organs to diverse pathologies. This review provides insights into the role of Trx-1 in different physiological situations and cardiac hypertrophy, ischemia reperfusion injury, heart failure, atherosclerosis, and diabetes mellitus type 2, underscoring the central role of Trx-1 in cardiovascular health and disease. Future Directions: Thus, the manipulation of Trx-1 activity in the heart and/or vasculature, for example, by small molecules, seems to be a promising therapeutic option in cardiovascular diseases, as general anti-oxidant treatments would not take into account interactions of Trx-1 with other proteins and also eliminate vital ROS. Antioxid. Redox Signal. 18, 1053-1062.
1 Molecular Cell and Aging Research, IUF-Leibniz Research Institute for Environmental Medicine, University of Duesseldorf gGmbH , Duesseldorf, Germany .
This article was published in the following journal.
Name: Antioxidants & redox signaling
- PubMed Source: http://www.ncbi.nlm.nih.gov/pubmed/22867430
- DOI: http://dx.doi.org/10.1089/ars.2012.4822
Medical and Biotech [MESH] Definitions
A thioredoxin subtype that is ubiquitously found in the plant kingdom. It reduces a variety of seed storage proteins and may play a role in the germination process of seeds.
A FLAVOPROTEIN enzyme that catalyzes the oxidation of THIOREDOXINS to thioredoxin disulfide in the presence of NADP+. It was formerly listed as EC 188.8.131.52
Thioredoxin Reductase 1
A subtype of thioredoxin reductase found primarily in the CYTOSOL.
Thioredoxin Reductase 2
A subtype of thioredoxin reductase found primarily in MITOCHONDRIA.
Animate or inanimate sources which normally harbor disease-causing organisms and thus serve as potential sources of disease outbreaks. Reservoirs are distinguished from vectors (DISEASE VECTORS) and carriers, which are agents of disease transmission rather than continuing sources of potential disease outbreaks.
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