Journal
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume 1840, Issue 7, Pages 2105-2111Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbagen.2014.02.028
Keywords
Thioredoxin reductase; Alanine aminotransferase; Hepatotoxicity; Serum
Categories
Funding
- National Natural Science Foundation of China [31170648]
- Performance Appraisal Fund of the Anhui Provincial Science and Technology Department [1306c083018]
- Foundation of AHAU Subject Construction
- Karolinska Institutet
- Swedish Cancer Society
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Background: Mammalian thioredoxin reductases (TrxR) are selenoproteins with important roles in antioxidant defense and redox regulation, principally linked to functions of their main substrates thioredoxins (Trx). All major forms of TrxR are intracellular while levels in serum are typically very low. Methods: Serum TrxR levels were determined with immunoblotting using antibodies against mouse TrxR1 and total enzyme activity measurements were performed, with serum and tissue samples from mouse models of liver injury, as triggered by either thioacetamide (TAA) or carbon tetrachloride (CCl4). Results: TrxR levels in serum increased upon treatment and correlated closely with those of alanine aminotransferase (ALT), an often used serum biomarker for liver damage. In contrast, Trx1, glutathione reductase, superoxide dismutase or selenium-containing glutathione peroxidase levels in serum displayed much lower increases than TrxR or ALT. Conclusions: Serum TrxR levels are robustly elevated in mouse models of chemically induced liver injury. General significance: The exaggerated TrxR release to serum upon liver injury may reflect more complex events than a mere passive release of hepatic enzymes to the extracellular milieu. It can also not be disregarded that enzymatically active TrxR in serum could have yet unidentified physiological functions. (C) 2014 Elsevier B.V. All rights reserved.
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