title: Serum thioredoxin reductase levels increase in response to chemically induced acute liver injury.
abstract: 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.
  
  
  CONCLUSIONS
  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.
authors.affiliation: School of Tea and Food Science, Anhui Agricultural University, Hefei 230036, Anhui, PR China.
authors.forename: Kang
authors.initials: K
authors.lastname: Sun
authors.affiliation: Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 77 Stockholm, Sweden.
authors.forename: Sofi E
authors.initials: SE
authors.lastname: Eriksson
authors.affiliation: School of Tea and Food Science, Anhui Agricultural University, Hefei 230036, Anhui, PR China.
authors.forename: Yanping
authors.initials: Y
authors.lastname: Tan
authors.affiliation: School of Tea and Food Science, Anhui Agricultural University, Hefei 230036, Anhui, PR China.
authors.forename: Le
authors.initials: L
authors.lastname: Zhang
authors.affiliation: Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 77 Stockholm, Sweden.
authors.forename: Elias S J
authors.initials: ES
authors.lastname: Arnér
authors.affiliation: School of Tea and Food Science, Anhui Agricultural University, Hefei 230036, Anhui, PR China. Electronic address: zjs@ahau.edu.cn.
authors.forename: Jinsong
authors.initials: J
authors.lastname: Zhang
mesh_terms: D000818:Animals; D000975:Antioxidants / Q000378:metabolism*; D056486:Chemical and Drug Induced Liver Injury / Q000097:blood*; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D051379:Mice; D013853:Thioacetamide / Q000633:toxicity; D054481:Thioredoxin Reductase 1 / Q000097:blood*; D013879:Thioredoxins / Q000378:metabolism*
chemical_list: D000975:Antioxidants; D013853:Thioacetamide; D013879:Thioredoxins; D054481:Thioredoxin Reductase 1; C516125:Txnrd1 protein, mouse
keywords: Alanine aminotransferase; Hepatotoxicity; Serum; Thioredoxin reductase