title: Redox imbalance in peripheral blood of type 1 myotonic dystrophy patients.
abstract: OBJECTIVE
  The aim of our study was to determine if redox imbalance caused by the activities of antioxidant enzymes existed in erythrocytes of type 1 myotonic dystrophy (DM1) patients.
  
  
  METHODS
  The activities of erythrocyte superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase were measured in 30 DM1 patients and 15 healthy controls (HCs). The obtained values were correlated with the Muscular Impairment Rating Scale (MIRS) score and creatine kinase (CK).
  
  
  RESULTS
  Superoxide dismutase and catalase activities were lower in DM1 patients compared to HCs. A positive correlation was found between disease duration and MIRS score as well as with glutathione reductase activity. In DM1 patients, there were positive correlations between catalase, glutathione peroxidase, and glutathione reductase activities. After sub-dividing DM1 patients according to CK levels, superoxide dismutase activity was still statistically different from HCs. However, catalase activity was significantly lower only in DM1 patients with increased CK.
  
  
  CONCLUSIONS
  Undesirable alterations in antioxidant enzyme activities during DM1 disease progression may result in conditions favoring oxidative stress and changes in metabolism which together could contribute to muscle wasting.
authors.affiliation: a Department of Physiology, Institute for Biological Research Siniša Stanković , University of Belgrade , Serbia.
authors.forename: Aleksandra
authors.initials: A
authors.lastname: Nikolić-Kokić
authors.affiliation: b Faculty for Special Education and Rehabilitation , University of Belgrade , Serbia.
authors.forename: Dragan
authors.initials: D
authors.lastname: Marinković
authors.affiliation: c Neurology Clinic, Clinical Centre of Serbia, School of Medicine , University of Belgrade , Serbia.
authors.forename: Stojan
authors.initials: S
authors.lastname: Perić
authors.affiliation: c Neurology Clinic, Clinical Centre of Serbia, School of Medicine , University of Belgrade , Serbia.
authors.forename: Zorica
authors.initials: Z
authors.lastname: Stević
authors.affiliation: a Department of Physiology, Institute for Biological Research Siniša Stanković , University of Belgrade , Serbia.
authors.forename: Mihajlo B
authors.initials: MB
authors.lastname: Spasić
authors.affiliation: a Department of Physiology, Institute for Biological Research Siniša Stanković , University of Belgrade , Serbia.
authors.forename: Duško
authors.initials: D
authors.lastname: Blagojević
authors.affiliation: c Neurology Clinic, Clinical Centre of Serbia, School of Medicine , University of Belgrade , Serbia.
authors.forename: Vidosava
authors.initials: V
authors.lastname: Rakocˇević-Stojanović
mesh_terms: D000328:Adult; D002374:Catalase / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism; D005260:Female; D005979:Glutathione Peroxidase / Q000378:metabolism; D005980:Glutathione Reductase / Q000378:metabolism; D006801:Humans; D008297:Male; D009223:Myotonic Dystrophy / Q000378:metabolism* / Q000473:pathology; D010084:Oxidation-Reduction; D018384:Oxidative Stress / Q000502:physiology; D013482:Superoxide Dismutase / Q000378:metabolism
chemical_list: D002374:Catalase; D005979:Glutathione Peroxidase; D013482:Superoxide Dismutase; D005980:Glutathione Reductase
keywords: Catalase; Erythrocytes; Glutathione reductase; Glutatione peroxidase; Superoxide dismutase; Type 1 myotonic dystrophy
references.citation: Anal Biochem. 1971 Nov;44(1):276-87
references.pmid: 4943714
references.citation: Biochem J. 1974 Apr;139(1):43-8
references.pmid: 4377099
references.citation: J Physiol. 2004 Nov 15;561(Pt 1):233-44
references.pmid: 15331678
references.citation: Neuromuscul Disord. 1991;1(1):19-29
references.pmid: 1822774
references.citation: Mech Ageing Dev. 2006 Nov;127(11):830-9
references.pmid: 16996110
references.citation: Antioxid Redox Signal. 2011 Nov 1;15(9):2477-86
references.pmid: 21699411
references.citation: Biochem Biophys Res Commun. 2000 Jan 27;267(3):739-43
references.pmid: 10673361
references.citation: J Appl Physiol (1985). 1993 Sep;75(3):1081-7
references.pmid: 8226515
references.citation: J Neurol. 1995 Feb;242(3):119-22
references.pmid: 7751852
references.citation: J Aging Res. 2012;2012:194821
references.pmid: 22888430
references.citation: Biochem Soc Trans. 2009 Dec;37(Pt 6):1281-6
references.pmid: 19909263
references.citation: Nature. 1970 Aug 15;227(5259):680-5
references.pmid: 5432063
references.citation: Free Radic Biol Med. 2003 May 1;34(9):1217-20
references.pmid: 12706502
references.citation: An Acad Bras Cienc. 2015 Sep;87(3):1809-18
references.pmid: 25910175
references.citation: Cardiovasc Res. 2006 Jul 15;71(2):310-21
references.pmid: 16581043
references.citation: J Appl Physiol (1985). 2007 Apr;102(4):1677-86
references.pmid: 17095633
references.citation: Free Radic Res. 2005 Jul;39(7):771-6
references.pmid: 16036357
references.citation: J Environ Pathol Toxicol Oncol. 1998;17(3-4):241-50
references.pmid: 9726797
references.citation: Neurology. 2001 Feb 13;56(3):336-40
references.pmid: 11171898
references.citation: Hum Mol Genet. 2005 Aug 1;14(15):2189-200
references.pmid: 15972723
references.citation: Free Radic Res. 2014 Apr;48(4):503-10
references.pmid: 24472045
references.citation: Pract Neurol. 2015 Apr;15(2):121
references.pmid: 25573341
references.citation: Free Radic Biol Med. 2006 Jun 1;40(11):1993-2004
references.pmid: 16716900
references.citation: Free Radic Biol Med. 2008 Jan 15;44(2):132-41
references.pmid: 18191749
references.citation: Clin Chem Lab Med. 2005;43(7):745-7
references.pmid: 16207136
references.citation: Psychiatry Res. 2010 Jun 30;178(1):68-72
references.pmid: 20452039
references.citation: J Neurosci Res. 2011 Mar;89(3):275-85
references.pmid: 21259315
references.citation: Clin Chem Lab Med. 2006;44(5):589-93
references.pmid: 16681429
references.citation: Biochimie. 2011 Nov;93(11):2006-12
references.pmid: 21763392
references.citation: Methods Enzymol. 1981;76:707-15
references.pmid: 7329285