Melatonin treatment counteracts the hyperoxidative status in erythrocytes of patients suffering from Duchenne muscular dystrophy.

Clin Biochem

Instituto de Biotecnología, Centro de Investigación Biomédica, Parque Tecnológico de Ciencias de la Salud, Universidad de Granada, Granada, Spain.

Published: July 2011

Objectives: To analyze whether the antioxidant melatonin could reduce the hyperoxidative status in the blood of patients with Duchenne's muscular dystrophy.

Design And Methods: Ten patients aged 12.8±0.9 years were treated with melatonin (60mg at 21:00h plus 10mg at 09:00h) for 9 months, and erythrocyte markers of oxidative stress were determined at 3, 6, and 9 months of treatment. Healthy age- and sex-matched subjects served as controls.

Results: Prior to treatment, the patients had higher glutathione disulfide/glutathione ratio and higher glutathione transferase and superoxide dismutase activities, and lower glutathione reductase activity than controls. After 3 months of melatonin treatment, the hyperoxidative status of these patients was counteracted, being reduced to the normal redox state between 3 and 9 months.

Conclusion: These results, together with the reduction in the inflammatory process and in muscle injury recently reported in the same patients, support the efficacy of melatonin therapy in DMD patients.

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.clinbiochem.2011.04.001DOI Listing

Publication Analysis

Top Keywords

hyperoxidative status
12
melatonin treatment
8
higher glutathione
8
patients
7
melatonin
5
treatment counteracts
4
counteracts hyperoxidative
4
status erythrocytes
4
erythrocytes patients
4
patients suffering
4

Similar Publications

Aim: Duchenne muscular dystrophy is a progressive muscle-wasting disease caused by mutations in the dystrophin gene. Despite progress in dystrophin-targeted gene therapies, it is still a fatal disease requiring novel therapeutics that can be used synergistically or alternatively to emerging gene therapy. Defective autophagy and disorganized microtubule networks contribute to dystrophic pathogenesis, yet the mechanisms by which microtubule alterations regulate autophagy remain elusive.

View Article and Find Full Text PDF

Hyperoxidized Species of Heme Have a Potent Capacity to Induce Autoreactivity of Human IgG Antibodies.

Int J Mol Sci

February 2023

Centre de Recherche des Cordeliers, INSERM, CNRS, Sorbonne Université, Université Paris Cité, 75006 Paris, France.

The interaction of some human antibodies with heme results in posttranslational acquisition of binding to various self- and pathogen-derived antigens. The previous studies on this phenomenon were performed with oxidized heme (Fe). In the present study, we elucidated the effect of other pathologically relevant species of heme, i.

View Article and Find Full Text PDF

Differential oxidation processes of peroxiredoxin 2 dependent on the reaction with several peroxides in human red blood cells.

Biochem Biophys Res Commun

October 2019

Departments of Analytical Biochemistry, Meiji Pharmaceutical University, 2-522-1 Noshio, Kiyose, Tokyo, 204-8588, Japan. Electronic address:

Peroxiredoxins (Prxs) detoxify hydrogen peroxide (HO), peroxynitrite, and various organic hydroperoxides. However, the differential oxidative status of Prxs reacted with each peroxide remains unclear. In the present study, we focused on the oxidative alteration of Prxs and demonstrated that, in human red blood cells (RBCs), peroxiredoxin 2 (Prx2) is readily reactive with HO, forming disulfide dimers, but was not easily hyperoxidized.

View Article and Find Full Text PDF

Role of Cytosolic 2-Cys Prx1 and Prx2 in Redox Signaling.

Antioxidants (Basel)

June 2019

Department of Health Sciences and Technology, Graduate School of Medicine, Gachon University, Incheon 21999, Korea.

Peroxiredoxins (Prxs), a family of peroxidases, are reactive oxygen species scavengers that hydrolyze HO through catalytic cysteine. Mammalian Prxs comprise six isoforms (typical 2-Cys Prxs; Prx1-4, atypical 2-Cys Prx; Prx5, and 1-Cys Prx; Prx6) that are distributed over various cellular compartments as they are classified according to the position and number of conserved cysteine. 2-Cys Prx1 and Prx2 are abundant proteins that are ubiquitously expressed mainly in the cytosol, and over 90% of their amino acid sequences are homologous.

View Article and Find Full Text PDF

Variability in the redox status of plant 2-Cys peroxiredoxins in relation to species and light cycle.

J Exp Bot

September 2019

Aix Marseille Univ, CEA, CNRS, BIAM, Plant Protective Proteins Team, Saint Paul-Lez-Durance, France.

Plant 2-Cys peroxiredoxins (2-CysPRXs) are abundant plastidial thiol-peroxidases involved in key signaling processes such as photosynthesis deactivation at night. Their functions rely on the redox status of their two cysteines and on the enzyme quaternary structure, knowledge of which remains poor in plant cells. Using ex vivo and biochemical approaches, we thoroughly characterized the 2-CysPRX dimer/monomer distribution, hyperoxidation level, and thiol content in Arabidopsis, barley, and potato in relation to the light cycle.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!