Malondialdehyde and carbonyl levels in skeletal muscle tissues after intermittent hypobaric hypoxia exposures
Abstract
Background: Hypobaric hypoxia is a state of decreased oxygen pressure at high altitudes that can lead to hypoxia and oxidative stress as a result. Skeletal muscle is one of the important organs that can be affected by oxidative stress and cause contractile dysfunction.
Objective: This study aimed to evaluate the impact of intermittent hypobaric hypoxia on oxidative stress markers in rat skeletal muscle, by measuring malondialdehyde (MDA) and carbonyl levels.
Methods: Twenty-five Wistar rats were allocated into five groups, including one control group and four hypoxic groups (I-IV). The hypoxic groups were exposed to an altitude of 25,000 feet for 5 minutes using hypobaric chamber in once (I), twice (II), three (III), and four (IV) times, with a 7-day interval period between exposures. The control group remained in normobaric conditions throughout the study. MDA levels were measured by thiobarbituric acid (TBA) test, while carbonyl levels were measured using 2,4-dinitrophenylhydrazine (DNPH) reagent.
Results: The MDA level was significantly increased in group I compared to the control group (p=0.008). There were decreasing MDA levels in groups II, III, and IV compared to group I. The carbonyl level was significantly higher in group I than the control group (p=0.000), with an even higher level observed in group II. Although the carbonyl levels tended to decrease in groups III and IV, they still remained higher than those of the control group.
Conclusion: Exposure to hypobaric hypoxia leads to an increase in MDA and carbonyl levels in the skeletal muscles, indicating an elevation of oxidative stress levels. However, the subsequent intermittent hypobaric hypoxia exposure resulted in a reduction in these levels, implying that skeletal muscles may adapt to hypoxic conditions.
References
Tu M-Y, Chiang K-T, Cheng C-C, Li F-L, Wen Y-H, Lin S-H, et al. Comparison of hypobaric hypoxia symptoms between a recalled exposure and a current exposure. PLoS One. 2020;15: e0239194. https://doi.org/10.1371/journal.pone.0239194
Grocott M, Montgomery H, Vercueil A. High-altitude physiology and pathophysiology: Implications and relevance for intensive care medicine. Critical Care. 2007. https://doi.org/10.1186/cc5142
Peacock A. ABC of oxygen. Oxygen at high altitude. Br Med J. 1998;317: 1063-1066. https://doi.org/10.1136/bmj.317.7165.1063
Solaini G, Baracca A, Lenaz G, Sgarbi G. Hypoxia and mitochondrial oxidative metabolism. Biochim Biophys Acta - Bioenerg. 2010;1797: 1171-1177. https://doi.org/10.1016/j.bbabio.2010.02.011
Fuhrmann DC, Brüne B. Mitochondrial composition and function under the control of hypoxia. Redox Biol. 2017;12: 208-215. https://doi.org/10.1016/j.redox.2017.02.012
Gaweł S, Wardas M, Niedworok E, Wardas P. [Malondialdehyde (MDA) as a lipid peroxidation marker]. Wiad Lek. 2004;57: 453-455.
Suzuki YJ, Carini M, Butterfield DA. Protein carbonylation. Antioxidants & redox signaling. 2010. pp. 323-325. https://doi.org/10.1089/ars.2009.2887
Pamplona R. Membrane phospholipids, lipoxidative damage and molecular integrity: A causal role in aging and longevity. Biochimica et Biophysica Acta - Bioenergetics. 2008. https://doi.org/10.1016/j.bbabio.2008.07.003
Janero DR. Malondialdehyde and thiobarbituric acid-reactivity as diagnostic indices of lipid peroxidation and peroxidative tissue injury. Free Radical Biology and Medicine. 1990. https://doi.org/10.1016/0891-5849(90)90131-2
Dalle-Donne I, Rossi R, Giustarini D, Milzani A, Colombo R. Protein carbonyl groups as biomarkers of oxidative stress. Clinica Chimica Acta. 2003. https://doi.org/10.1016/S0009-8981(03)00003-2
Levine RL, Williams JA, Stadtman EP, Shacter E. Carbonyl assays for determination of oxidatively modified proteins. Methods in Enzymology. 1994. pp. 346-357. https://doi.org/10.1016/S0076-6879(94)33040-9
Joyner MJ, Casey DP. Regulation of increased blood flow (Hyperemia) to muscles during exercise: A hierarchy of competing physiological needs. Physiological Reviews. 2015. pp. 549-601. https://doi.org/10.1152/physrev.00035.2013
Jones S, D'Silva A, Bhuva A, Lloyd G, Manisty C, Moon JC, et al. Improved exercise-related skeletal muscle oxygen consumption following uptake of endurance training measured using near-infrared spectroscopy. Front Physiol. 2017;8: 1-8. https://doi.org/10.3389/fphys.2017.01018
Steinbacher P, Eckl P. Impact of oxidative stress on exercising skeletal muscle. Biomolecules. 2015;5: 356-377. https://doi.org/10.3390/biom5020356
Hou Y, Wang X, Chen X, Zhang J, Ai X, Liang Y, et al. Establishment and evaluation of a simulated high‑altitude hypoxic brain injury model in SD rats. Mol Med Rep. 2019;19. https://doi.org/10.3892/mmr.2019.9939
Chaudhary P, Suryakumar G, Sharma YK, Ilavazhagan G. Differential response of the gastrocnemius and soleus muscles of rats to chronic hypobaric hypoxia. Aviat Sp Environ Med. 2012;83. https://doi.org/10.3357/ASEM.3278.2012
Agrawal A, Rathor R, Suryakumar G. Oxidative protein modification alters proteostasis under acute hypobaric hypoxia in skeletal muscles: a comprehensive in vivo study. Cell Stress Chaperones. 2017;22. https://doi.org/10.1007/s12192-017-0795-8
Dewi S, Mulyawan W, Wanandi SI, Sadikin M. The Effect of Intermittent Hypobaric Hypoxia on Oxidative Stress Status and Antioxidant Enzymes Activity in Rat Brain. Acta Biochim Indones. 2018;1: 46-51. https://doi.org/10.32889/actabioina.v1i2.16
Debevec T, Millet GP, Pialoux V. Hypoxia-induced oxidative stress modulation with physical activity. Frontiers in Physiology. 2017. https://doi.org/10.3389/fphys.2017.00084
Murray AJ. Metabolic adaptation of skeletal muscle to high altitude hypoxia: How new technologies could resolve the controversies. Genome Med. 2009;1. https://doi.org/10.1186/gm117
Deldicque L, Francaux M. Acute vs chronic hypoxia: what are the consequences for skeletal muscle mass? Cell Mol Exerc Physiol. 2013;2. https://doi.org/10.7457/cmep.v2i1.e5
Ji W, Wang L, He S, Yan L, Li T, Wang J, et al. Effects of acute hypoxia exposure with different durations on activation of Nrf2-ARE pathway in mouse skeletal muscle. PLoS One. 2018;13. https://doi.org/10.1371/journal.pone.0208474
Listrat A, Lebret B, Louveau I, Astruc T, Bonnet M, Lefaucheur L, et al. How muscle structure and composition influence meat and flesh quality. Scientific World Journal. 2016. https://doi.org/10.1155/2016/3182746
Penggalih MHS, Solichah KM. Dietary Intake and Strength Training Management among Weight Sports Athlete Category: Role of Protein Intake Level to Body Composition and Muscle Formation. Asian J Clin Nutr. 2018;11. https://doi.org/10.3923/ajcn.2019.24.31
Copyright (c) 2022 Authors
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
