Malondialdehyde and carbonyl levels in skeletal muscle tissues after intermittent hypobaric hypoxia exposures

  • Syarifah Dewi Department of Biochemistry and Molecular Biology, Faculty of Medicine Universitas Indonesia, Jakarta, Indonesia https://orcid.org/0000-0003-2148-9020
  • Alexander Rafael Satyadharma Undergraduate Program in Medical Sciences, Faculty of Medicine Universitas Indonesia, Jakarta, Indonesia
  • Albertus Raditya Danendra Undergraduate Program in Medical Sciences, Faculty of Medicine Universitas Indonesia, Jakarta, Indonesia
  • Wardaya Department of Aerophysiology, Lakespra Saryanto, Indonesian National Air Force Army, Jakarta, Indonesia
Keywords: intermittent hypobaric hypoxia, malondialdehyde, carbonyl, skeletal muscle

Abstract

Background: Hypobaric hypoxia is a hypoxic condition in high altitude because of low oxygen pressure, which can induce oxidative stress. Skeletal muscle is one of important organ that could be affected by oxidative stress and cause contractile dysfunction.

Objective: The aim of this study was investigating the effect of intermittent hypobaric hypoxia induction on malondialdehyde (MDA) and carbonyl levels as oxidative stress marker in rat skeletal muscle.

Methods: This is an in vivo experimental study that carried out by conditioning four groups of Wistar rats in a hypobaric hypoxic state in a hypobaric chamber one- (I), two- (II), three- (III), and four- (IV) times (IV) with interval 7 days. Rats in normobaric conditions act as control group. The gastrocnemius muscle of all rats was taken to measure the MDA and carbonyl level.

Results: The MDA level was significantly increased in the group I compared to control group (p<0.05). There were decreasing of MDA level in group II, III and IV compared to group I. The carbonyl level was found significantly increased in group I compared to control group (p<0.05), but the higher level was found in group II. Carbonyl level tend to decrease in group III and IV, but the level was still higher compared to control group.

Conclusion: We concluded that the MDA and carbonyl levels were increased in skeletal muscle after one-time hypobaric hypoxia exposure which meant oxidative stress increases, and they tend to decrease after intermittent hypobaric hypoxia exposure which indicate an adaptation of skeletal muscle to hypoxic condition.

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. doi:10.1371/journal.pone.0239194

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. doi:10.1186/cc5142

https://doi.org/10.1186/cc5142

Peacock A. ABC of oxygen. Oxygen at high altitude. Br Med J. 1998;317: 1063-1066. doi:10.1136/bmj.317.7165.1063

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. doi:10.1016/j.bbabio.2010.02.011

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. doi:10.1016/j.redox.2017.02.012

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. doi:10.1089/ars.2009.2887

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. doi:10.1016/j.bbabio.2008.07.003

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. doi:10.1016/0891-5849(90)90131-2

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. doi:10.1016/S0009-8981(03)00003-2

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. doi:10.1152/physrev.00035.2013

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. doi:10.3389/fphys.2017.01018

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. doi:10.3390/biom5020356

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. doi:10.3892/mmr.2019.9939

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. doi:10.3357/ASEM.3278.2012

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. doi:10.1007/s12192-017-0795-8

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. doi:10.3389/fphys.2017.00084

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. doi:10.1186/gm117

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. doi:10.7457/cmep.v2i1.e5

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. doi:10.1371/journal.pone.0208474

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. doi:10.1155/2016/3182746

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. doi:10.3923/ajcn.2019.24.31

https://doi.org/10.3923/ajcn.2019.24.31

Published
2022-11-18
How to Cite
Dewi, S., Satyadharma, A. R., Danendra, A. R., & Wardaya. (2022). Malondialdehyde and carbonyl levels in skeletal muscle tissues after intermittent hypobaric hypoxia exposures. Acta Biochimica Indonesiana, 5(2), 113. https://doi.org/10.32889/actabioina.113