Submit or Track your Manuscript LOG-IN

Role of Mitochondrial Function in Farm Animals’ Health and Production

AAVS_13_5_1142-1148

Review Article

Role of Mitochondrial Function in Farm Animals’ Health and Production

Mohsen Shakeri1, Hieu H Le2, Majid Shakeri3*

1Arka Industrial Cluster, Mashhad, Iran; 2Department of Animal Production, Faculty of Animal Science, Vietnam National University of Agriculture, Hanoi, Vietnam; 3National Poultry Research Center Agricultural Research Service, Athens GA, USA.

Abstract | Mitochondria are organelles found in most cells, play a crucial role in maintaining the body’s health by regulating energy metabolism, oxidative stress, and calcium homeostasis which all are essential for most body functions. The efficiency and quantity of mitochondria within cells are essential for several normal activities including grow, reproduce, and respond to environmental stressors. One of the factors that have been suggested as a reason for mitochondria dysfunction is genetics modifications. Farm animals have been genetically modified to produce more products to meet the market demand. However, along with the positive gains in production efficiency have come some unintended consequences such as lower products quality and impair animal’s health. Healthy mitochondria are essential for postmortem meat quality, impacting color and tenderness of the meat, while mitochondria dysfunction impairs performance and deteriorating final product quality. Mitochondria dysfunction alters cellular functions leading to a range of problems, including metabolic disorders and higher tissue damages. Although, several strategies have been introduced to improve mitochondria function, but none of them has fully addressed the problem in farm animals. Understanding the relationship between mitochondrial function and farm animal’s performance is crucial for the development of targeted therapies aimed at improving their performance and health. This review attempted to summarize recent works on mitochondrial function and its implications for animal health and performance and suggest potential treatment strategies.

Keywords | Mitochondria, Environment, Livestock, Performance, Meat quality, Treatment strategies


Received | March 11, 2025; Accepted | March 27, 2025; Published | April 28, 2025

*Correspondence | Majid Shakeri, National Poultry Research Center Agricultural Research Service, Athens GA, USA; Email: [email protected], [email protected]

Citation | Shakeri M, Le HH, Shakeri M (2025). Role of mitochondrial function in farm animals’ health and production. Adv. Anim. Vet. Sci. 13(5): 1142-1148.

DOI | https://dx.doi.org/10.17582/journal.aavs/2025/13.5.1142.1148

ISSN (Online) | 2307-8316; ISSN (Print) | 2309-3331

Copyright: 2025 by the authors. Licensee ResearchersLinks Ltd, England, UK.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).



Mitochondria

Mitochondria biology in farm animals: Mitochondria are oval/round organelles (approximately 0.5 to 10 μm in size) that exist in the cytoplasm of most eukaryotic cells with several vital functions in the body. Mitochondria are highly mobile, but they also can stay in one place and constantly changing their shape or performing fission (divide into two) and fusion (fuse two and make a larger one) depends on the body requirement. They are associated with microtubules (provide structure and shape to cells), which determines the orientation and distribution of mitochondria in different types of cells. Mitochondria distribution/population in tissues varies depending on the required amount of ATP (Kara, 2025). Mitochondria structure includes inner and outer membranes with completely different functions. The outer membrane is permeable to small and large molecules while the inner membrane is lipid bilayer and selectively permeable to only very small molecules into the matrix. The matrix contains DNA of the mitochondrial and the enzymes of the Krebs cycle or citric acid cycle (TCA cycle) (Alberts et al., 2002). Mitochondria has the cristae which helps to increase the surface area of the inner mitochondrial membrane, providing a higher number of electron transport chain enzymes and ATP synthase fits into the mitochondrion (Paumard et al., 2002). The intermembrane space is essential for protein transport, lipid homeostasis, and signaling pathways like apoptosis, basically coordinating various cellular activities by linking the outer membrane and the inner membrane (Herrmann and Riemer, 2010). The structure of mitochondria is presented in Figure 1.

 

The essential function of mitochondria is to generate a high amount of ATP for the body through oxidative phosphorylation and a series of reactions known as TCA cycle in the inner membrane (cristae). Although ATP production is the primary role of the mitochondrial, they are also responsible for several other important tasks including apoptosis, storing calcium, synthesis of heme (an iron-carrying protein) and maintain body temperature (Tzagoloff, 2012). Electrons move through protein complexes in the inner membrane, and energy generated from the electron chain is then used to transport proteins back across the membrane, which power ATP synthase to ATP (Zangari et al., 2020).

Apoptosis is a pathway that destroys old or unhealthy cells as part of growth and development (Palmer et al., 2021). Because certain diseases involve a breakdown in normal apoptosis, mitochondria are thought to play a role in the disease. The mitochondria release cytochrome C into the cytoplasm as a signal that activates cascade lead to cell degeneration and damage-induced degeneration (BossyWetzel et al., 1998).

Calcium is essential for a range of cellular functions including regulating cell survival, aerobic metabolism, neurotransmitter, muscle function and blood clotting (Protasoni and Zeviani, 2021). Mitochondria stores calcium using a transport mechanism named calcium uniporter that helps to move calcium into the mitochondria (Reggiani and Marcucci, 2022) and managing calcium level (Romero-Garcia and Prado-Garcia, 2019). The stored calcium releases when it needed by mitochondria for several purposes such as regulating calcium signaling (Pivovarova and Andrews, 2010), apoptosis and the citric acid (Reggiani and Marcucci, 2022).

Mitochondria respiration play an essential role in maintaining body temperature by generating heat within the body through a process called thermogenesis (Lane, 2018). More specifically, mitochondria produce heat through a mechanism called mitochondrial uncoupling where energy that would normally be used to create ATP is instead released as heat due to the movement of protons across the mitochondrial membrane without generating ATP. This occurs mainly through the activity of uncoupling proteins and is considered the primary source of heat generation within the body’s cells (Kang et al., 2024).

Mitochondria susceptible to mutations: Mitochondrial DNA (mtDNA), the circular chromosome located within mitochondria, is important for cellular energy production, and its integrity, and mutations or damages to mtDNA impacts overall cell’s health (Sharma and Sampath, 2019). Different sort of mutations may occur in mtDNA as follow: point mutation (single base change in the mtDNA sequence) (Craigen, 2012), large deletions or rearrangements (Tuppen et al., 2010), insertion (addition of DNA sequences) (Fields et al., 2022), duplication (creation of extra copies of DNA sequences) (Craigen, 2012), inversions (reversal of DNA sequences) (Tuppen et al., 2010) and heteroplasmy (Wallace and Chalkia, 2013). Majority of disorders associated with mitochondrial dysfunction are caused by mutations in mtDNA (Ryzhkova et al., 2018) resulting in reduced the production of cellular ATP. mtDNA is highly susceptible to mutations as the mitochondria is major a site of generating reactive oxygen species (ROS) (Shokolenko et al., 2009). mtDNA is in the mitochondrial matrix, when mitochondria’s health is disrupted, the mitochondria environment generates high levels of ROS, making mtDNA susceptible to oxidative damage (Nissanka and Moraes, 2018). Although several antioxidants within the mitochondria neutralize ROS, but some ROS may inflict damage to mtDNA. In addition, extensive oxidative damages caused by external factors may also increase damages to mtDNA.

Environmental Stressors and Mitochondria Dysfunction

Several environmental factors, such as high environmental temperature, high level of ammonia, and heavy metals, alter mitochondria function by increasing oxidative stress resulting in higher mutations in mtDNA followed by disruptions in cellular ATP production and potentially contributing to various diseases (Figure 2). In fact, mitochondrial health directly impacts livestock productivity, and it could be compromised by environmental factors.

 

High environmental temperature: Farm animals require optimum environmental temperature to improve the immune system, meat quality and growth performance (Belhadj Slimen et al., 2016; Shakeri et al., 2020). Under heat stress conditions, when body’s temperature passes a certain level, it will add additional pressure on animal’s body and will push them to use more nutrients to cool their body temperature than improving their performance. Heat stress negatively impacts biological molecules, cell functions and induces oxidative cell damage and activates of apoptosis pathways (Pandey et al., 2012). Long-term high temperature increases the production of ROS leading to higher oxidative damages to tissues by altering mitochondria function (Belhadj Slimen et al., 2016). ROS are a group of unstable molecules that can damage cell components when generated in high amount.

Although mitochondria are not the only place that generate ROS, they are responsible for the highest amount of ROS production in the body. When normal concentration of ROS is disturbed, mitochondria are the first cellular compartment to be damaged (England et al., 2004). Alterations in mitochondria structure caused by increased ROS production under heat stress lead to swollen mitochondria and broken cristae (Song et al., 2000), mitochondrial protein denaturation (Mujahid et al., 2007) and higher cell death (Du et al., 2008) which leads to higher tissue damage and potentially impairs animal’s performance and health. In fact, heat stress misfolds and aggregates proteins within the mitochondria by increasing ROS, leading to impaired mitochondrial function (Wilkening et al., 2018). Additionally, heat stress disrupts the mitochondrial membrane, which is important for ATP production and can increase apoptosis (Qian et al., 2004).

Ammonia: Livestock produce ammonia (colorless gas) by breakdown of animal’s urea/feces (Atia, 2006). When ammonia reaches to a danger level, increases lysosomal pH and results in the termination of lysosomal ammonia storage and ammonia reflux into mitochondria leading to higher mitochondrial damage and apoptosis (Shahid M et al., 2014). Ammonia damages mitochondria by disrupting the mitochondrial membrane leading to increased production of ROS, ultimately increasing oxidative stress and potentially causing cell death (Niknahad et al., 2017). Higher oxidative stress means higher tissue damages and deteriorating the production quality. In fact, if high amount of ammonia accumulates in the blood, damages mitochondria by inhibiting key enzymes in tricarboxylic acid cycle resulting in low energy production within mitochondria (Felipo and Butterworth, 2002).

Heavy metals: Heavy metals such as lead, cadmium, zinc and nickel can be found in livestock feed or water which can be toxic at high levels (Ebrahimi et al., 2023; Tahir and Alkheraije, 2023). Heavy metals can generate high amounts of ROS as well as ROS clearance malfunction lead to higher DNA damage (Itziou et al., 2011), alter mitochondria membrane permeability and inhibit antioxidant enzyme activity resulting in mitochondrial dysfunction (Sun et al., 2022) through Fenton reaction. The reaction acts as a catalyst to break down hydrogen peroxide and generates ROS (Shahid M et al., 2014). Furthermore, heavy metals disrupt the electron transport chain (within mitochondria) and increase damages to the mitochondrial membranes (inner and outer membranes), which can disrupt mitochondrial function, leading to reduced ATP production and increased ROS production (Sun et al., 2022).

Livestock Production and Mitochondria

Dairy: In dairy animals, mitochondria play a crucial role in milk production by generating the necessary ATP through cellular respiration, making them essential for the biosynthesis of milk components like proteins and fats, as the mammary gland requires a significant amount of ATP to synthesize milk. mtDNA is an important factor in mitochondrial function and impacts milk composition and energy density (Brajkovic et al., 2025). Conditions like heat stress can disrupt mitochondrial function in dairy cows, impacting their milk production and overall health (Favorit et al., 2021). Therefore, healthy mitochondrial is vital for high milk yield and overall dairy cow health (Favorit et al., 2021). Increased milking frequency in dairy cattle is associated with increased mitochondrial density in the mammary gland (Favorit et al., 2021).

Pig: In pigs, mitochondrial function is directly linked to their overall performance, particularly in terms of muscle growth and feed efficiency, as healthy mitochondria are crucial for producing energy needed for muscle contraction, meaning that pigs with better mitochondrial function tend to exhibit improved growth rates and better conversion of feed into muscle mass; research suggests that analyzing mitochondrial function in muscle tissue can be a good indicator of a pig’s overall performance potential (Qiao et al., 2023). Researchers often take muscle biopsies from pigs to analyze mitochondrial function by measuring parameters like oxygen consumption, ATP production, and mitochondrial membrane potential (Bekebrede et al., 2021; Fu et al., 2017).

Broiler chickens: In broiler chickens, mitochondrial function is directly linked to their performance, as healthy mitochondria are crucial for efficient energy production in muscle tissue, which is essential for optimal growth and feed conversion efficiency. However, factors like heat stress can significantly impair mitochondrial function, leading to reduced broiler performance and potential meat quality issues (Bottje et al., 2006; Shakeri et al., 2023). Studies have shown a correlation between mitochondrial function and feed efficiency (Algothmi et al., 2024; Bottje et al., 2006) and meat quality (Zhang et al., 2023), with broilers exhibiting better feed conversion ratios having more efficient mitochondria. Mitochondrial dysfunction can contribute to meat quality issues like woody breast (Shakeri et al., 2024) and spaghetti (Shakeri et al., 2024) in broilers, characterized by tough and fibrous muscle texture or broken fibers. Heat stress is a major concern for broiler production, as it can significantly impair mitochondrial function and lead to reduced growth rates (Algothmi et al., 2024).

Aquatic: Mitochondria in fish are important for energy production, heart function, and thermal tolerance (John et al., 2024). Mitochondrial generate heat during ROS production. Mitochondrial properties adjust during thermal acclimation, and the acclimation potential of cardiac mitochondria could be key to fish temperature tolerance/adaptation (John et al., 2024). Mitochondria from aquatic invertebrates show an increase in the rate of ROS efflux/formation as the assay temperature increases (Banh et al., 2016). Furthermore, mitochondrial internal temperature can be significantly higher than the surrounding cellular environment (Lane, 2018). This higher mitochondrial temperature acts like a “thermostatic radiator” to help maintain a stable body temperature. Additionally to thermal tolerance function and ATP production in aquatic, mitochondria are important for osmotic balance in aquatic, which means increases fish adaptation to different aquatic environments (Brijs et al., 2017). In fact, when cells experience osmotic stress, mitochondria initiate a rapid metabolic shift by changing glucose metabolism (suppressing pyruvate dehydrogenase) from oxidative phosphorylation to aerobic glycolysis, resulting in a decrease in oxygen consumption rate and an increase in extracellular acidification rate (Ikizawa et al., 2023).

 

Table 1: Strategies to improve mitochondria function in farm animals.

Name

Function

Alpha-lipoic acid and acetyl-L-carnitine

Helps to reduce oxidative stress

β-hydroxy-β-methylbutyrate

Enhances muscle health

N-acetylcysteine

Anti-inflammatory agent

Resveratrol

Mitigating oxidative stress

Ribonucleotide reductase

Improves mtDNA health

 

Potential Ways to Improve Mitochondria Function

Mitochondrial function in livestock can be improved through a variety of nutritional and pharmacological approaches (Table 1). Nutritional strategies, such as α-lipoic acid and acetyl-L-carnitine (increase mitochondrial ATP production) (Pizzorno, 2014) by reducing oxidative stress and increasing flow of oxygen-rich blood. In farm animals, studies showed that alpha-lipoic acid and acetyl-L-carnitine reduced oxidative stress while improved performance and health in goats and poultry (Li et al., 2019; Wang et al., 2017). β-hydroxy-β-methylbutyrate is a branched-chain amino acid leucine (increases mitochondrial mass, respiration capacity, and mitochondrial biogenesis) (Zhong et al., 2019) by increasing oxidative metabolism and gene expression of mitochondrial biogenesis. In farm animals, β-hydroxy-β-methylbutyrate enhanced muscle health, improve performance and immunity (Szcześniak et al., 2015). N-acetylcysteine (improves mitochondrial function) (Lapointe, 2014) by reducing oxidative stress and supporting cellular repair mechanisms, and antioxidants (improve mitochondrial efficiency) (Lowes et al., 2013) by reducing ROS production. In farm animals, N-acetylcysteine has antioxidant properties and acts as an anti-inflammatory agent (Ninković et al., 2024). Pharmacological strategies such as resveratrol (enhances mitochondrial biogenesis) (Ungvari et al., 2011) by regulating mitochondria. In farm animals, resveratrol as an antioxidant, showed improved health, growth, and meat quality in livestock, mitigating oxidative stress as well as improved various physiological functions (Meng et al., 2023). Ribonucleotide reductase activity (improve mitochondria function) (Shakeri et al., 2023) by improving mtDNA health. In poultry, reduction in ribonucleotide reductase activity showed to have adverse effects on meat quality (Shakeri et al., 2024).

CONCLUSIONS AND RECOMMENDATIONS

Mitochondria as a source of energy are essential for having functional cells. Malfunctioning mitochondria may increase oxidative damage in tissue resulting in deteriorating the quality of products. Environmental factors such as heat stress have major impact on mitochondria function. Although, many solutions have been introduced to improve mitochondria function, it seems nutritional modifications might be good an approach so far to cope with the problem but not a complete solution. Therefore, further investigations will be required to provide more reliable strategies such as genetics modifications (maybe edit mtDNA) and controlling environmental factors to have better outcomes. In short, mitochondrial-targeted therapies may bridge the gap between intensive farming and animal welfare.

ACKNOWLEDGEMENTS

The authors declare that this work was conducted solely by the listed authors, with no contributions from external individuals or organizations.

NOVELTY STATEMENTS

The novelty of this review lies in its specific focus on the causal link between environmental stress-induced mitochondrial impairment and its downstream negative effects on key animal production traits, paving the way for targeted mitigation strategies.

AUTHOR’S CONTRIBUTIONS

Mohsen Shakeri: Writing – original draft.

Majid Shakeri and Hieu Le: Writing – review and editing.

Ethical Statement

As this manuscript does not involve research on humans or animals, nor does it include vulnerable populations, an ethical statement is not applicable.

Funding

There was no funding received for this research.

Ethics Approval

Not applicable.

Consent for Publication

All the authors have read and approved the work.

Data Availability Statement

All data have been included in the article or referenced in the article.

Conflict of Interest

Authors declare no conflict of interest.

REFERENCES

Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P (2002). The mitochondrion. In Molecular Biology of the Cell. 4th edition. Garland Science.

Algothmi KM, Mahasneh ZM, Abdelnour SA, Khalaf QA, Noreldin AE, Barkat RA, Khalifa NE, Khafaga AF, Tellez-Isaias G, Alqhtani AH (2024). Protective impacts of mitochondria enhancers against thermal stress in poultry. Poult. Sci., 103(1): 103218. https://doi.org/10.1016/j.psj.2023.103218

Atia A (2006). Ammonia emissions and safety.

Banh S, Wiens L, Sotiri E, Treberg J (2016). Mitochondrial reactive oxygen species production by fish muscle mitochondria: potential role in acute heat-induced oxidative stress. Comparative Comp. Biochem. Physiol. B Biochem. Mol. Biol., 191: 99-107. https://doi.org/10.1016/j.cbpb.2015.10.001

Bekebrede AF, Keijer J, Gerrits WJ, de Boer VC (2021). Mitochondrial and glycolytic extracellular flux analysis optimization for isolated pig intestinal epithelial cells. Sci. Rep., 11(1): 19961. https://doi.org/10.1038/s41598-021-99460-0

Belhadj Slimen I, Najar T, Ghram A, Abdrrabba M (2016). Heat stress effects on livestock: molecular, cellular and metabolic aspects, a review. J. Anim. Physiol. Anim. Nutr., 100(3): 401-412. https://doi.org/10.1111/jpn.12379

BossyWetzel E, Newmeyer D, Green D (1998). Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVDspecific caspase activation and independently of mitochondrial transmembrane depolarization. The EMBO J., 17: 37–49. 1998. https://doi.org/10.1093/emboj/17.1.37

Bottje W, Pumford N, Ojano-Dirain C, Iqbal M, Lassiter K (2006). Feed efficiency and mitochondrial function. Poult. Sci., 85(1): 8-14. https://doi.org/10.1093/ps/85.1.8

Brajkovic V, Pocrnic I, Kaps M, Špehar M, Cubric-Curik V, Ristov S, Novosel D, Gorjanc G, Curik I (2025). Quantifying the effects of the mitochondrial genome on milk production traits in dairy cows: Empirical results and modeling challenges. J. Dairy Sci., 108(1): 664-678. https://doi.org/10.3168/jds.2024-25203

Brijs J, Sandblom E, Sundh H, Gräns A, Hinchcliffe J, Ekström A, Sundell K, Olsson C, Axelsson M, Pichaud N (2017). Increased mitochondrial coupling and anaerobic capacity minimizes aerobic costs of trout in the sea. Sci. Rep., 7(1): 45778. https://doi.org/10.1038/srep45778

Craigen WJ (2012). Mitochondrial DNA mutations: an overview of clinical and molecular aspects. Mitochondrial Disorders: Biochem. Mol. Anal., 3-15. https://doi.org/10.1007/978-1-61779-504-6_1

Du J, Di HS, Guo L, Li ZH, Wang GL (2008). Hyperthermia causes bovine mammary epithelial cell death by a mitochondrial-induced pathway. J. Therm. Biol., 33(1): 37-47. https://doi.org/10.1016/j.jtherbio.2007.06.002

Ebrahimi R, Ebrahimi M, Shakeri M (2023). Mitigating the adverse effects of lead and cadmium heavy metals-induced oxidative stress by phytogenic compounds in poultry. Poultry, 2(2): 235-251. https://doi.org/10.3390/poultry2020019

England K, O’Driscoll C, Cotter T (2004). Carbonylation of glycolytic proteins is a key response to drug-induced oxidative stress and apoptosis. Cell Death Differ., 11(3): 252-260. https://doi.org/10.1038/sj.cdd.4401338

Favorit V, Hood W, Kavazis A, Skibiel A (2021). Graduate Student Literature Review: Mitochondrial adaptations across lactation and their molecular regulation in dairy cattle. J. Dairy Sci., 104(9): 10415-10425. https://doi.org/10.3168/jds.2021-20138

Felipo V, Butterworth RF (2002). Mitochondrial dysfunction in acute hyperammonemia. Neurochem. Int., 40(6): 487-491. https://doi.org/10.1016/S0197-0186(01)00119-X

Fields PD, Waneka G, Naish M, Schatz MC, Henderson IR, Sloan DB (2022). Complete sequence of a 641-kb insertion of mitochondrial DNA in the Arabidopsis thaliana nuclear genome. Genome Biol. Evol., 14(5): evac059. https://doi.org/10.1093/gbe/evac059

Fu L, Xu Y, Hou Y, Qi X, Zhou L, Liu H, Luan Y, Jing L, Miao Y, Zhao S (2017). Proteomic analysis indicates that mitochondrial energy metabolism in skeletal muscle tissue is negatively correlated with feed efficiency in pigs. Sci. Rep. 7(1): 45291. https://doi.org/10.1038/srep45291

Herrmann J, Riemer J (2010). The intermembrane space of mitochondria. Antioxidants and redox signaling. Antioxid. Redox Signal., 13. https://doi.org/10.1089/ars.2009.3063

Ikizawa T, Ikeda K, Arita M, Kitajima S, Soga T, Ichijo H, Naguro I (2023). Mitochondria directly sense osmotic stress to trigger rapid metabolic remodeling via regulation of pyruvate dehydrogenase phosphorylation. J. Biol. Chem., 299(2). https://doi.org/10.1016/j.jbc.2022.102837

Itziou A, Kaloyianni M, Dimitriadis V (2011). In vivo and in vitro effects of metals in reactive oxygen species production, protein carbonylation, and DNA damage in land snails Eobania vermiculata. Arch. Environ. Contam. Toxicol., 60: 697-707. https://doi.org/10.1007/s00244-010-9583-5

John NI, Hadimundeen A, Abigeal DA, David HH, Ann G, Wendy S, David Ol, Jonathan CE (2024). Optimizing growth and mitochondrial function in rainbow trout, Oncorhynchus mykiss through eco-friendly dietary and changes in water temperature regimen strategies. Aquaculture, 595. https://doi.org/10.1016/j.aquaculture.2024.741591

Kang MG, Kim HR, Lee HY, Kwak C, Koh H, Kang BH, Roe JS, Rhee HW (2024). Mitochondrial Thermogenesis Can Trigger Heat Shock Response in the Nucleus. ACS Cent. Sci., 10: 1118-1303. https://doi.org/10.1021/acscentsci.3c01589

Kara R (2025). mitochondrion. Britannica. https://www.britannica.com/science/apoptosis

Lane N (2018). Hot mitochondria? PLoS Biol., 16(1): e2005113. https://doi.org/10.1371/journal.pbio.2005113

Lapointe J (2014). Mitochondria as promising targets for nutritional interventions aiming to improve performance and longevity of sows. J. Anim. Physiol. Anim. Nutr., 98(5): 809-821. https://doi.org/10.1111/jpn.12160

Li W, Wei F, Xu B, Sun Q, Deng W, Ma H, Bai J, Li S (2019). Effect of stocking density and alpha-lipoic acid on the growth performance, physiological and oxidative stress and immune response of broilers. Asian-Australas. J. Anim. Sci., 32(12): 1914. https://doi.org/10.5713/ajas.18.0939

Lowes D, Webster N, Murphy M, Galley H (2013). Antioxidants that protect mitochondria reduce interleukin-6 and oxidative stress, improve mitochondrial function, and reduce biochemical markers of organ dysfunction in a rat model of acute sepsis. Br. J. Anaesth., 110(3): 472-480. https://doi.org/10.1093/bja/aes577

Meng Q, Li J, Wang C, Shan A (2023). Biological function of resveratrol and its application in animal production: a review. J. Anim. Sci. Biotechnol., 14(1): 25. https://doi.org/10.1186/s40104-022-00822-z

Mujahid A, Pumford NR, Bottje W, Nakagawa K, Miyazawa T, Akiba Y, Toyomizu M (2007). Mitochondrial oxidative damage in chicken skeletal muscle induced by acute heat stress. Poult. Sci. J., 44(4): 439-445. https://doi.org/10.2141/jpsa.44.439

Niknahad H, Jamshidzadeh A, Heidari R, Zarei M, Ommati MM (2017). Ammonia-induced mitochondrial dysfunction and energy metabolism disturbances in isolated brain and liver mitochondria, and the effect of taurine administration: relevance to hepatic encephalopathy treatment. J. Clin. Exp. Hepatol., 3(3): 141-151. https://doi.org/10.5114/ceh.2017.68833

Ninković M, Žutić J, Tasić A, Arsić S, Bojkovski J, Zdravković N (2024). An innovative approach: The usage of N-Acetylcysteine in the therapy of pneumonia in neonatal calves. Animals., 14(19): 2852. https://doi.org/10.3390/ani14192852

Nissanka N, Moraes CT (2018). Mitochondrial DNA damage and reactive oxygen species in neurodegenerative disease. FEBS Lett., 592(5): 728-742. https://doi.org/10.1002/1873-3468.12956

Palmer CS, Anderson AJ, Stojanovski D (2021). Mitochondrial protein import dysfunction: mitochondrial disease, neurodegenerative disease and cancer. FEBS lett., 595(8): 1107-1131. https://doi.org/10.1002/1873-3468.14022

Pandey N, Kataria N, Kataria AK, Joshi A, Sankhala LN, Asopa S, Pachaury R (2012). Extreme ambiences vis-à-vis endogenous antioxidants of Marwari goat from arid tracts in India. Extreme Life, Biospeol. Astrobiol., 4(2): 29-33.

Paumard P, Vaillier J, Coulary B, Schaeffer J, Soubannier V, Mueller D, Velours J (2002). The ATP synthase is involved in generating mitochondrial cristae morphology. The EMBO J., 21: 221-230. https://doi.org/10.1093/emboj/21.3.221

Pivovarova NB, Andrews SB (2010). Calciumdependent mitochondrial function and dysfunction in neurons. The FEBS J., 277(18): 3622-3636. https://doi.org/10.1111/j.1742-4658.2010.07754.x

Pizzorno J (2014). Mitochondria fundamental to life and health. Integr. Med.: A Clin. J., 13(2): 8.

Protasoni M, Zeviani M (2021). Mitochondrial structure and bioenergetics in normal and disease conditions. Int. J. Mol. Sci., 22(2): 586. https://doi.org/10.3390/ijms22020586

Qian L, Song X, Ren H, Gong J, Cheng S (2004). Mitochondrial mechanism of heat stress-induced injury in rat cardiomyocyte. Cell Stress Chaperones, 9(3): 281. https://doi.org/10.1379/CSC-20R.1

Qiao L, Dou X, Song X, Chang J, Yi H, Xu C (2023). Targeting mitochondria with antioxidant nutrients for the prevention and treatment of postweaning diarrhea in piglets. Anim. Nutr., 15: 275-287. https://doi.org/10.1016/j.aninu.2023.09.002

Reggiani C, Marcucci L (2022). A controversial issue: Can mitochondria modulate cytosolic calcium and contraction of skeletal muscle fibers? J. Gen. Physiol., 154(9). https://doi.org/10.1085/jgp.202213167

Romero-Garcia S, Prado-Garcia H (2019). Mitochondrial calcium: Transport and modulation of cellular processes in homeostasis and cancer. Int. J. Oncol., 54(4): 1155-1167. https://doi.org/10.3892/ijo.2019.4696

Ryzhkova AI, Sazonova MA, Sinyov VV, Galitsyna EV, Chicheva MM, Melnichenko AA, Grechko AV, Postnov AY, Orekhov AN, Shkurat TP (2018). Mitochondrial diseases caused by mtDNA mutations: a mini-review. Ther. Clin. Risk Manag., 1933-1942. https://doi.org/10.2147/TCRM.S154863

Shahid M, Pourrut B, Dumat C, Nadeem M, Aslam M, Pinelli E (2014). Heavy-metal-induced reactive oxygen species: phytotoxicity and physicochemical changes in plants. Rev Environ Contam T., 232: 1-44. https://doi.org/10.1007/978-3-319-06746-9_1

Shakeri M, Choi J, Harris C, Buhr RJ, Kong B, Zhuang H, Bowker B (2024). Reduced ribonucleotide reductase RRM2 subunit expression increases DNA damage and mitochondria dysfunction in woody breast chickens. Am. J. Vet. Res., 1(aop): 1-7. https://doi.org/10.2460/ajvr.23.12.0283

Shakeri M, Choi J, Kong B, Zhuang H, Bowker B (2024). Proteomics Analysis Suggests Mitochondria Disorders and Cell Death Lead to Spaghetti Meat Myopathy. MMB., 8(1). https://doi.org/10.22175/mmb.18205

Shakeri M, Kong B, Zhuang H, Bowker B (2023). Potential role of ribonucleotide reductase enzyme in mitochondria function and woody breast condition in broiler chickens. Animals, 13(12): 2038. https://doi.org/10.3390/ani13122038

Shakeri M, Oskoueian E, Le HH, Shakeri M (2020). Strategies to combat heat stress in broiler chickens: Unveiling the roles of selenium, vitamin E and vitamin C. Vet. Sci., 7(2): 71. https://doi.org/10.3390/vetsci7020071

Sharma P, Sampath H (2019). Mitochondrial DNA integrity: Role in health and disease. Cells 8, 100. Mol. Ther. Nucleic Acids. https://doi.org/10.3390/cells8020100

Shokolenko I, Venediktova N, Bochkareva A, Wilson GL, Alexeyev MF (2009). Oxidative stress induces degradation of mitochondrial DNA. Nucleic Acids Res., 37(8): 2539-2548. https://doi.org/10.1093/nar/gkp100

Song XL, Qian LJ, Li FZ (2000). Injury of heat-stress to rat cardiomyocytes. Chin. J. Appl. Physiol., 16(3): 227-230.

Sun Q, Li Y, Shi L, Hussain R, Mehmood K, Tang Z, Zhang H (2022). Heavy metals induced mitochondrial dysfunction in animals: Molecular mechanism of toxicity. Toxicology, 469: 153136. https://doi.org/10.1016/j.tox.2022.153136

Szcześniak K, Ostaszewski P, Fuller JRJ, Ciecierska A, Sadkowski T (2015). Dietary supplementation of β‐hydroxy‐β‐methylbutyrate in animals–a review. J. Anim. Physiol. Anim. Nutr., 99(3): 405-417. https://doi.org/10.1111/jpn.12234

Tahir I, Alkheraije KA (2023). A review of important heavy metals toxicity with special emphasis on nephrotoxicity and its management in cattle. Front. Vet. Sci., 10: 1149720. https://doi.org/10.3389/fvets.2023.1149720

Tuppen HA, Blakely EL, Turnbull DM, Taylor RW (2010). Mitochondrial DNA mutations and human disease. Biochim. Biophys. Acta, Bioenerg., 1797(2): 113-128. https://doi.org/10.1016/j.bbabio.2009.09.005

Tzagoloff A (2012). Mitochondria. Springer Science and Business Media.

Ungvari Z, Sonntag WE, de Cabo R, Baur JA, Csiszar A (2011). Mitochondrial protection by resveratrol. ESSR., 39(3): 128-132. https://doi.org/10.1097/JES.0b013e3182141f80

Wallace DC, Chalkia D (2013). Mitochondrial DNA genetics and the heteroplasmy conundrum in evolution and disease. Cold Spring Harb. Perspect. Biol., 5(11): a021220. https://doi.org/10.1101/cshperspect.a021220

Wang D, Zhou L, Zhou H, Hou G, Shi L (2017). Effects of dietary α-lipoic acid on carcass characteristics, antioxidant capability and meat quality in Hainan black goats. Ital. J. Anim. Sci., 16(1): 61-67. https://doi.org/10.1080/1828051X.2016.1263546

Wilkening A, Rüb C, Sylvester M, Voos W (2018). Analysis of heat-induced protein aggregation in human mitochondria. J. Biol. Chem., 293(29): 11537-11552. https://doi.org/10.1074/jbc.RA118.002122

Zangari J, Petrelli F, Maillot B, Martinou JC (2020). The multifaceted pyruvate metabolism: role of the mitochondrial pyruvate carrier. Biomolecules, 10(7): 1068. https://doi.org/10.3390/biom10071068

Zhang X, Xing T, Li J, Zhang L, Gao F (2023). Mitochondrial dysfunction and calcium dyshomeostasis in the pectoralis major muscle of broiler chickens with wooden breast myopathy. Poult. Sci., 102(9): 102872. https://doi.org/10.1016/j.psj.2023.102872

Zhong Y, Zeng L, Deng J, Duan Y, Li F (2019). β-hydroxy-β-methylbutyrate (HMB) improves mitochondrial function in myocytes through pathways involving PPARβ/δ and CDK4. Nutrition, 60: 217-226. https://doi.org/10.1016/j.nut.2018.09.032

To share on other social networks, click on any share button. What are these?

Advances in Animal and Veterinary Sciences

May

Adv. Anim. Vet. Sci., Vol. 13, Iss. 5,

Featuring

Click here for more

Subscribe Today

Receive free updates on new articles, opportunities and benefits


Subscribe Unsubscribe