The “Sunshine Vitamin” and Its Antioxidant Benefits for Enhancing Muscle Function
<p>Vitamin D’s role in skeletal muscle. Vitamin D can be acquired through skin synthesis or from diet. Both vitamin D3 and D2 undergo the same metabolic processes to produce their active forms. While the primary role of vitamin D is to regulate calcium levels and ensure skeletal and muscle health, it also serves as a powerful immunoregulator, influencing the inflammatory response, muscle damage, and aerobic capacity. Circulating 25(OH)D binds to the carrier protein DBP. PTH promotes renal Ca<sup>2+</sup> retention and activates the synthesis of active vitamin D, which, in conjunction with the vitamin D receptor (VDR), facilitates Ca<sup>2+</sup> and phosphate absorption. Vitamin D deficiency (VDD) or inadequate sun exposure can elevate PTH levels, leading to skeletal fragility. In skeletal muscle, the 25(OH)D-DBP complex is transported into target cells through the LRP2/CUBN transmembrane complex. Inside the cell, the D-DBP complex associates with cytoplasmic actin. 1,25(OH)2D triggers the expression of protein 1, affecting MyoD1 activation. Vitamin D also regulates the FOXO3 signaling pathways, enhancing myoblast self-renewal. VDR expression in skeletal muscle promotes muscle protein synthesis, is crucial for maintaining muscle mass, and aids in muscle regeneration. Abbreviations in alphabetical order: 1,25(OH)2D3—calcitriol; FOXO—forkhead family of transcription factors; LRP2/CUBN—megalin–cubilin transmembrane complex; MyoD1—myogenic determination factor 1; PTH—parathyroid hormone; DBP—vitamin D binding protein; vitamin D receptor (VDR).</p> "> Figure 2
<p>Relationship between oxidative stress and weakness of muscle. ROS generated from localized inflammation activate immune cells, initiating a harmful cycle characterized by the release of pro-inflammatory mediators, such as TNFα, IL-6, and CRP. Despite the presence of an impaired antioxidant system, including decreased levels of GSH and SOD, oxidative damage remains unchecked. Furthermore, inflammation disrupts mitochondrial function in muscle through the NO signaling pathway, triggering cell death via OMM permeabilization. Oxidative stress accelerates cellular senescence by activating FOXO and diminishing SIRT-1, leading to heightened MMP-9 and NF-κB activity. This escalated oxidative stress precipitates myocyte dysfunction and apoptosis, resulting in contractile dysfunction, fibrosis, hypertrophy, and impaired muscle remodeling. Additionally, there is a transition towards a type-IIx-oriented muscle phenotype with compromised oxygen distribution and utilization, ultimately impairing functionality. Abbreviations in alphabetical order: CRP—C reactive protein; FOXO—forkhead family of transcription factors; GSH—glutathione peroxidase; IL-6—Interleukin 6; MMP-9—matrix metallopeptidase 9; NF-κB—nuclear factor kappa-light-chain-enhancer of activated B cells; NO—nitrogen monoxide; OMM—outer mitochondrial membrane; RNS—reactive nitrogen species; ROS—reactive oxygen species; SIRT-1—sirtuin-1; SOD—superoxide dismutase; TNFα—tumor receptor necrosis factor alpha.</p> "> Figure 3
<p>Antioxidative role of vitamin D in muscle dysfunction. Blue arrow indicates activation; red arrow indicates inhibition. Vitamin D activates the VDR in satellite cells, enhancing their self-renewal, proliferation, and differentiation capabilities. Activation of the VDR also mitigates oxidative stress, promoting mitochondrial biogenesis and fusion while reducing oxidative damage and dysfunction. This process improves mitochondrial network structure through the regulation of MFN1/2, OPA1, and Drp1 expression. Vitamin D positively influences Sirt1 activity and enhances mitochondrial function. Supplementation with vitamin D activates Sirt1 and AMPK in skeletal muscle cells. Vitamin D further increases the expression of irisin precursors in muscle cells, contingent upon intact Sirt1 expression. Both AMPK and Sirt1 regulate PGC-1α activation and transcription, influencing irisin secretion in skeletal muscle cells. Vitamin D upregulates FOXO1 protein and suppresses atrogin-1 and MuRF1 expression. Additionally, VDS triggers VDR and induces the Nrf2-Keap1 antioxidant pathway. Abbreviations in alphabetical order: AMP—5′ AMP-activated protein kinase; 1,25(OH)2D3—calcitriol; Drp1—dynamin-related protein 1; IL-1β—interleukin-1 beta; MFN1/2—mitofusin; OPA—mitochondrial dynamin like GTPase; PGC-1α—peroxisome proliferator-activated receptor-gamma coactivator; PTH—parathyroid hormone; ROS—reactive oxygen species; SIRT-1—sirtuin-1; SOD—superoxide dis-mutase; TNFα—tumor receptor necrosis factor alpha; VDR—vitamin D receptor.</p> ">
Abstract
:1. Introduction
2. Understanding the Biological Influence of Vitamin D on Muscle Performance
3. Exploring the Role of Oxidative Stress on Muscle Weakness
4. Unveiling the Molecular Pathways of Vitamin D in Musculoskeletal Balance
5. Vitamin D Deficiency and Muscle Dysfunction
6. The Antioxidative Capacity of Vitamin D in Muscle Dysfunction
7. Examining the Role of Mitochondrial Function in Muscle Weakness
8. Modulating Mitochondrial Functionality through Vitamin D Regulation
9. Conclusions
Author Contributions
Funding
Informed Consent Statement
Data Availability Statement
Conflicts of Interest
References
- Rai, M.; Demontis, F. Systemic Nutrient and Stress Signaling via Myokines and Myometabolites. Annu. Rev. Physiol. 2016, 78, 85–107. [Google Scholar] [CrossRef] [PubMed]
- Blaauw, B.; Schiaffino, S.; Reggiani, C. Mechanisms modulating skeletal muscle phenotype. Compr. Physiol. 2013, 3, 1645–1687. [Google Scholar] [CrossRef] [PubMed]
- Srikanthan, P.; Karlamangla, A.S. Muscle mass index as a predictor of longevity in older adults. Am. J. Med. 2014, 127, 547–553. [Google Scholar] [CrossRef]
- Casabona, A.; Valle, M.S.; Laudani, L.; Crimi, C.; Russo, C.; Malaguarnera, L.; Crimi, N.; Cioni, M. Is the Power Spectrum of Electromyography Signal a Feasible Tool to Estimate Muscle Fiber Composition in Patients with COPD? J. Clin. Med. 2021, 10, 3815. [Google Scholar] [CrossRef] [PubMed]
- Derbré, F.; Gratas-Delamarche, A.; Gómez-Cabrera, M.C.; Viña, J. Inactivity-induced oxidative stress: A central role in age-related sarcopenia? Eur. J. Sport Sci. 2014, 1, S98–S108. [Google Scholar] [CrossRef] [PubMed]
- Cao, R.Y.; Li, J.; Dai, Q.; Li, Q.; Yang, J. Muscle Atrophy: Present and Future. Adv. Exp. Med. Biol. 2018, 1088, 605–624. [Google Scholar] [CrossRef]
- Valle, M.S.; Casabona, A.; Di Fazio, E.; Crimi, C.; Russo, C.; Malaguarnera, L.; Crimi, N.; Cioni, M. Impact of chronic obstructive pulmonary disease on passive viscoelastic components of the musculoarticular system. Sci. Rep. 2021, 11, 18077. [Google Scholar] [CrossRef]
- Russo, C.; Valle, M.S.; Casabona, A.; Spicuzza, L.; Sambataro, G.; Malaguarnera, L. Vitamin D Impacts on Skeletal Muscle Dysfunction in Patients with COPD Promoting Mitochondrial Health. Biomedicines 2022, 10, 898. [Google Scholar] [CrossRef]
- Patergnani, S.; Bouhamida, E.; Leo, S.; Pinton, P.; Rimessi, A. Mitochondrial Oxidative Stress and “Mito-Inflammation”: Actors in the Diseases. Biomedicines 2021, 9, 216. [Google Scholar] [CrossRef]
- Sartori, R.; Romanello, V.; Sandri, M. Mechanisms of muscle atrophy and hypertrophy: Implications in health and disease. Nat. Commun. 2021, 12, 330. [Google Scholar] [CrossRef]
- Romanello, V.; Sandri, M. The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass. Cell Mol. Life Sci. 2021, 78, 1305–1328. [Google Scholar] [CrossRef] [PubMed]
- Bollen, S.E.; Bass, J.J.; Fujita, S.; Wilkinson, D.; Hewison, M.; Atherton, P.J. The Vitamin D/Vitamin D receptor (VDR) axis in muscle atrophy and sarcopenia. Cell Signal. 2022, 96, 110355. [Google Scholar] [CrossRef]
- Valle, M.S.; Russo, C.; Casabona, A.; Crimi, N.; Crimi, C.; Colaianni, V.; Cioni, M.; Malaguarnera, L. Anti-inflammatory role of vitamin D in muscle dysfunctions of patients with chronic obstructive pulmonary disease: A comprehensive review. Minerva Med. 2023, 114, 357–371. [Google Scholar] [CrossRef] [PubMed]
- Laird, E.; Ward, M.; McSorley, E.; Strain, J.J.; Wallace, J. Vitamin D and bone health: Potential mechanisms. Nutrients 2010, 2, 693–724. [Google Scholar] [CrossRef]
- Ceglia, L. Vitamin D and skeletal muscle tissue and function. Mol. Aspects Med. 2008, 29, 407–414. [Google Scholar] [CrossRef]
- Bischoff, H.A.; Borchers, M.; Gudat, F.; Duermueller, U.; Theiler, R.; Stähelin, H.B.; Dick, W. In situ detection of 1,25-dihydroxyvitamin D3 receptor in human skeletal muscle tissue. Histochem. J. 2001, 33, 19–24. [Google Scholar] [CrossRef] [PubMed]
- Garcia, L.A.; King, K.K.; Ferrini, M.G.; Norris, K.C.; Artaza, J.N. 1,25(OH)2 vitamin D3 stimulates myogenic differentiation by inhibiting cell proliferation and modulating the expression of promyogenic growth factors and myostatin in C2C12 skeletal muscle cells. Endocrinology 2011, 152, 2976–2986. [Google Scholar] [CrossRef]
- Mannino, G.; Russo, C.; Maugeri, G.; Musumeci, G.; Vicario, N.; Tibullo, D.; Giuffrida, R.; Parenti, R.; Lo Furno, D. Adult stem cell niches for tissue homeostasis. J. Cell. Physiol. 2022, 237, 239–257. [Google Scholar] [CrossRef]
- Srikuea, R.; Hirunsai, M.; Charoenphandhu, N. Regulation of vitamin D system in skeletal muscle and resident myogenic stem cell during development, maturation, and ageing. Sci. Rep. 2020, 10, 8239. [Google Scholar] [CrossRef]
- Dalton, T.P.; Shertzer, H.G.; Puga, A. Regulation of gene expression by reactive oxygen. Annu. Rev. Pharmacol. Toxicol. 1999, 39, 67–101. [Google Scholar] [CrossRef]
- Sies, H.; Belousov, V.V.; Chandel, N.S.; Davies, M.J.; Jones, D.P.; Mann, G.E.; Murphy, M.P.; Yamamoto, M.; Winterbourn, C. Defining roles of specific reactive oxygen species (ROS) in cell biology and physiology. Nat. Rev. Mol. Cell Biol. 2022, 23, 499–515. [Google Scholar] [CrossRef] [PubMed]
- Piacenza, L.; Zeida, A.; Trujillo, M.; Radi, R. The superoxide radical switch in the biology of nitric oxide and peroxynitrite. Physiol. Rev. 2022, 102, 1881–1906. [Google Scholar] [CrossRef] [PubMed]
- Warraich, U.E.; Hussain, F.; Kayani, H.U.R. Aging-Oxidative stress, antioxidants and computational modeling. Heliyon 2020, 6, e04107. [Google Scholar] [CrossRef] [PubMed]
- Ji, Y.; Li, M.; Chang, M.; Liu, R.; Qiu, J.; Wang, K.; Deng, C.; Shen, Y.; Zhu, J.; Wang, W.; et al. Inflammation: Roles in Skeletal Muscle Atrophy. Antioxidants 2022, 11, 1686. [Google Scholar] [CrossRef] [PubMed]
- Andrade, B.; Jara-Gutiérrez, C.; Paz-Araos, M.; Vázquez, M.C.; Díaz, P.; Murgas, P. The Relationship between Reactive Oxygen Species and the cGAS/STING Signaling Pathway in the Inflammaging Process. Int. J. Mol. Sci. 2022, 23, 15182. [Google Scholar] [CrossRef] [PubMed]
- Grivennikova, V.G.; Vinogradov, A.D. Mitochondrial production of reactive oxygen species. Biochemistry 2013, 78, 1490–1511. [Google Scholar] [CrossRef] [PubMed]
- Turrens, J.F. Mitochondrial formation of reactive oxygen species. J. Physiol. 2003, 552 Pt 2, 335–344. [Google Scholar] [CrossRef] [PubMed]
- Cinelli, M.A.; Do, H.T.; Miley, G.P.; Silverman, R.B. Inducible nitric oxide synthase: Regulation, structure, and inhibition. Med. Res. Rev. 2020, 40, 158–189. [Google Scholar] [CrossRef] [PubMed]
- Magnani, F.; Mattevi, A. Structure and mechanisms of ROS generation by NADPH oxidases. Curr. Opin. Struct. Biol. 2019, 59, 91–97. [Google Scholar] [CrossRef]
- Miller, A.F. Superoxide dismutases: Ancient enzymes and new insights. FEBS Lett. 2012, 586, 585–595. [Google Scholar] [CrossRef]
- Cantin, A.M.; Larivée, P.; Bégin, R.O. Extracellular glutathione suppresses human lung fibroblast proliferation. Am. J. Respir. Cell Mol. Biol. 1990, 3, 79–85. [Google Scholar] [CrossRef] [PubMed]
- Akira, S.; Kishimoto, A. NF-IL6 and NF-kB in cytokine gene regulation. Immunol. Adv. 1997, 65, 1–46. [Google Scholar]
- Gilmore, T.D. Introduction to NF-kappa B: Players, paths, perspectives. Oncogene 2006, 25, 6680–6684. [Google Scholar] [CrossRef] [PubMed]
- Hirota, K.; Murata, M.; Sachi, Y.; Nakamura, H.; Takeuchi, J.; Mori, K.; Yodoi, J. Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step redox regulation mechanism of NF-kappaB transcription factor. J. Biol. Chem. 1999, 274, 27891–27897. [Google Scholar] [CrossRef] [PubMed]
- Barnes, P.J.; Baker, J.; Donnelly, L.E. Cellular Senescence as a Mechanism and Target in Chronic Lung Diseases. Am. J. Respir. Crit. Care Med. 2019, 200, 556–564. [Google Scholar] [CrossRef] [PubMed]
- Gambini, J.; Stromsnes, K. Oxidative Stress and Inflammation: From Mechanisms to Therapeutic Approaches. Biomedicines 2022, 10, 753. [Google Scholar] [CrossRef] [PubMed]
- Bienaimé, F.; Prié, D.; Friedlander, G.; Souberbielle, J.C. Metabolism and activity of vitamin D in the parathyroid gland. Mol. Cell. Endocrinol. 2011, 347, 30–41. [Google Scholar] [CrossRef] [PubMed]
- Ainbinder, A.; Boncompagni, S.; Protasi, F.; Dirksen, R.T. Role of Mitofusin-2 in mitochondrial localization and calcium uptake in skeletal muscle. Cell Calcium 2015, 57, 14–24. [Google Scholar] [CrossRef] [PubMed]
- Wang, Y.; Gu, Y.; Huang, J.; Wu, H.; Meng, G.; Zhang, Q.; Liu, L.; Zhang, S.; Wang, X.; Zhang, J.; et al. Serum vitamin D status and circulating irisin levels in older adults with sarcopenia. Front. Nutr. 2022, 9, 1051870. [Google Scholar] [CrossRef]
- Cannon, B.; Nedergaard, J. Brown adipose tissue: Function and physiological significance. Physiol. Rev. 2004, 84, 277–359. [Google Scholar] [CrossRef]
- Halling, J.F.; Pilegaard, H. PGC-1α-mediated regulation of mitochondrial function and physiological implications. Appl. Physiol. Nutr. Metab. 2020, 45, 927–936. [Google Scholar] [CrossRef] [PubMed]
- Adamovich, Y.; Shlomai, A.; Tsvetkov, P.; Umansky, K.B.; Reuven, N.; Estall, J.L.; Spiegelman, B.M.; Shaul, Y. The protein level of PGC-1α, a key metabolic regulator, is controlled by NADH-NQO1. Mol. Cell Biol. 2013, 33, 2603–2613. [Google Scholar] [CrossRef] [PubMed]
- Korta, P.; Pocheć, E.; Mazur-Biały, A. Irisin as a Multifunctional Protein: Implications for Health and Certain Diseases. Medicina 2019, 55, 485. [Google Scholar] [CrossRef]
- Askari, H.; Rajani, S.F.; Poorebrahim, M.; Haghi-Aminjan, H.; Raeis-Abdollahi, E.; Abdollahi, M. A glance at the therapeutic potential of irisin against diseases involving inflammation, oxidative stress, and apoptosis: An introductory review. Pharmacol. Res. 2018, 129, 44–55. [Google Scholar] [CrossRef] [PubMed]
- Xin, C.; Liu, J.; Zhang, J.; Zhu, D.; Wang, H.; Xiong, L.; Lee, Y.; Ye, J.; Lian, K.; Xu, C.; et al. Irisin improves fatty acid oxidation and glucose utilization in type 2 diabetes by regulating the AMPK signaling pathway. Int. J. Obes. 2016, 40, 443–451. [Google Scholar] [CrossRef] [PubMed]
- Stavenuiter, A.W.; Arcidiacono, M.V.; Ferrantelli, E.; Keuning, E.D.; Vila Cuenca, M.; Wee, P.M.; Beelen, R.H.; Vervloet, M.G.; Dusso, A.S. A novel rat model of vitamin D deficiency: Safe and rapid induction of vitamin D and calcitriol deficiency without hyperparathyroidism. Biomed. Res. Int. 2015, 2015, 604275. [Google Scholar] [CrossRef] [PubMed]
- Nadimi, H.; Djazayery, A.; Javanbakht, M.H.; Dehpour, A.; Ghaedi, E.; Derakhshanian, H.; Mohammadi, H.; Zarei, M.; Djalali, M. The Effect of Vitamin D Supplementation on Serum and Muscle Irisin Levels, and FNDC5 Expression in Diabetic Rats. Rep. Biochem. Mol. Biol. 2019, 8, 236–243. [Google Scholar] [PubMed]
- Faienza, M.F.; Brunetti, G.; Sanesi, L.; Colaianni, G.; Celi, M.; Piacente, L.; D’Amato, G.; Schipani, E.; Colucci, S.; Grano, M. High irisin levels are associated with better glycemic control and bone health in children with Type 1 diabetes. Diabetes Res. Clin. Pract. 2018, 141, 10–17. [Google Scholar] [CrossRef] [PubMed]
- Colaianni, G.; Oranger, A.; Dicarlo, M.; Lovero, R.; Storlino, G.; Pignataro, P.; Fontana, A.; Di Serio, F.; Ingravallo, A.; Caputo, G.; et al. Irisin Serum Levels and Skeletal Muscle Assessment in a Cohort of Charcot-Marie-Tooth Patients. Front. Endocrinol. (Lausanne) 2022, 13, 886243. [Google Scholar] [CrossRef]
- Chang, E. 1,25-Dihydroxyvitamin D Decreases Tertiary Butyl-Hydrogen Peroxide-Induced Oxidative Stress and Increases AMPK/SIRT1 Activation in C2C12 Muscle Cells. Molecules 2019, 24, 3903. [Google Scholar] [CrossRef]
- Cantó, C.; Jiang, L.Q.; Deshmukh, A.S.; Mataki, C.; Coste, A.; Lagouge, M.; Zierath, J.R.; Auwerx, J. Interdependence of AMPK and SIRT1 for metabolic adaptation to fasting and exercise in skeletal muscle. Cell Metab. 2010, 11, 213–219. [Google Scholar] [CrossRef]
- Wiciński, M.; Adamkiewicz, D.; Adamkiewicz, M.; Śniegocki, M.; Podhorecka, M.; Szychta, P.; Malinowski, B. Impact of Vitamin D on Physical Efficiency and Exercise Performance-A Review. Nutrients 2019, 11, 2826. [Google Scholar] [CrossRef] [PubMed]
- Wimalawansa, S.J. Vitamin D Deficiency: Effects on Oxidative Stress, Epigenetics, Gene Regulation, and Aging. Biology 2019, 8, 30. [Google Scholar] [CrossRef] [PubMed]
- Prokopidis, K.; Giannos, P.; Katsikas Triantafyllidis, K.; Kechagias, K.S.; Mesinovic, J.; Witard, O.C.; Scott, D. Effect of vitamin D monotherapy on indices of sarcopenia in community-dwelling older adults: A systematic review and meta-analysis. J. Cachexia Sarcopenia Muscle 2022, 13, 1642–1652. [Google Scholar] [CrossRef]
- Ceglia, L.; Niramitmahapanya, S.; da Silva Morais, M.; Rivas, D.A.; Harris, S.S.; Bischoff-Ferrari, H.; Fielding, R.A.; Dawson-Hughes, B. A randomized study on the effect of vitamin D3 supplementation on skeletal muscle morphology and vitamin D receptor concentration in older women. J. Clin. Endocrinol. Metab. 2013, 98, E1927–E1935. [Google Scholar] [CrossRef]
- Pfeifer, M.; Begerow, B.; Minne, H.W.; Suppan, K.; Fahrleitner-Pammer, A.; Dobnig, H. Effects of a long-term vitamin D and calcium supplementation on falls and parameters of muscle function in community-dwelling older individuals. Osteoporos. Int. 2009, 20, 315–322. [Google Scholar] [CrossRef]
- Hirose, Y.; Onishi, T.; Miura, S.; Hatazawa, Y.; Kamei, Y. Vitamin D Attenuates FOXO1-Target Atrophy Gene Expression in C2C12 Muscle Cells. J. Nutr. Sci. Vitaminol. 2018, 64, 229–232. [Google Scholar] [CrossRef] [PubMed]
- Endo, I.; Inoue, D.; Mitsui, T.; Umaki, Y.; Akaike, M.; Yoshizawa, T.; Kato, S.; Matsumoto, T. Deletion of vitamin D receptor gene in mice results in abnormal skeletal muscle development with deregulated expression of myoregulatory transcription factors. Endocrinology 2003, 144, 5138–5144. [Google Scholar] [CrossRef]
- Valle, M.S.; Russo, C.; Malaguarnera, L. Protective role of vitamin D against oxidative stress in diabetic retinopathy. Diabetes Metab. Res. Rev. 2021, 37, e3447. [Google Scholar] [CrossRef]
- Rossi, A.; Pizzo, P.; Filadi, R. Calcium, mitochondria and cell metabolism: A functional triangle in bioenergetics. Biochim. Biophys. Acta Mol. Cell Res. 2019, 1866, 1068–1078. [Google Scholar] [CrossRef]
- Modesti, L.; Danese, A.; Vitto, V.A.M.; Ramaccini, D.; Aguiari, G.; Gafà, R.; Lanza, G.; Giorgi, C.; Pinton, P. Mitochondrial Ca2+ Signaling in Health, Disease and Therapy. Cells 2021, 10, 1317. [Google Scholar] [CrossRef] [PubMed]
- van der Meijden, K.; Bravenboer, N.; Dirks, N.F.; Heijboer, A.C.; den Heijer, M.; de Wit, G.M.; Offringa, C.; Lips, P.; Jaspers, R.T. Effects of 1,25(OH)2D3 and 25(OH)D3 on C2C12 Myoblast Proliferation, Differentiation, and Myotube Hypertrophy. J. Cell Physiol. 2016, 231, 2517–2528. [Google Scholar] [CrossRef] [PubMed]
- Latham, C.M.; Brightwell, C.R.; Keeble, A.R.; Munson, B.D.; Thomas, N.T.; Zagzoog, A.M.; Fry, C.S.; Fry, J.L. Vitamin D Promotes Skeletal Muscle Regeneration and Mitochondrial Health. Front. Physiol. 2021, 12, 660498. [Google Scholar] [CrossRef] [PubMed]
- Bhat, M.; Ismail, A. Vitamin D treatment protects against and reverses oxidative stress induced muscle proteolysis. J. Steroid Biochem. Mol. Biol. 2015, 152, 171–179. [Google Scholar] [CrossRef] [PubMed]
- Ryan, Z.C.; Craig, T.A.; Folmes, C.D.; Wang, X.; Lanza, I.R.; Schaible, N.S.; Salisbury, J.L.; Nair, K.S.; Terzic, A.; Sieck, G.C.; et al. 1α,25-Dihydroxyvitamin D3 Regulates Mitochondrial Oxygen Consumption and Dynamics in Human Skeletal Muscle Cells. J. Biol. Chem. 2016, 291, 1514–1528. [Google Scholar] [CrossRef] [PubMed]
- Seldeen, K.L.; Berman, R.N.; Pang, M.; Lasky, G.; Weiss, C.; MacDonald, B.A.; Thiyagarajan, R.; Redae, Y.; Troen, B.R. Vitamin D Insufficiency Reduces Grip Strength, Grip Endurance and Increases Frailty in Aged C57Bl/6J Mice. Nutrients 2020, 12, 3005. [Google Scholar] [CrossRef] [PubMed]
- Ke, C.Y.; Yang, F.L.; Wu, W.T.; Chung, C.H.; Lee, R.P.; Yang, W.T.; Subeq, Y.M.; Liao, K.W. Vitamin D3 Reduces Tissue Damage and Oxidative Stress Caused by Exhaustive Exercise. Int. J. Med. Sci. 2016, 13, 147–153. [Google Scholar] [CrossRef]
- Chen, L.; Yang, R.; Qiao, W.; Zhang, W.; Chen, J.; Mao, L.; Goltzman, D.; Miao, D. 1,25-Dihydroxyvitamin D exerts an antiaging role by activation of Nrf2-antioxidant signaling and inactivation of p16/p53-senescence signaling. Aging Cell 2019, 18, e12951. [Google Scholar] [CrossRef] [PubMed]
- Xiang, Y.; Fu, L.; Xiang, H.X.; Zheng, L.; Tan, Z.X.; Wang, L.X.; Cao, W.; Xu, D.X.; Zhao, H. Correlations among Pulmonary DJ-1, VDR and Nrf-2 in patients with Chronic Obstructive Pulmonary Disease: A Case-control Study. Int. J. Med. Sci. 2021, 18, 2449–2456. [Google Scholar] [CrossRef]
- Mathyssen, C.; Aelbrecht, C.; Serré, J.; Everaerts, S.; Maes, K.; Gayan-Ramirez, G.; Vanaudenaerde, B.; Janssens, W. Local expression profiles of vitamin D-related genes in airways of COPD patients. Respir. Res. 2020, 21, 137. [Google Scholar] [CrossRef]
- Montecinos-Franjola, F.; Ramachandran, R. Imaging Dynamin-Related Protein 1 (Drp1)-Mediated Mitochondrial Fission in Living Cells. Methods Mol. Biol. 2020, 2159, 205–217. [Google Scholar] [CrossRef] [PubMed]
- Zsurka, G.; Peeva, V.; Kotlyar, A.; Kunz, W.S. Is There Still Any Role for Oxidative Stress in Mitochondrial DNA-Dependent Aging? Genes 2018, 9, 175. [Google Scholar] [CrossRef]
- Wang, J.; Aung, L.H.; Prabhakar, B.S.; Li, P. The mitochondrial ubiquitin ligase plays an anti-apoptotic role in cardiomyocytes by regulating mitochondrial fission. J. Cell Mol. Med. 2016, 20, 2278–2288. [Google Scholar] [CrossRef]
- Tengan, C.H.; Moraes, C.T. NO control of mitochondrial function in normal and transformed cells. Biochim. Biophys. Acta Bioenerg. 2017, 1858, 573–581. [Google Scholar] [CrossRef] [PubMed]
- Boyd, C.S.; Cadenas, E. Nitric oxide and cell signaling pathways in mitochondrial-dependent apoptosis. Biol. Chem. 2002, 383, 411–423. [Google Scholar] [CrossRef]
- Parameswaran, N.; Patial, S. Tumor necrosis factor-α signaling in macrophages. Crit. Rev. Eukaryot. Gene Expr. 2010, 20, 87–103. [Google Scholar] [CrossRef] [PubMed]
- Remels, A.H.; Langen, R.C.; Schrauwen, P.; Schaart, G.; Schols, A.M.; Gosker, H.R. Regulation of mitochondrial biogenesis during myogenesis. Mol. Cell Endocrinol. 2010, 315, 113–120. [Google Scholar] [CrossRef]
- Tang, K.; Murano, G.; Wagner, H.; Nogueira, L.; Wagner, P.D.; Tang, A.; Dalton, N.D.; Gu, Y.; Peterson, K.L.; Breen, E.C. Impaired exercise capacity and skeletal muscle function in a mouse model of pulmonary inflammation. J. Appl. Physiol. (1985) 2013, 114, 1340–1350. [Google Scholar] [CrossRef]
- De la Fuente, M.; Miquel, J. An update of the oxidation-inflammation theory of aging: The involvement of the immune system in oxi-inflamm-aging. Curr. Pharm. Des. 2009, 15, 3003–3026. [Google Scholar] [CrossRef]
- Rosa, M.D.; Distefano, G.; Gagliano, C.; Rusciano, D.; Malaguarnera, L. Autophagy in Diabetic Retinopathy. Curr. Neuropharmacol. 2016, 14, 810–825. [Google Scholar] [CrossRef]
- St-Pierre, J.; Drori, S.; Uldry, M.; Silvaggi, J.M.; Rhee, J.; Jäger, S.; Handschin, C.; Zheng, K.; Lin, J.; Yang, W.; et al. Suppression of reactive oxygen species and neurodegeneration by the PGC-1 transcriptional coactivators. Cell 2006, 127, 397–408. [Google Scholar] [CrossRef]
- Salles, J.; Chanet, A.; Giraudet, C.; Patrac, V.; Pierre, P.; Jourdan, M.; Luiking, Y.C.; Verlaan, S.; Migné, C.; Boirie, Y.; et al. 1,25(OH)2-vitamin D3 enhances the stimulating effect of leucine and insulin on protein synthesis rate through Akt/PKB and mTOR mediated pathways in murine C2C12 skeletal myotubes. Mol. Nutr. Food Res. 2013, 57, 2137–2146. [Google Scholar] [CrossRef] [PubMed]
- Sandri, M.; Sandri, C.; Gilbert, A.; Skurk, C.; Calabria, E.; Picard, A.; Walsh, K.; Schiaffino, S.; Lecker, S.H.; Goldberg, A.L. Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. Cell 2004, 117, 399–412. [Google Scholar] [CrossRef]
- Tran, H.; Brunet, A.; Griffith, E.C.; Greenberg, M.E. The many forks in FOXO’s road. Sci. STKE 2003, 2003, RE5. [Google Scholar] [CrossRef] [PubMed]
- Chen, S.; Villalta, S.A.; Agrawal, D.K. FOXO1 Mediates Vitamin D Deficiency-Induced Insulin Resistance in Skeletal Muscle. J. Bone Miner. Res. 2016, 31, 585–595. [Google Scholar] [CrossRef] [PubMed]
- Kitajima, Y.; Yoshioka, K.; Suzuki, N. The ubiquitin-proteasome system in regulation of the skeletal muscle homeostasis and atrophy: From basic science to disorders. J. Physiol. Sci. 2020, 70, 40. [Google Scholar] [CrossRef] [PubMed]
- Saline, M.; Badertscher, L.; Wolter, M.; Lau, R.; Gunnarsson, A.; Jacso, T.; Norris, T.; Ottmann, C.; Snijder, A. AMPK and AKT protein kinases hierarchically phosphorylate the N-terminus of the FOXO1 transcription factor, modulating interactions with 14-3-3 proteins. J. Biol. Chem. 2019, 294, 13106–13116. [Google Scholar] [CrossRef]
- Brenkman, A.B.; van den Broek, N.J.; de Keizer, P.L.; van Gent, D.C.; Burgering, B.M. The DNA damage repair protein Ku70 interacts with FOXO4 to coordinate a conserved cellular stress response. FASEB J. 2010, 24, 4271–4280. [Google Scholar] [CrossRef] [PubMed]
- DeLuca, G.C.; Kimball, S.M.; Kolasinski, J.; Ramagopalan, S.V.; Ebers, G.C. Review: The role of vitamin D in nervous system health and disease. Neuropathol. Appl. Neurobiol. 2013, 39, 458–484. [Google Scholar] [CrossRef]
- Smolders, J.; Menheere, P.; Thewissen, M.; Peelen, E.; Cohen Tervaert, J.W.; Hupperts, R.; Damoiseaux, J. Regulatory T cell function correlates with serum 25-hydroxyvitamin D, but not with 1, 25-dihydroxyvita-min D, parathyroid hormone and calcium levels in patients with relapsing remitting multiple sclerosis. J. Steroid Biochem. Mol. Biol. 2010, 121, 243–246. [Google Scholar] [CrossRef]
- Mahon, B.D.; Gordon, S.A.; Cruz, J.; Cosman, F.; Cantorna, M.T. Cytokine profile in patients with multiple sclerosis following vitamin D supplementation. J. Neuroimmunol. 2003, 134, 128–132. [Google Scholar] [CrossRef] [PubMed]
- Usategui-Martín, R.; De Luis-Román, D.A.; Fernández-Gómez, J.M.; Ruiz-Mambrilla, M.; Pérez-Castrillón, J.L. Vitamin D Receptor (VDR) Gene Polymorphisms Modify the Response to Vitamin D Supplementation: A Systematic Review and Meta-Analysis. Nutrients 2022, 14, 360. [Google Scholar] [CrossRef] [PubMed] [PubMed Central]
Disclaimer/Publisher’s Note: The statements, opinions and data contained in all publications are solely those of the individual author(s) and contributor(s) and not of MDPI and/or the editor(s). MDPI and/or the editor(s) disclaim responsibility for any injury to people or property resulting from any ideas, methods, instructions or products referred to in the content. |
© 2024 by the authors. Licensee MDPI, Basel, Switzerland. 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/).
Share and Cite
Russo, C.; Santangelo, R.; Malaguarnera, L.; Valle, M.S. The “Sunshine Vitamin” and Its Antioxidant Benefits for Enhancing Muscle Function. Nutrients 2024, 16, 2195. https://doi.org/10.3390/nu16142195
Russo C, Santangelo R, Malaguarnera L, Valle MS. The “Sunshine Vitamin” and Its Antioxidant Benefits for Enhancing Muscle Function. Nutrients. 2024; 16(14):2195. https://doi.org/10.3390/nu16142195
Chicago/Turabian StyleRusso, Cristina, Rosa Santangelo, Lucia Malaguarnera, and Maria Stella Valle. 2024. "The “Sunshine Vitamin” and Its Antioxidant Benefits for Enhancing Muscle Function" Nutrients 16, no. 14: 2195. https://doi.org/10.3390/nu16142195