{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T04:35:12Z","timestamp":1791520512251,"version":"4.3.4"},"reference-count":171,"publisher":"MDPI AG","issue":"23","license":[{"start":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T00:00:00Z","timestamp":1701388800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Department of Nutritional Sciences and the College of Agriculture, Health, and Natural Resources at the University of Connecticut"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Calcium research, since its pivotal discovery in the early 1800s through the heating of limestone, has led to the identification of its multi-functional roles. These include its functions as a reducing agent in chemical processes, structural properties in shells and bones, and significant role in cells relating to this review: cellular signaling. Calcium signaling involves the movement of calcium ions within or between cells, which can affect the electrochemical gradients between intra- and extracellular membranes, ligand binding, enzyme activity, and other mechanisms that determine cell fate. Calcium signaling in muscle, as elucidated by the sliding filament model, plays a significant role in muscle contraction. However, as organisms age, alterations occur within muscle tissue. These changes include sarcopenia, loss of neuromuscular junctions, and changes in mineral concentration, all of which have implications for calcium\u2019s role. Additionally, a field of study that has gained recent attention, cellular senescence, is associated with aging and disturbed calcium homeostasis, and is thought to affect sarcopenia progression. Changes seen in calcium upon aging may also be influenced by its crosstalk with other minerals such as iron and zinc. This review investigates the role of calcium signaling in aging muscle and cellular senescence. We also aim to elucidate the interactions among calcium, iron, and zinc across various cells and conditions, ultimately deepening our understanding of calcium signaling in muscle aging.<\/jats:p>","DOI":"10.3390\/ijms242317034","type":"journal-article","created":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T08:36:59Z","timestamp":1701419819000},"page":"17034","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":81,"title":["Calcium\u2019s Role and Signaling in Aging Muscle, Cellular Senescence, and Mineral Interactions"],"prefix":"10.3390","volume":"24","author":[{"given":"Kristofer","family":"Terrell","sequence":"first","affiliation":[{"name":"Department of Nutritional Sciences, College of Agriculture, Health, and Natural Resources, University of Connecticut, Storrs, CT 06269, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suyun","family":"Choi","sequence":"additional","affiliation":[{"name":"Department of Nutritional Sciences, College of Agriculture, Health, and Natural Resources, University of Connecticut, Storrs, CT 06269, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6316-7068","authenticated-orcid":false,"given":"Sangyong","family":"Choi","sequence":"additional","affiliation":[{"name":"Department of Nutritional Sciences, College of Agriculture, Health, and Natural Resources, University of Connecticut, Storrs, CT 06269, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,12,1]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1007\/s12603-012-0434-0","article-title":"Mortality as An Adverse Outcome of Sarcopenia","volume":"17","author":"Arroyo","year":"2013","journal-title":"J. Nutr. Health Aging"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1038\/s41586-022-05535-x","article-title":"Senescence atlas reveals an aged-like inflamed niche that blunts muscle regeneration","volume":"613","author":"Moiseeva","year":"2023","journal-title":"Nature"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1557988319841934","DOI":"10.1177\/1557988319841934","article-title":"The Relation of Inflammaging with Skeletal Muscle Properties in Elderly Men","volume":"13","author":"Dziubek","year":"2019","journal-title":"Am. J. Mens. Health"},{"key":"ref_4","first-page":"e14607","article-title":"Mechanisms of muscle insulin resistance and the cross-talk with liver and adipose tissue","volume":"8","author":"Rosa","year":"2020","journal-title":"Physiol. Rep."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1246","DOI":"10.1038\/s41591-018-0092-9","article-title":"Senolytics improve physical function and increase lifespan in old age","volume":"24","author":"Xu","year":"2018","journal-title":"Nat. Med."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"601189","DOI":"10.3389\/fphys.2020.601189","article-title":"Senescence Is Associated With Elevated Intracellular Resting [Ca2+] in Mice Skeletal Muscle Fibers. An in vivo Study","volume":"11","author":"Mijares","year":"2021","journal-title":"Front. Physiol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"102701","DOI":"10.1016\/j.ceca.2023.102701","article-title":"Regulation and Role of Calcium in Cellular Senescence","volume":"110","author":"Martin","year":"2023","journal-title":"Cell Calcium"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1093\/oxfordjournals.jbchem.a128628","article-title":"Troponin as the Ca++-receptive protein in the contractile system","volume":"62","author":"Seturo","year":"1967","journal-title":"J. Biochem."},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Kami\u0144ski, M., Kr\u0119gielska-Naro\u017cna, M., and Bogda\u0144ski, P. (2020). Determination of the Popularity of Dietary Supplements Using Google Search Rankings. Nutrients, 12.","DOI":"10.3390\/nu12040908"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"3184","DOI":"10.3390\/nu5083184","article-title":"Iron and Zinc Nutrition in the Economically-Developed World: A Review","volume":"5","author":"Lim","year":"2013","journal-title":"Nutrients"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1038\/s41467-022-28060-x","article-title":"The mouse metallomic landscape of aging and metabolism","volume":"13","author":"Morel","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1044","DOI":"10.1111\/j.1600-0854.2008.00717.x","article-title":"Sarcoplasmic Reticulum: An Organized Patchwork of Specialized Domains","volume":"9","author":"Rossi","year":"2008","journal-title":"Traffic"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.yjmcc.2018.09.008","article-title":"Phospholamban regulates nuclear Ca2+ stores and inositol 1,4,5-trisphosphate mediated nuclear Ca2+ cycling in cardiomyocytes","volume":"123","author":"Chen","year":"2018","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"20849","DOI":"10.1074\/jbc.R116.735894","article-title":"Why Calcium? How Calcium Became the Best Communicator","volume":"291","author":"Carafoli","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Lanner, J.T., Georgiou, D.K., Joshi, A.D., and Hamilton, S.L. (2010). Ryanodine Receptors: Structure, Expression, Molecular Details, and Function in Calcium Release. Cold Spring Harb. Perspect. Biol., 2.","DOI":"10.1101\/cshperspect.a003996"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1152\/physrev.00035.2006","article-title":"Inositol Trisphosphate Receptor Ca2+ Release Channels","volume":"87","author":"Foskett","year":"2007","journal-title":"Physiol. Rev."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"24","DOI":"10.2174\/156652413804486214","article-title":"Functions of S100 Proteins","volume":"13","author":"Donato","year":"2013","journal-title":"Curr. Mol. Med."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"2017","DOI":"10.1016\/j.bbamcr.2016.04.021","article-title":"Tracking and localization of calmodulin in live cells","volume":"1863","author":"Johnson","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/j.bbrc.2015.02.004","article-title":"Ca2+ homeostasis and endoplasmic reticulum (ER) stress: An integrated view of calcium signaling","volume":"460","author":"Krebs","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"e2302837120","DOI":"10.1073\/pnas.2302837120","article-title":"Activation of skeletal muscle is controlled by a dual-filament mechano-sensing mechanism","volume":"120","author":"Brunello","year":"2023","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1038\/s41467-019-14008-1","article-title":"Cardiac muscle thin filament structures reveal calcium regulatory mechanism","volume":"11","author":"Yamada","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"985","DOI":"10.1016\/S0006-3495(99)76949-3","article-title":"Tropomyosin positions in regulated thin filaments revealed by cryoelectron microscopy","volume":"77","author":"Xu","year":"1999","journal-title":"Biophys. J."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Pierantozzi, E., Szentesi, P., Paolini, C., Dienes, B., Fodor, J., Ol\u00e1h, T., Colombini, B., Rassier, D.E., Rubino, E.M., and Lange, S. (2022). Impaired Intracellular Ca2+ Dynamics, M-Band and Sarcomere Fragility in Skeletal Muscles of Obscurin KO Mice. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23031319"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"C16","DOI":"10.1152\/ajpcell.00098.2016","article-title":"Exercise-induced alterations and loss of sarcomeric M-line organization in the diaphragm muscle of obscurin knockout mice","volume":"312","author":"Randazzo","year":"2017","journal-title":"Am. J. Physiol.-Cell Physiol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/bs.ircmb.2019.12.007","article-title":"Sarcoplasmic reticulum and calcium signaling in muscle cells: Homeostasis and disease","volume":"350","author":"Parra","year":"2020","journal-title":"Int. Rev. Cell Mol. Biol."},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Yoshida, T., and Delafontaine, P. (2020). Mechanisms of IGF-1-Mediated Regulation of Skeletal Muscle Hypertrophy and Atrophy. Cells, 9.","DOI":"10.3390\/cells9091970"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.ceca.2016.02.005","article-title":"Calcium signaling in skeletal muscle development, maintenance and regeneration","volume":"59","author":"Tu","year":"2016","journal-title":"Cell Calcium"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1452","DOI":"10.1002\/jcp.24298","article-title":"IGF-1 induces IP3-dependent calcium signal involved in the regulation of myostatin gene expression mediated by NFAT during myoblast differentiation","volume":"228","author":"Flores","year":"2013","journal-title":"J. Cell. Physiol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/j.cell.2022.11.001","article-title":"Hallmarks of aging: An expanding universe","volume":"186","author":"Blasco","year":"2023","journal-title":"Cell"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1042\/CS20140051","article-title":"Cellular aging of skeletal muscle: Telomeric and free radical evidence that physical inactivity is responsible and not age","volume":"127","author":"Venturelli","year":"2014","journal-title":"Clin. Sci."},{"key":"ref_31","unstructured":"Bruce, A., Alexander, J., Julian, L., Martin, R., and Keith, R. (2022). Walter, Peter, Genesis, Modulation, and Regeneration of Skeletal Muscle, Molecular Biology of the Cell, Garland Science. [4th ed.]."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"101883","DOI":"10.1016\/j.arr.2023.101883","article-title":"An elusive consensus definition of sarcopenia impedes research and clinical treatment: A narrative review","volume":"86","author":"Coletta","year":"2023","journal-title":"Ageing Res. Rev."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1093\/gerona\/61.10.1059","article-title":"The Loss of Skeletal Muscle Strength, Mass, and Quality in Older Adults: The Health, Aging and Body Composition Study","volume":"61","author":"Goodpaster","year":"2006","journal-title":"J. Gerontol. Ser. A Biol. Sci. Med. Sci."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"2396","DOI":"10.1016\/j.celrep.2017.05.054","article-title":"Single Muscle Fiber Proteomics Reveals Fiber-Type-Specific Features of Human Muscle Aging","volume":"19","author":"Murgia","year":"2017","journal-title":"Cell Rep."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"e13039","DOI":"10.1111\/acel.13039","article-title":"Metformin blunts muscle hypertrophy in response to progressive resistance exercise training in older adults: A randomized, double-blind, placebo-controlled, multicenter trial: The MASTERS trial","volume":"18","author":"Walton","year":"2019","journal-title":"Aging Cell"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"19551","DOI":"10.1038\/s41598-020-75250-y","article-title":"Prevalence and risk factors of primary sarcopenia in community-dwelling outpatient elderly: A cross-sectional study","volume":"10","author":"Therakomen","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"756626","DOI":"10.3389\/fphys.2021.756626","article-title":"Microbiopsy Sampling for Examining Age-Related Differences in Skeletal Muscle Fiber Morphology and Composition","volume":"12","author":"Hester","year":"2022","journal-title":"Front. Physiol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"112120","DOI":"10.1016\/j.exger.2023.112120","article-title":"FGF19 and muscle architecture in older patients","volume":"174","author":"Bres","year":"2023","journal-title":"Exp. Gerontol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"3333","DOI":"10.1021\/acs.jproteome.8b00093","article-title":"Single Muscle Fiber Proteomics Reveals Distinct Protein Changes in Slow and Fast Fibers during Muscle Atrophy","volume":"17","author":"Lang","year":"2018","journal-title":"J. Proteome Res."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1016\/j.stem.2018.12.014","article-title":"Aging Disrupts Muscle Stem Cell Function by Impairing Matricellular WISP1 Secretion from Fibro-Adipogenic Progenitors","volume":"24","author":"Lukjanenko","year":"2019","journal-title":"Cell Stem Cell"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1582","DOI":"10.1002\/jcsm.12768","article-title":"Muscle mitochondrial catalase expression prevents neuromuscular junction disruption, atrophy, and weakness in a mouse model of accelerated sarcopenia","volume":"12","author":"Xu","year":"2021","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Kim, K.H., Chung, Y., Huh, J., Park, D.J., Cho, Y., Oh, Y., Jeong, H., Yoon, J., Kang, J., and Shin, H. (2022). Gut microbiota of the young ameliorates physical fitness of the aged in mice. Microbiome, 10.","DOI":"10.1186\/s40168-022-01386-w"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1178","DOI":"10.1001\/jama.2019.13771","article-title":"Bhupathiraju, Shilpa. Trends in Dietary Carbohydrate, Protein, and Fat Intake and Diet Quality Among US Adults, 1999\u20132016","volume":"322","author":"Shan","year":"2019","journal-title":"JAMA"},{"key":"ref_44","first-page":"208","article-title":"The Neuromuscular Junction: Aging at the Crossroad between Nerves and Muscle","volume":"6","author":"Studenski","year":"2014","journal-title":"Front. Aging Neurosci."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"253","DOI":"10.12968\/hmed.2018.79.5.253","article-title":"Osteosarcopenia","volume":"79","author":"Paintin","year":"2018","journal-title":"Br. J. Hosp. Med."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1634","DOI":"10.1002\/jbmr.4027","article-title":"Effects of High-Intensity Resistance Training on Osteopenia and Sarcopenia Parameters in Older Men with Osteosarcopenia\u2014One-Year Results of the Randomized Controlled Franconian Osteopenia and Sarcopenia Trial (FrOST)","volume":"35","author":"Kemmler","year":"2020","journal-title":"J. Bone Min. Res."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1007\/s00223-019-00581-6","article-title":"A Vitamin D, Calcium and Leucine-Enriched Whey Protein Nutritional Supplement Improves Measures of Bone Health in Sarcopenic Non-Malnourished Older Adults: The PROVIDE Study","volume":"105","author":"Hill","year":"2019","journal-title":"Calcif. Tissue Int."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"101200","DOI":"10.1016\/j.arr.2020.101200","article-title":"Sarcopenia\u2014Molecular mechanisms and open questions","volume":"65","author":"Wiedmer","year":"2021","journal-title":"Ageing Res. Rev."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-017-00629-x","article-title":"The Ca2+ influx through the mammalian skeletal muscle dihydropyridine receptor is irrelevant for muscle performance","volume":"8","author":"Dayal","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Liu, Y., Sugiura, Y., Chen, F., Lee, K., Ye, Q., and Lin, W. (2019). Blocking skeletal muscle DHPRs\/Ryr1 prevents neuromuscular synapse loss in mutant mice deficient in type III Neuregulin 1 (CRD-Nrg1). PLoS Genet., 15.","DOI":"10.1371\/journal.pgen.1007857"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1111\/j.1474-9726.2011.00706.x","article-title":"Store-operated calcium entry remains fully functional in aged mouse skeletal muscle despite a decline in STIM1 protein expression","volume":"10","author":"Edwards","year":"2011","journal-title":"Aging Cell"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1083\/jcb.200604166","article-title":"Muscle Aging Is Associated with Compromised Ca2+ Spark Signaling and Segregated Intracellular Ca2+ Release","volume":"174","author":"Weisleder","year":"2006","journal-title":"J. Cell Biol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"24403","DOI":"10.1073\/pnas.2008032117","article-title":"ORAI1 and ORAI2 modulate murine neutrophil calcium signaling, cellular activation, and host defense","volume":"117","author":"Grimes","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1111\/nyas.12938","article-title":"Diseases caused by mutations in ORAI1 and STIM1","volume":"1356","author":"Lacruz","year":"2015","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"868-24","DOI":"10.1096\/fasebj.2019.33.1_supplement.868.24","article-title":"MG29 Interacts with Bin-1 to Maintain T-Tubule Structure in Skeletal Muscle Physiology and Regeneration","volume":"33","author":"Yi","year":"2019","journal-title":"FASEB J."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1016\/j.nbd.2005.07.012","article-title":"Fiber type-related changes in rat skeletal muscle calcium homeostasis during aging and restoration by growth hormone","volume":"21","author":"Fraysse","year":"2006","journal-title":"Neurobiol. Dis."},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Kim, Y., Hong, K., Han, K., Park, Y.C., Park, J., Kim, K., and Kim, B.T. (2020). Longitudinal Observation of Muscle Mass over 10 Years According to Serum Calcium Levels and Calcium Intake among Korean Adults Aged 50 and Older: The Korean Genome and Epidemiology Study. Nutrients, 12.","DOI":"10.3390\/nu12092856"},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Asghar, M.Y., and T\u00f6rnquist, K. (2020). Transient Receptor Potential Canonical (TRPC) Channels as Modulators of Migration and Invasion. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21051739"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1016\/0014-4827(61)90192-6","article-title":"The serial cultivation of human diploid cell strains","volume":"25","author":"Hayflick","year":"1961","journal-title":"Exp. Cell Res."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1038\/s43587-022-00250-8","article-title":"Characterization of cellular senescence in aging skeletal muscle","volume":"2","author":"Zhang","year":"2022","journal-title":"Nat. Aging"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"5093","DOI":"10.1073\/pnas.081061898","article-title":"Influences of aging and caloric restriction on the transcriptional profile of transcriptional profile of skeletal muscle from rhesus monkeys","volume":"98","author":"Tsuyoshi","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_62","first-page":"9393","article-title":"Single nuclei profiling identifies cell specific markers of skeletal muscle aging, frailty, and senescence","volume":"14","author":"Perez","year":"2022","journal-title":"Aging"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"7018","DOI":"10.1096\/fj.202000111RR","article-title":"In vivo analysis of \u03b3H2AX+ cells in skeletal muscle from aged and obese humans","volume":"34","author":"Dungan","year":"2020","journal-title":"FASEB J."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1016\/j.devcel.2014.11.012","article-title":"An Essential Role for Senescent Cells in Optimal Wound Healing through Secretion of PDGF-AA","volume":"31","author":"Demaria","year":"2014","journal-title":"Dev. Cell"},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Prieto, L., Graves, S., and Baker, D. (2020). Insights from In Vivo Studies of Cellular Senescence. Cells, 9.","DOI":"10.3390\/cells9040954"},{"key":"ref_66","doi-asserted-by":"crossref","unstructured":"Raynard, C., Tessier, N., Huna, A., Warnier, M., Flaman, J., Van Coppenolle, F., Ducreux, S., Martin, N., and Bernard, D. (2022). Expression of the Calcium-Binding Protein CALB1 Is Induced and Controls Intracellular Ca2+ Levels in Senescent Cells. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23169376"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1038\/s41467-021-20993-z","article-title":"Calcium channel ITPR2 and mitochondria\u2013ER contacts promote cellular senescence and aging","volume":"12","author":"Ziegler","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1007\/s11427-016-5089-3","article-title":"Mitochondrial Ca2+ uptake in skeletal muscle health and disease","volume":"59","author":"Zhou","year":"2016","journal-title":"Sci. China Life Sci."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"2349","DOI":"10.1152\/physrev.00058.2021","article-title":"Mitochondria in Health, Disease, and Aging.","volume":"103","author":"Harrington","year":"2023","journal-title":"Physiol. Rev."},{"key":"ref_70","doi-asserted-by":"crossref","unstructured":"Abrisch, R.G., Gumbin, S.C., Wisniewski, B.T., Lackner, L.L., and Voeltz, G.K. (2020). Fission and fusion machineries converge at ER contact sites to regulate mitochondrial morphology. J. Cell Biol., 219.","DOI":"10.1083\/jcb.201911122"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"e158447","DOI":"10.1172\/JCI158447","article-title":"Mitochondrial dysfunction in cell senescence and aging","volume":"132","author":"Miwa","year":"2022","journal-title":"J. Clin. Investig."},{"key":"ref_72","first-page":"3367","article-title":"LETM1 is required for mitochondrial homeostasis and cellular viability","volume":"19","author":"Li","year":"2019","journal-title":"Mol. Med. Rep."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1038\/s41467-017-02638-2","article-title":"Sequential forward and reverse transport of the Na+ Ca2+ exchanger generates Ca2+ oscillations within mitochondria","volume":"9","author":"Samanta","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.yjmcc.2014.10.013","article-title":"The mitochondrial calcium uniporter: Mice can live and die without it","volume":"78","author":"Harrington","year":"2015","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Young, M.P., Schug, Z.T., Booth, D.M., Yule, D.I., Mikoshiba, K., Hajnoczky, G., and Joseph, S.K. (2022). Metabolic adaptation to the chronic loss of Ca2+ signaling induced by KO of IP3 receptors or the mitochondrial Ca2+ uniporter. J. Biol. Chem., 298.","DOI":"10.1016\/j.jbc.2021.101436"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.molcel.2012.09.025","article-title":"Physiological Roles of Mitochondrial Reactive Oxygen Species","volume":"48","author":"Sena","year":"2012","journal-title":"Mol. Cell"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"110444","DOI":"10.1016\/j.celrep.2022.110444","article-title":"Age-associated decline of MondoA drives cellular senescence through impaired autophagy and mitochondrial homeostasis","volume":"38","author":"Minami","year":"2022","journal-title":"Cell Rep."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"1274","DOI":"10.1016\/j.celrep.2019.09.063","article-title":"Dysregulation of Mitochondrial Ca2+ Uptake and Sarcolemma Repair Underlie Muscle Weakness and Wasting in Patients and Mice Lacking MICU1","volume":"29","author":"Debattisti","year":"2019","journal-title":"Cell Rep."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1038\/ng.2851","article-title":"Loss-of-function mutations in MICU1 cause a brain and muscle disorder linked to primary alterations in mitochondrial calcium signaling","volume":"46","author":"Logan","year":"2014","journal-title":"Nat. Genet."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/j.autrev.2014.11.008","article-title":"Zinc and its role in immunity and inflammation","volume":"14","author":"Bonaventura","year":"2015","journal-title":"Autoimmun. Rev."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1093\/jn\/103.8.1175","article-title":"Effects of dietary zinc on zinc enzymes in the rat","volume":"103","author":"Huber","year":"1973","journal-title":"J. Nutr."},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Hern\u00e1ndez-Camacho, J.D., Vicente-Garc\u00eda, C., Parsons, D.S., and Navas-Enamorado, I. (2020). Zinc at the crossroads of exercise and proteostasis. Redox Biol., 35.","DOI":"10.1016\/j.redox.2020.101529"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"e301","DOI":"10.1002\/hsr2.301","article-title":"The effect of zinc supplementation on fatigue among elderly community dwellers: A parallel clinical trial","volume":"4","author":"Afzali","year":"2021","journal-title":"Health Sci. Rep."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1089\/152308603770310158","article-title":"Iron Accumulation During Cellular Senescence in Human Fibroblasts In Vitro","volume":"5","author":"Killilea","year":"2003","journal-title":"Antioxid. Redox Signal."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"C1342","DOI":"10.1152\/ajpcell.00061.2008","article-title":"Zinc-induced G2\/M blockage is P53 and P21 dependent in normal human bronchial epithelial cells","volume":"294","author":"Wong","year":"2008","journal-title":"Am. J. Physiol.-Cell Physiol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/j.freeradbiomed.2017.03.032","article-title":"Zinc regulates Nox1 expression through a NF-\u03baB and mitochondrial ROS dependent mechanism to induce senescence of vascular smooth muscle cells","volume":"108","author":"Salazar","year":"2017","journal-title":"Free Radic. Biol. Med."},{"key":"ref_87","doi-asserted-by":"crossref","unstructured":"Dabravolski, S.A., Sadykhov, N.K., Kartuesov, A.G., Borisov, E.E., Sukhorukov, V.N., and Orekhov, A.N. (2022). Interplay between Zn2+ Homeostasis and Mitochondrial Functions in Cardiovascular Diseases and Heart Ageing. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23136890"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"83","DOI":"10.3389\/fphar.2014.00083","article-title":"Iron deficiency in the elderly population, revisited in the hepcidin era","volume":"5","author":"Busti","year":"2014","journal-title":"Front. Pharmacol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1093\/gerona\/glac139","article-title":"Age-Related Changes in Skeletal Muscle Iron Homeostasis","volume":"78","author":"Alves","year":"2023","journal-title":"J. Gerontol. Ser. A Biol. Sci. Med. Sci."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1002\/jcsm.12685","article-title":"Iron accumulation in skeletal muscles of old mice is associated with impaired regeneration after ischaemia\u2013reperfusion damage","volume":"12","author":"Alves","year":"2021","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"151","DOI":"10.7150\/ijbs.53126","article-title":"Ferroptosis in a sarcopenia model of senescence accelerated mouse prone 8 (SAMP8)","volume":"17","author":"Huang","year":"2021","journal-title":"Int. J. Biol. Sci."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1146\/annurev-med-043021-032816","article-title":"Hepcidin and Iron in Health and Disease","volume":"74","author":"Nemeth","year":"2023","journal-title":"Annu. Rev. Med."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.redox.2017.08.015","article-title":"Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis","volume":"14","author":"Masaldan","year":"2018","journal-title":"Redox Biol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1111\/j.1474-9726.2008.00418.x","article-title":"Mitochondrial iron accumulation with age and functional consequences","volume":"7","author":"Seo","year":"2008","journal-title":"Aging Cell"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1198","DOI":"10.1039\/C4MT00064A","article-title":"Zinc\u2019ing sensibly: Controlling zinc homeostasis at the transcriptional level","volume":"6","author":"Choi","year":"2014","journal-title":"Metallomics"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1007\/s00424-013-1295-z","article-title":"Contribution of calcium-conducting channels to the transport of zinc ions","volume":"466","author":"Bouron","year":"2014","journal-title":"Pflug. Arch. Eur. J. Physiol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1111\/j.1469-7793.2000.00039.x","article-title":"Zn2+ current is mediated by voltage-gated Ca2+ channels and enhanced by extracellular acidity in mouse cortical neurones","volume":"528","author":"Kerchner","year":"2000","journal-title":"J. Physiol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"2473","DOI":"10.1074\/jbc.270.6.2473","article-title":"Excitation-Transcription Coupling Mediated by Zinc Influx through Voltage-dependent Calcium Channels (\u2217)","volume":"270","author":"Atar","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"9361","DOI":"10.1074\/jbc.M508542200","article-title":"The Zn2+-transporting pathways in pancreatic beta-cells: A role for the L-type voltage-gated Ca2+ channel","volume":"281","author":"Gyulkhandanyan","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"Yamasaki, S., Hasegawa, A., Hojyo, S., Ohashi, W., Fukada, T., Nishida, K., and Hirano, T. (2012). A Novel Role of the L-Type Calcium Channel [alpha].sub.1D Subunit as a Gatekeeper for Intracellular Zinc Signaling: Zinc Wave. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0039654"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1085\/jgp.20028740","article-title":"TRPM7 Provides an Ion Channel Mechanism for Cellular Entry of Trace Metal Ions","volume":"121","author":"Hermosura","year":"2003","journal-title":"J. Gen. Physiol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1016\/j.ceca.2006.10.003","article-title":"Molecular determinants of permeation through the cation channel TRPM6","volume":"41","author":"Topala","year":"2007","journal-title":"Cell Calcium"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1085\/jgp.200609502","article-title":"Functional Characterization of Homo- and Heteromeric Channel Kinases TRPM6 and TRPM7","volume":"127","author":"Li","year":"2006","journal-title":"J. Gen. Physiol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"e4320","DOI":"10.1002\/pro.4320","article-title":"The crystal structure of TRPM2 MHR1\/2 domain reveals a conserved Zn2+-binding domain essential for structural integrity and channel activity","volume":"31","author":"Sander","year":"2022","journal-title":"Protein Sci."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1042\/BJ20140747","article-title":"TRPM2-mediated intracellular Zn2+ release triggers pancreatic \u03b2-cell death","volume":"466","author":"Manna","year":"2015","journal-title":"Biochem. J."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"11106","DOI":"10.1074\/jbc.M400005200","article-title":"Inhibitory Mechanism of Store-operated Ca2+ Channels by Zinc","volume":"279","author":"Gore","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1096\/fj.201700227RRR","article-title":"Selective inhibitory effects of zinc on cell proliferation in esophageal squamous cell carcinoma through Orai1","volume":"32","author":"Choi","year":"2018","journal-title":"FASEB J."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1085\/jgp.51.3.427","article-title":"Effects of Potentiators of Muscular Contraction on Binding of Cations by Sarcoplasmic Reticulum","volume":"51","author":"Carvalho","year":"1968","journal-title":"J. Gen. Physiol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1007\/BF02785313","article-title":"Interaction between zinc and calcium in skeletal muscle in young growing rats","volume":"38","author":"Rossowska","year":"1993","journal-title":"Biol. Trace Elem. Res."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1007\/BF01929351","article-title":"Zinc ions block the intracellular calcium release induced by caffeine in guinea-pig taenia caeci","volume":"51","author":"Nasu","year":"1995","journal-title":"Experientia"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1042\/BST20140285","article-title":"Examining a new role for zinc in regulating calcium release in cardiac muscle","volume":"43","author":"Pitt","year":"2015","journal-title":"Biochem. Soc. Trans."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1159\/000047795","article-title":"Inhibition of ryanodine binding to sarcoplasmic reticulum vesicles of cardiac muscle by Zn2+ ions","volume":"11","author":"Wang","year":"2001","journal-title":"Cell. Physiol. Biochem."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"17599","DOI":"10.1074\/jbc.M115.661280","article-title":"Intracellular Zinc Modulates Cardiac Ryanodine Receptor-mediated Calcium Release","volume":"290","author":"Woodier","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"13361","DOI":"10.1074\/jbc.M117.781708","article-title":"Dysregulated Zn2+ homeostasis impairs cardiac type-2 ryanodine receptor and mitsugumin 23 functions, leading to sarcoplasmic reticulum Ca2+ leakage","volume":"292","author":"Robertson","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"e202213206","DOI":"10.1085\/jgp.202213206","article-title":"The role of Zn2+ in shaping intracellular Ca2+ dynamics in the heart","volume":"155","author":"Dorward","year":"2023","journal-title":"J. Gen. Physiol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1006\/bbrc.1993.1668","article-title":"Human Liver Calreticulin: Characterization and Zn2+-Dependent Interaction with Phenyl-Sepharose","volume":"193","author":"Heilmann","year":"1993","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1016\/j.bbagen.2006.02.003","article-title":"The calcium- and zinc-responsive regions of calreticulin reside strictly in the N-\/C-domain","volume":"1760","author":"Tan","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"1922","DOI":"10.1182\/bloodadvances.2020002402","article-title":"Zinc-dependent multimerization of mutant calreticulin is required for MPL binding and MPN pathogenesis","volume":"5","author":"Rivera","year":"2021","journal-title":"Blood Adv."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1006\/bbrc.1995.1504","article-title":"Zn2+ Binding to Cardiac Calsequestrin","volume":"209","author":"Baksh","year":"1995","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1016\/0006-291X(92)90797-O","article-title":"Low-affinity Ca2+-binding sites versus Zn2+-binding sites in histidine-rich Ca2+-binding protein of skeletal muscle sarcoplasmic reticulum","volume":"186","author":"Picello","year":"1992","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1002\/cbf.3168","article-title":"Reduced expressions of calmodulin genes and protein and reduced ability of calmodulin to activate plasma membrane Ca2+-ATPase in the brain of protein undernourished rats: Modulatory roles of selenium and zinc supplementation","volume":"34","author":"Adebayo","year":"2016","journal-title":"Cell Biochem. Funct."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"1138","DOI":"10.1016\/0006-291X(83)90681-2","article-title":"Zinc ion binding to human brain calcium binding proteins, Calmodulin and S100b protein","volume":"114","author":"Baudier","year":"1983","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1002\/ajh.2830070107","article-title":"Zinc inhibition of calmodulin: A proposed molecular mechanism of zinc action on cellular functions","volume":"7","author":"Brewer","year":"1979","journal-title":"Am. J. Hematol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1385\/BTER:76:3:229","article-title":"Effect of Zinc on Cellular Levels of Calmodulin and Cyclic Adenosine Monophosphate in the Adipocyte","volume":"76","author":"Lin","year":"2000","journal-title":"Biol. Trace Elem. Res."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1111\/j.1365-2133.1993.tb11847.x","article-title":"Reciprocity between tissue calmodulin and cAMP levels: Modulation by excess zinc","volume":"129","author":"Heng","year":"1993","journal-title":"Br. J. Dermatol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1111\/j.1471-4159.1991.tb03791.x","article-title":"Effect of Zinc on Calmodulin-Stimulated Protein Kinase II and Protein Phosphorylation in Rat Cerebral Cortex","volume":"57","author":"Weinberger","year":"1991","journal-title":"J. Neurochem."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"8192","DOI":"10.1016\/S0021-9258(19)83895-4","article-title":"Ions binding to S100 proteins. I. Calcium- and zinc-binding properties of bovine brain S100 alpha alpha, S100a (alpha beta), and S100b (beta beta) protein: Zn2+ regulates Ca2+ binding on S100b protein","volume":"261","author":"Baudier","year":"1986","journal-title":"J. Biol. Chem."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1111\/brv.12585","article-title":"The Zn2+ and Ca2+-binding S100B and S100A1 proteins: Beyond the myths","volume":"95","author":"Baudier","year":"2020","journal-title":"Biol. Rev. Camb. Philos. Soc."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1695","DOI":"10.1021\/bi982483d","article-title":"Zinc-Binding Site of an S100 Protein Revealed. Two Crystal Structures of Ca2+-Bound Human Psoriasin (S100A7) in the Zn2+-Loaded and Zn2+-Free States","volume":"38","author":"Brodersen","year":"1999","journal-title":"Biochemistry"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1007\/s00726-010-0540-4","article-title":"The role of zinc in the S100 proteins: Insights from the X-ray structures","volume":"41","author":"Moroz","year":"2011","journal-title":"Amino Acids"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"1372","DOI":"10.1002\/cbic.201900623","article-title":"Calcium Regulates S100A12 Zinc Sequestration by Limiting Structural Variations","volume":"21","author":"Wang","year":"2020","journal-title":"ChemBioChem A Eur. J. Chem. Biol."},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Baksheeva, V.E., Tsvetkov, P.O., Zalevsky, A.O., Vladimirov, V.I., Gorokhovets, N.V., Zinchenko, D.V., Permyakov, S.E., Devred, F., and Zernii, E.Y. (2022). Zinc Modulation of Neuronal Calcium Sensor Proteins: Three Modes of Interaction with Different Structural Outcomes. Biomolecules, 12.","DOI":"10.3390\/biom12070956"},{"key":"ref_133","doi-asserted-by":"crossref","unstructured":"Baksheeva, V.E., Baldin, A.V., Zalevsky, A.O., Nazipova, A.A., Kazakov, A.S., Vladimirov, V.I., Gorokhovets, N.V., Devred, F., Philippov, P.P., and Bazhin, A.V. (2021). Disulfide Dimerization of Neuronal Calcium Sensor-1: Implications for Zinc and Redox Signaling. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms222212602"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"459","DOI":"10.3389\/fnmol.2018.00459","article-title":"Functional Status of Neuronal Calcium Sensor-1 Is Modulated by Zinc Binding","volume":"11","author":"Tsvetkov","year":"2018","journal-title":"Front. Mol. Neurosci."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1021\/pr025553i","article-title":"Recoverin Is a Zinc-Binding Protein","volume":"2","author":"Permyakov","year":"2003","journal-title":"J. Proteome Res."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.yjmcc.2020.12.002","article-title":"Downregulation of the zinc transporter SLC39A13 (ZIP13) is responsible for the activation of CaMKII at reperfusion and leads to myocardial ischemia\/reperfusion injury in mouse hearts","volume":"152","author":"Wang","year":"2021","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"1145","DOI":"10.1016\/j.bbrc.2004.08.211","article-title":"A role for ZnT-1 in regulating cellular cation influx","volume":"323","author":"Segal","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"32434","DOI":"10.1074\/jbc.M109.058842","article-title":"Molecular Basis for Zinc Transporter 1 Action as an Endogenous Inhibitor of L-type Calcium Channels","volume":"284","author":"Levy","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"102505","DOI":"10.1016\/j.ceca.2021.102505","article-title":"ZnT1 is a neuronal Zn2+\/Ca2+ exchanger","volume":"101","author":"Gottesman","year":"2022","journal-title":"Cell Calcium"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1024\/0300-9831\/a000036","article-title":"Calcium and Iron Absorption\u2014Mechanisms and Public Health Relevance","volume":"80","year":"2010","journal-title":"Int. J. Vitam. Nutr. Res."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/j.bbrc.2010.02.025","article-title":"Interaction of calcium with the human divalent metal-ion transporter-1","volume":"393","author":"Shawki","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1080\/15216540701222906","article-title":"Calcium, iron and neuronal function","volume":"59","author":"Hidalgo","year":"2007","journal-title":"IUBMB Life"},{"key":"ref_143","first-page":"14","article-title":"Modulation of iron metabolism by iron chelation regulates intracellular calcium and increases sensitivity to doxorubicin","volume":"16","author":"Yalcintepe","year":"2016","journal-title":"Bosn. J. Basic. Med. Sci."},{"key":"ref_144","doi-asserted-by":"crossref","unstructured":"Phoaubon, S., Lertsuwan, K., Teerapornpuntakit, J., and Charoenphandhu, N. (2021). Hepcidin induces intestinal calcium uptake while suppressing iron uptake in Caco-2 cells. PLoS ONE, 16.","DOI":"10.1371\/journal.pone.0258433"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1007\/s00109-005-0029-x","article-title":"Role of L-type Ca2+ channels in iron transport and iron-overload cardiomyopathy","volume":"84","author":"Oudit","year":"2006","journal-title":"J. Mol. Med."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1161\/01.RES.84.11.1302","article-title":"Modulation of Iron Uptake in Heart by L-Type Ca2+ Channel Modifiers: Possible Implications in Iron Overload","volume":"84","author":"Tsushima","year":"1999","journal-title":"Circ. Res."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1007\/s11010-012-1294-y","article-title":"Effect of hepcidin on intracellular calcium in human osteoblasts","volume":"366","author":"Li","year":"2012","journal-title":"Mol. Cell Biochem."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.regpep.2011.08.009","article-title":"Hepcidin increases intracellular Ca2+ of osteoblast hFOB1.19 through L-type Ca2+ channels","volume":"172","author":"Xu","year":"2011","journal-title":"Regul. Pept."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1111\/j.1600-0609.2010.01549.x","article-title":"T-type calcium channel as a portal of iron uptake into cardiomyocytes of beta-thalassemic mice","volume":"86","author":"Kumfu","year":"2011","journal-title":"Eur. J. Haematol."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1124\/mol.112.080184","article-title":"Fe2+ block and permeation of CaV3.1 (\u03b11G) T-type calcium channels: Candidate mechanism for non-transferrin-mediated Fe2+ influx","volume":"82","author":"Lopin","year":"2012","journal-title":"Mol. Pharmacol."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1006\/taap.1995.1008","article-title":"Iron(II) Is a Modulator of Ryanodine-Sensitive Calcium Channels of Cardiac Muscle Sarcoplasmic Reticulum","volume":"130","author":"Kim","year":"1995","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_152","first-page":"13","article-title":"Ryanodine receptor-mediated Ca2+ release underlies iron-induced mitochondrial fission and stimulates mitochondrial Ca2+ uptake in primary hippocampal neurons","volume":"7","author":"Barattini","year":"2014","journal-title":"Front. Mol. Neurosci."},{"key":"ref_153","first-page":"189","article-title":"Effect of iron on the activation of the MAPK\/ERK pathway in PC12 neuroblastoma cells","volume":"39","author":"Zavala","year":"2006","journal-title":"Biol. Res."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"e125618","DOI":"10.1172\/jci.insight.125618","article-title":"Iron-deficiency anemia reduces cardiac contraction by downregulating RyR2 channels and suppressing SERCA pump activity","volume":"4","author":"Chung","year":"2019","journal-title":"JCI Insight"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"3075","DOI":"10.1038\/s41467-018-05446-4","article-title":"Calcium is an essential cofactor for metal efflux by the ferroportin transporter family","volume":"9","author":"Deshpande","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"e82947","DOI":"10.7554\/eLife.82947","article-title":"Mechanism of Ca2+ transport by ferroportin","volume":"12","author":"Shen","year":"2023","journal-title":"eLife"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/S0143-4160(02)00240-3","article-title":"Intracellular Ca2+ regulates the cellular iron uptake in K562 cells","volume":"33","author":"Ci","year":"2003","journal-title":"Cell Calcium"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1186\/s12964-020-00575-0","article-title":"CAMKK2-CAMK4 signaling regulates transferrin trafficking, turnover, and iron homeostasis","volume":"18","author":"Sabbir","year":"2020","journal-title":"Cell Commun. Signal."},{"key":"ref_159","doi-asserted-by":"crossref","unstructured":"Sabbir, M.G. (2018). Loss of Ca2+\/Calmodulin Dependent Protein Kinase Kinase 2 Leads to Aberrant Transferrin Phosphorylation and Trafficking: A Potential Biomarker for Alzheimer\u2019s Disease. Front. Mol. Biosci., 5.","DOI":"10.3389\/fmolb.2018.00099"},{"key":"ref_160","doi-asserted-by":"crossref","unstructured":"Sabbir, M.G., Taylor, C.G., and Zahradka, P. (2020). Hypomorphic CAMKK2 in EA.hy926 endothelial cells causes abnormal transferrin trafficking, iron homeostasis and glucose metabolism. Biochim. Biophys. Acta Mol. Cell Res., 1867.","DOI":"10.1016\/j.bbamcr.2020.118763"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"916082","DOI":"10.3389\/fonc.2022.916082","article-title":"The crosstalk effect between ferrous and other ions metabolism in ferroptosis for therapy of cancer","volume":"12","author":"Ke","year":"2022","journal-title":"Front. Oncol."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"48","DOI":"10.3389\/fnins.2019.00048","article-title":"Noxious Iron\u2013Calcium Connections in Neurodegeneration","volume":"13","author":"Hidalgo","year":"2019","journal-title":"Front. Neurosci."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.freeradbiomed.2021.08.231","article-title":"The calcium\u2013iron connection in ferroptosis-mediated neuronal death","volume":"175","author":"Gleitze","year":"2021","journal-title":"Free Radic. Biol. Med."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1042\/BST0361309","article-title":"Iron and calcium in the central nervous system: A close relationship in health and sickness","volume":"36","author":"Pelizzoni","year":"2008","journal-title":"Biochem. Soc. Trans."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.ceca.2017.05.007","article-title":"The role of Ca2+ in cell death caused by oxidative glutamate toxicity and ferroptosis","volume":"70","author":"Maher","year":"2018","journal-title":"Cell Calcium"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1089\/cns.1985.2.269","article-title":"Interaction of Lipid Peroxidation and Calcium in the Pathogenesis of Neuronal Injury","volume":"2","author":"Braughler","year":"1985","journal-title":"Cent. Nerv. Syst. Trauma"},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"e009291","DOI":"10.1161\/CIRCEP.120.009291","article-title":"Activation of TRPC (Transient Receptor Potential Canonical) Channel Currents in Iron Overloaded Cardiac Myocytes","volume":"14","author":"Song","year":"2021","journal-title":"Circ. Arrhythmia Electrophysiol."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"4498","DOI":"10.1038\/s41467-023-40268-z","article-title":"Cysteines 1078 and 2991 cross-linking plays a critical role in redox regulation of cardiac ryanodine receptor (RyR)","volume":"14","author":"Nikolaienko","year":"2023","journal-title":"Nat. Commun."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1038\/s41514-020-00048-1","article-title":"Targeting of intracellular Ca2+ stores as a therapeutic strategy against age-related neurotoxicities","volume":"6","author":"Goldberg","year":"2020","journal-title":"npj Aging Mech. Dis."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.nbd.2016.05.011","article-title":"Ferroptosis, a newly characterized form of cell death in Parkinson\u2019s disease that is regulated by PKC","volume":"94","author":"Gouel","year":"2016","journal-title":"Neurobiol. Dis."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.jid.2021.05.025","article-title":"CAMKK2 Defines Ferroptosis Sensitivity of Melanoma Cells by Regulating AMPK\u2014NRF2 Pathway","volume":"142","author":"Wang","year":"2022","journal-title":"J. Investig. Dermatol."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/23\/17034\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T21:36:01Z","timestamp":1760132161000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/23\/17034"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,12,1]]},"references-count":171,"journal-issue":{"issue":"23","published-online":{"date-parts":[[2023,12]]}},"alternative-id":["ijms242317034"],"URL":"https:\/\/doi.org\/10.3390\/ijms242317034","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,12,1]]}}}