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(Landmark Ed)"],"abstract":"<jats:p>Objective: Ca2+ overload of muscle fibers is one of the factors that secondarily aggravate the development of Duchenne muscular dystrophy (DMD). The purpose of this study is to evaluate the effects of the Ca2+ channel modulator 2-aminoethoxydiphenyl borate (APB) on skeletal muscle pathology in dystrophin-deficient mdx mice. Methods: Mice were randomly divided into six groups: wild type (WT), WT+3 mg\/kg APB, WT+10 mg\/kg APB, mdx, mdx+3 mg\/kg APB, mdx+10 mg\/kg APB. APB was administered intraperitoneally daily for 28 days. Finally, we assessed the grip strength and hanging time of mice, the histology and ultrastructure of the quadriceps, as well as the parameters reflecting quadricep mitochondrial function. Results: 3 mg\/kg APB was shown to reduce creatine kinase activity in the serum, intensity of degeneration and the level of fibrosis in the quadriceps of mdx mice, and improved tissue ultrastructure. However, this effect of APB was not sufficient to improve grip strength and hanging time of mdx mice. The effect of 3 mg\/kg APB may be due to improve Ca2+ homeostasis in skeletal muscles, as evidenced by a trend toward decreased Ca2+ overload of quadricep mitochondria. High dose of APB (10 mg\/kg body weight) showed less pronounced effect on the pathological phenotype of mdx mice. Moreover, 10 mg\/kg APB disrupted the ultrastructure of the quadriceps and caused a decrease in grip strength in WT mice. Conclusions: APB is able to improve the phenotype in mdx mouse DMD model. However, the effect of APB is quite limited, which may be due to its multitargeting of Ca2+ channels in the membranes of muscle fibers and intracellular organelles, differentially expressed in DMD.<\/jats:p>","DOI":"10.31083\/j.fbl2912428","type":"journal-article","created":{"date-parts":[[2024,12,30]],"date-time":"2024-12-30T11:37:01Z","timestamp":1735558621000},"source":"Crossref","is-referenced-by-count":3,"title":["Effect of 2-Aminoethoxydiphenyl Borate on the State of Skeletal Muscles in Dystrophin-Deficient mdx Mice"],"prefix":"10.31083","volume":"29","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7453-3390","authenticated-orcid":true,"given":"Mikhail V.","family":"Dubinin","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Cell Biology and Microbiology, Mari State University, 424001 Yoshkar-Ola, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2573-4847","authenticated-orcid":true,"given":"Anastasia E.","family":"Stepanova","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Cell Biology and Microbiology, Mari State University, 424001 Yoshkar-Ola, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0000-2272-1229","authenticated-orcid":true,"given":"Anastasia D.","family":"Igoshkina","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Cell Biology and Microbiology, Mari State University, 424001 Yoshkar-Ola, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8054-0477","authenticated-orcid":true,"given":"Irina B.","family":"Mikheeva","sequence":"first","affiliation":[{"name":"Laboratory of Experimental Neurobiology, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6227-7409","authenticated-orcid":true,"given":"Eugeny Yu.","family":"Talanov","sequence":"first","affiliation":[{"name":"Laboratory of Mitochondrial Transport, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0008-8782-1552","authenticated-orcid":true,"given":"Alena A.","family":"Cherepanova","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Cell Biology and Microbiology, Mari State University, 424001 Yoshkar-Ola, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5392-7035","authenticated-orcid":true,"given":"Konstantin N.","family":"Belosludtsev","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Cell Biology and Microbiology, Mari State University, 424001 Yoshkar-Ola, Russia"},{"name":"Laboratory of Mitochondrial Transport, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"16242","published-online":{"date-parts":[[2024,12,25]]},"reference":[{"key":"ref1","doi-asserted-by":"publisher","unstructured":"Monaco AP, Neve RL, Colletti-Feener C, Bertelson CJ, Kurnit DM, Kunkel LM. Isolation of candidate cDNAs for portions of the Duchenne muscular dystrophy gene. Nature. 1986; 323: 646\u2013650.","DOI":"10.1038\/323646a0."},{"key":"ref2","doi-asserted-by":"publisher","unstructured":"Duan D, Goemans N, Takeda S, Mercuri E, Aartsma-Rus A. Duchenne muscular dystrophy. Nature Reviews. Disease Primers. 2021; 7: 13.","DOI":"10.1038\/s41572-021-00248-3."},{"key":"ref3","doi-asserted-by":"publisher","unstructured":"Dubinin MV, Belosludtsev KN. Ion Channels of the Sarcolemma and Intracellular Organelles in Duchenne Muscular Dystrophy: A Role in the Dysregulation of Ion Homeostasis and a Possible Target for Therapy. International Journal of Molecular Sciences. 2023; 24: 2229.","DOI":"10.3390\/ijms24032229."},{"key":"ref4","doi-asserted-by":"publisher","unstructured":"Mareedu S, Million ED, Duan D, Babu GJ. Abnormal Calcium Handling in Duchenne Muscular Dystrophy: Mechanisms and Potential Therapies. Frontiers in Physiology. 2021; 12: 647010.","DOI":"10.3389\/fphys.2021.647010."},{"key":"ref5","doi-asserted-by":"publisher","unstructured":"Leyva-Leyva M, Sandoval A, Felix R, Gonz\u00e1lez-Ram\u00edrez R. Biochemical and Functional Interplay Between Ion Channels and the Components of the Dystrophin-Associated Glycoprotein Complex. The Journal of Membrane Biology. 2018; 251: 535\u2013550.","DOI":"10.1007\/s00232-018-0036-9."},{"key":"ref6","doi-asserted-by":"publisher","unstructured":"Maruyama T, Kanaji T, Nakade S, Kanno T, Mikoshiba K. 2APB, 2-aminoethoxydiphenyl borate, a membrane-penetrable modulator of Ins(1,4,5)P3-induced Ca2+ release. Journal of Biochemistry. 1997; 122: 498\u2013505.","DOI":"10.1093\/oxfordjournals.jbchem.a021780."},{"key":"ref7","doi-asserted-by":"publisher","unstructured":"Bilmen JG, Wootton LL, Godfrey RE, Smart OS, Michelangeli F. Inhibition of SERCA Ca2+ pumps by 2-aminoethoxydiphenyl borate (2-APB). 2-APB reduces both Ca2+ binding and phosphoryl transfer from ATP, by interfering with the pathway leading to the Ca2+-binding sites. European Journal of Biochemistry. 2002; 269: 3678\u20133687.","DOI":"10.1046\/j.1432-1033.2002.03060.x."},{"key":"ref8","doi-asserted-by":"publisher","unstructured":"Missiaen L, Callewaert G, De Smedt H, Parys JB. 2-Aminoethoxydiphenyl borate affects the inositol 1,4,5-trisphosphate receptor, the intracellular Ca2+ pump and the non-specific Ca2+ leak from the non-mitochondrial Ca2+ stores in permeabilized A7r5 cells. Cell Calcium. 2001; 29: 111\u2013116.","DOI":"10.1054\/ceca.2000.0163."},{"key":"ref9","doi-asserted-by":"publisher","unstructured":"Peppiatt CM, Collins TJ, Mackenzie L, Conway SJ, Holmes AB, Bootman MD, et al. 2-Aminoethoxydiphenyl borate (2-APB) antagonises inositol 1,4,5-trisphosphate-induced calcium release, inhibits calcium pumps and has a use-dependent and slowly reversible action on store-operated calcium entry channels. Cell Calcium. 2003; 34: 97\u2013108.","DOI":"10.1016\/s0143-4160(03)00026-5."},{"key":"ref10","doi-asserted-by":"publisher","unstructured":"Dellis O, Mercier P, Chomienne C. The boron-oxygen core of borinate esters is responsible for the store-operated calcium entry potentiation ability. BMC Pharmacology. 2011; 11: 1.","DOI":"10.1186\/1471-2210-11-1."},{"key":"ref11","doi-asserted-by":"publisher","unstructured":"Peinelt C, Lis A, Beck A, Fleig A, Penner R. 2-Aminoethoxydiphenyl borate directly facilitates and indirectly inhibits STIM1-dependent gating of CRAC channels. The Journal of Physiology. 2008; 586: 3061\u20133073.","DOI":"10.1113\/jphysiol.2008.151365."},{"key":"ref12","doi-asserted-by":"publisher","unstructured":"Wei M, Zhou Y, Sun A, Ma G, He L, Zhou L, et al. Molecular mechanisms underlying inhibition of STIM1-Orai1-mediated Ca2+ entry induced by 2-aminoethoxydiphenyl borate. Pflugers Archiv: European Journal of Physiology. 2016; 468: 2061\u20132074.","DOI":"10.1007\/s00424-016-1880-z."},{"key":"ref13","doi-asserted-by":"publisher","unstructured":"Lievremont JP, Bird GS, Putney JW, Jr. Mechanism of inhibition of TRPC cation channels by 2-aminoethoxydiphenylborane. Molecular Pharmacology. 2005; 68: 758\u2013762.","DOI":"10.1124\/mol.105.012856."},{"key":"ref14","doi-asserted-by":"publisher","unstructured":"Clapham DE. Calcium signaling. Cell. 2007; 131: 1047\u20131058.","DOI":"10.1016\/j.cell.2007.11.028."},{"key":"ref15","doi-asserted-by":"publisher","unstructured":"Chokshi R, Fruasaha P, Kozak JA. 2-aminoethyl diphenyl borinate (2-APB) inhibits TRPM7 channels through an intracellular acidification mechanism. Channels. 2012; 6: 362\u2013369.","DOI":"10.4161\/chan.21628."},{"key":"ref16","doi-asserted-by":"publisher","unstructured":"Malko P, Syed Mortadza SA, McWilliam J, Jiang LH. TRPM2 Channel in Microglia as a New Player in Neuroinflammation Associated With a Spectrum of Central Nervous System Pathologies. Frontiers in Pharmacology. 2019; 10: 239.","DOI":"10.3389\/fphar.2019.00239."},{"key":"ref17","doi-asserted-by":"publisher","unstructured":"Knox CD, Belous AE, Pierce JM, Wakata A, Nicoud IB, Anderson CD, et al. Novel role of phospholipase C-delta1: regulation of liver mitochondrial Ca2+ uptake. American Journal of Physiology. Gastrointestinal and Liver Physiology. 2004; 287: G533\u201340.","DOI":"10.1152\/ajpgi.00050.2004."},{"key":"ref18","doi-asserted-by":"publisher","unstructured":"Nicoud IB, Knox CD, Jones CM, Anderson CD, Pierce JM, Belous AE, et al. 2-APB protects against liver ischemia-reperfusion injury by reducing cellular and mitochondrial calcium uptake. American Journal of Physiology. Gastrointestinal and Liver Physiology. 2007; 293: G623\u2013G630.","DOI":"10.1152\/ajpgi.00521.2006."},{"key":"ref19","doi-asserted-by":"publisher","unstructured":"Dubinin MV, Chulkov AV, Igoshkina AD, Cherepanova AA, Mikina NV. Effect of 2-aminoethoxydiphenyl borate on the functions of mouse skeletal muscle mitochondria. Biochemical and Biophysical Research Communications. 2024; 712\u2013713: 149944.","DOI":"10.1016\/j.bbrc.2024.149944."},{"key":"ref20","doi-asserted-by":"publisher","unstructured":"Hu H, Grandl J, Bandell M, Petrus M, Patapoutian A. Two amino acid residues determine 2-APB sensitivity of the ion channels TRPV3 and TRPV4. Proceedings of the National Academy of Sciences of the United States of America. 2009; 106: 1626\u20131631.","DOI":"10.1073\/pnas.0812209106."},{"key":"ref21","doi-asserted-by":"publisher","unstructured":"Hu HZ, Gu Q, Wang C, Colton CK, Tang J, Kinoshita-Kawada M, et al. 2-aminoethoxydiphenyl borate is a common activator of TRPV1, TRPV2, and TRPV3. The Journal of Biological Chemistry. 2004; 279: 35741\u201335748.","DOI":"10.1074\/jbc.M404164200."},{"key":"ref22","doi-asserted-by":"publisher","unstructured":"Kovacs G, Montalbetti N, Simonin A, Danko T, Balazs B, Zsembery A, et al. Inhibition of the human epithelial calcium channel TRPV6 by 2-aminoethoxydiphenyl borate (2-APB). Cell Calcium. 2012; 52: 468\u2013480.","DOI":"10.1016\/j.ceca.2012.08.005."},{"key":"ref23","doi-asserted-by":"publisher","unstructured":"Pumroy RA, Protopopova AD, Fricke TC, Lange IU, Haug FM, Nguyen PT, et al. Structural insights into TRPV2 activation by small molecules. Nature Communications. 2022; 13: 2334.","DOI":"10.1038\/s41467-022-30083-3."},{"key":"ref24","doi-asserted-by":"publisher","unstructured":"Vaidya B, Kaur H, Thapak P, Sharma SS, Singh JN. Pharmacological Modulation of TRPM2 Channels via PARP Pathway Leads to Neuroprotection in MPTP-induced Parkinson\u2019s Disease in Sprague Dawley Rats. Molecular Neurobiology. 2022; 59: 1528\u20131542.","DOI":"10.1007\/s12035-021-02711-4."},{"key":"ref25","doi-asserted-by":"publisher","unstructured":"Thapak P, Khare P, Bishnoi M, Sharma SS. Neuroprotective Effect of 2-Aminoethoxydiphenyl Borate (2-APB) in Amyloid \u03b2-Induced Memory Dysfunction: A Mechanistic Study. Cellular and Molecular Neurobiology. 2022; 42: 1211\u20131223.","DOI":"10.1007\/s10571-020-01012-z."},{"key":"ref26","doi-asserted-by":"publisher","unstructured":"Morihara H, Obana M, Tanaka S, Kawakatsu I, Tsuchiyama D, Mori S, et al. 2-aminoethoxydiphenyl borate provides an anti-oxidative effect and mediates cardioprotection during ischemia reperfusion in mice. PLoS ONE. 2017; 12: e0189948.","DOI":"10.1371\/journal.pone.0189948."},{"key":"ref27","doi-asserted-by":"publisher","unstructured":"Vaidya B, Polepalli M, Sharma SS, Singh JN. 2-Aminoethoxydiphenyl borate ameliorates mitochondrial dysfunctions in MPTP\/MPP+ model of Parkinson\u2019s disease. Mitochondrion. 2023; 69: 95\u2013103.","DOI":"10.1016\/j.mito.2023.02.003."},{"key":"ref28","doi-asserted-by":"publisher","unstructured":"Mondin L, Balghi H, Constantin B, Cognard C, Sebille S. Negative modulation of inositol 1,4,5-trisphosphate type 1 receptor expression prevents dystrophin-deficient muscle cells death. American Journal of Physiology. Cell Physiology. 2009; 297: C1133\u2013C1145.","DOI":"10.1152\/ajpcell.00048.2009."},{"key":"ref29","unstructured":"van Putten M, Aartsma-Rus A, Louvain-la-Neuve L. The use of hanging wire tests to monitor muscle strength and condition over time. Treat-Nmd.Eu. 2012; 1\u201312."},{"key":"ref30","doi-asserted-by":"publisher","unstructured":"Dubinin MV, Mikheeva IB, Stepanova AE, Igoshkina AD, Cherepanova AA, Semenova AA, et al. Mitochondrial Transplantation Therapy Ameliorates Muscular Dystrophy in mdx Mouse Model. Biomolecules. 2024; 14: 316.","DOI":"10.3390\/biom14030316."},{"key":"ref31","doi-asserted-by":"publisher","unstructured":"Kumar A, Accorsi A, Rhee Y, Girgenrath M. Do\u2019s and don\u2019ts in the preparation of muscle cryosections for histological analysis. Journal of Visualized Experiments. 2015; e52793.","DOI":"10.3791\/52793."},{"key":"ref32","doi-asserted-by":"publisher","unstructured":"Spurney CF, Gordish-Dressman H, Guerron AD, Sali A, Pandey GS, Rawat R, et al. Preclinical drug trials in the mdx mouse: assessment of reliable and sensitive outcome measures. Muscle & Nerve. 2009; 39: 591\u2013602.","DOI":"10.1002\/mus.21211."},{"key":"ref33","doi-asserted-by":"publisher","unstructured":"Dubinin MV, Starinets VS, Belosludtseva NV, Mikheeva IB, Chelyadnikova YA, Igoshkina AD, et al. BKCa Activator NS1619 Improves the Structure and Function of Skeletal Muscle Mitochondria in Duchenne Dystrophy. Pharmaceutics. 2022; 14: 2336.","DOI":"10.3390\/pharmaceutics14112336."},{"key":"ref34","doi-asserted-by":"publisher","unstructured":"Thoudam T, Ha CM, Leem J, Chanda D, Park JS, Kim HJ, et al. PDK4 Augments ER-Mitochondria Contact to Dampen Skeletal Muscle Insulin Signaling During Obesity. Diabetes. 2019; 68: 571\u2013586.","DOI":"10.2337\/db18-0363."},{"key":"ref35","doi-asserted-by":"publisher","unstructured":"Frezza C, Cipolat S, Scorrano L. Organelle isolation: functional mitochondria from mouse liver, muscle and cultured fibroblasts. Nature Protocols. 2007; 2: 287\u2013295.","DOI":"10.1038\/nprot.2006.478."},{"key":"ref36","doi-asserted-by":"crossref","unstructured":"CHANCE B, WILLIAMS GR. Respiratory enzymes in oxidative phosphorylation. I. Kinetics of oxygen utilization. The Journal of Biological Chemistry. 1955; 217: 383\u2013393.","DOI":"10.1016\/S0021-9258(19)57189-7"},{"key":"ref37","doi-asserted-by":"publisher","unstructured":"Bround MJ, Havens JR, York AJ, Sargent MA, Karch J, Molkentin JD. ANT-dependent MPTP underlies necrotic myofiber death in muscular dystrophy. Science Advances. 2023; 9: eadi2767.","DOI":"10.1126\/sciadv.adi2767."},{"key":"ref38","doi-asserted-by":"publisher","unstructured":"Thapak P, Bishnoi M, Sharma SS. Pharmacological Inhibition of Transient Receptor Potential Melastatin 2 (TRPM2) Channels Attenuates Diabetes-induced Cognitive Deficits in Rats: A Mechanistic Study. Current Neurovascular Research. 2020; 17: 249\u2013258.","DOI":"10.2174\/1567202617666200415142211."},{"key":"ref39","doi-asserted-by":"publisher","unstructured":"Valladares D, Utreras-Mendoza Y, Campos C, Morales C, Diaz-Vegas A, Contreras-Ferrat A, et al. IP3 receptor blockade restores autophagy and mitochondrial function in skeletal muscle fibers of dystrophic mice. Biochimica et Biophysica Acta. Molecular Basis of Disease. 2018; 1864: 3685\u20133695.","DOI":"10.1016\/j.bbadis.2018.08.042."},{"key":"ref40","doi-asserted-by":"publisher","unstructured":"Dubinin MV, Stepanova AE, Mikheeva IB, Igoshkina AD, Cherepanova AA, Talanov EY, et al. Reduction of Mitochondrial Calcium Overload via MKT077-Induced Inhibition of Glucose-Regulated Protein 75 Alleviates Skeletal Muscle Pathology in Dystrophin-Deficient mdx Mice. International Journal of Molecular Sciences. 2024\u037e 25: 9892.","DOI":"10.3390\/ijms25189892."},{"key":"ref41","doi-asserted-by":"publisher","unstructured":"Periasamy M, Kalyanasundaram A. SERCA pump isoforms: their role in calcium transport and disease. Muscle & Nerve. 2007; 35: 430\u2013442.","DOI":"10.1002\/mus.20745."},{"key":"ref42","doi-asserted-by":"publisher","unstructured":"Tupling AR. The decay phase of Ca2+ transients in skeletal muscle: regulation and physiology. Applied Physiology, Nutrition, and Metabolism. 2009; 34: 373\u2013376.","DOI":"10.1139\/H09-033."},{"key":"ref43","doi-asserted-by":"publisher","unstructured":"Iwata Y, Katanosaka Y, Arai Y, Komamura K, Miyatake K, Shigekawa M. A novel mechanism of myocyte degeneration involving the Ca2+-permeable growth factor-regulated channel. The Journal of Cell Biology. 2003; 161: 957\u2013967.","DOI":"10.1083\/jcb.200301101."},{"key":"ref44","doi-asserted-by":"publisher","unstructured":"Iwata Y, Katanosaka Y, Arai Y, Shigekawa M, Wakabayashi S. Dominant-negative inhibition of Ca2+ influx via TRPV2 ameliorates muscular dystrophy in animal models. Human Molecular Genetics. 2009; 18: 824\u2013834.","DOI":"10.1093\/hmg\/ddn408."},{"key":"ref45","doi-asserted-by":"publisher","unstructured":"Liu X, Yao S, Pan M, Cai Y, Shentu W, Cai W, et al. Two-dimensional speckle tracking echocardiography demonstrates improved myocardial function after intravenous infusion of bone marrow mesenchymal stem in the X-Linked muscular dystrophy mice. BMC Cardiovascular Disorders. 2022; 22: 461.","DOI":"10.1186\/s12872-022-02886-1."},{"key":"ref46","doi-asserted-by":"publisher","unstructured":"Naume MM, J\u00f8rgensen MH, H\u00f8i-Hansen CE, Born AP, Vissing J, Borgwardt L, et al. Metabolic assessment in children with neuromuscular disorders shows risk of liver enlargement, steatosis and fibrosis. Acta Paediatrica. 2023; 112: 846\u2013853.","DOI":"10.1111\/apa.16649."},{"key":"ref47","doi-asserted-by":"publisher","unstructured":"Stedman HH, Sweeney HL, Shrager JB, Maguire HC, Panettieri RA, Petrof B, et al. The mdx mouse diaphragm reproduces the degenerative changes of Duchenne muscular dystrophy. 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