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Journal articles on the topic 'Dystrophin'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Straub, Volker, Jill A. Rafael, Jeffrey S. Chamberlain, and Kevin P. Campbell. "Animal Models for Muscular Dystrophy Show Different Patterns of Sarcolemmal Disruption." Journal of Cell Biology 139, no. 2 (1997): 375–85. http://dx.doi.org/10.1083/jcb.139.2.375.

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Genetic defects in a number of components of the dystrophin–glycoprotein complex (DGC) lead to distinct forms of muscular dystrophy. However, little is known about how alterations in the DGC are manifested in the pathophysiology present in dystrophic muscle tissue. One hypothesis is that the DGC protects the sarcolemma from contraction-induced damage. Using tracer molecules, we compared sarcolemmal integrity in animal models for muscular dystrophy and in muscular dystrophy patient samples. Evans blue, a low molecular weight diazo dye, does not cross into skeletal muscle fibers in normal mice.

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2

Cui, Chang-Hao, Taro Uyama, Kenji Miyado, et al. "Menstrual Blood-derived Cells Confer Human Dystrophin Expression in the Murine Model of Duchenne Muscular Dystrophy via Cell Fusion and Myogenic Transdifferentiation." Molecular Biology of the Cell 18, no. 5 (2007): 1586–94. http://dx.doi.org/10.1091/mbc.e06-09-0872.

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Duchenne muscular dystrophy (DMD), the most common lethal genetic disorder in children, is an X-linked recessive muscle disease characterized by the absence of dystrophin at the sarcolemma of muscle fibers. We examined a putative endometrial progenitor obtained from endometrial tissue samples to determine whether these cells repair muscular degeneration in a murine mdx model of DMD. Implanted cells conferred human dystrophin in degenerated muscle of immunodeficient mdx mice. We then examined menstrual blood–derived cells to determine whether primarily cultured nontransformed cells also repair

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3

Steen, Michelle S., Marvin E. Adams, Yan Tesch, and Stanley C. Froehner. "Amelioration of Muscular Dystrophy by Transgenic Expression of Niemann-Pick C1." Molecular Biology of the Cell 20, no. 1 (2009): 146–52. http://dx.doi.org/10.1091/mbc.e08-08-0811.

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Duchenne muscular dystrophy (DMD) and other types of muscular dystrophies are caused by the loss or alteration of different members of the dystrophin protein complex. Understanding the molecular mechanisms by which dystrophin-associated protein abnormalities contribute to the onset of muscular dystrophy may identify new therapeutic approaches to these human disorders. By examining gene expression alterations in mouse skeletal muscle lacking α-dystrobrevin (Dtna−/−), we identified a highly significant reduction of the cholesterol trafficking protein, Niemann-Pick C1 (NPC1). Mutations in NPC1 ca

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4

Peter, Angela K., Jamie L. Marshall, and Rachelle H. Crosbie. "Sarcospan reduces dystrophic pathology: stabilization of the utrophin–glycoprotein complex." Journal of Cell Biology 183, no. 3 (2008): 419–27. http://dx.doi.org/10.1083/jcb.200808027.

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Mutations in the dystrophin gene cause Duchenne muscular dystrophy and result in the loss of dystrophin and the entire dystrophin–glycoprotein complex (DGC) from the sarcolemma. We show that sarcospan (SSPN), a unique tetraspanin-like component of the DGC, ameliorates muscular dystrophy in dystrophin-deficient mdx mice. SSPN stabilizes the sarcolemma by increasing levels of the utrophin–glycoprotein complex (UGC) at the extrasynaptic membrane to compensate for the loss of dystrophin. Utrophin is normally restricted to the neuromuscular junction, where it replaces dystrophin to form a functiona

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5

Yeadon, J. E., H. Lin, S. M. Dyer, and S. J. Burden. "Dystrophin is a component of the subsynaptic membrane." Journal of Cell Biology 115, no. 4 (1991): 1069–76. http://dx.doi.org/10.1083/jcb.115.4.1069.

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A subsynaptic protein of Mr approximately 300 kD is a major component of Torpedo electric organ postsynaptic membranes and copurifies with the AChR and the 43-kD subsynaptic protein. mAbs against this protein react with neuromuscular synapses in higher vertebrates, but not at synapses in dystrophic muscle. The Torpedo 300-kD protein comigrates in SDS-PAGE with murine dystrophin and reacts with antibodies against murine dystrophin. The sequence of a partial cDNA isolated by screening an expression library with mAbs against the Torpedo 300-kD protein shows striking homology to mammalian dystroph

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6

Chen, Yi-Wen, Po Zhao, Rehannah Borup, and Eric P. Hoffman. "Expression Profiling in the Muscular Dystrophies." Journal of Cell Biology 151, no. 6 (2000): 1321–36. http://dx.doi.org/10.1083/jcb.151.6.1321.

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We used expression profiling to define the pathophysiological cascades involved in the progression of two muscular dystrophies with known primary biochemical defects, dystrophin deficiency (Duchenne muscular dystrophy) and α-sarcoglycan deficiency (a dystrophin-associated protein). We employed a novel protocol for expression profiling in human tissues using mixed samples of multiple patients and iterative comparisons of duplicate datasets. We found evidence for both incomplete differentiation of patient muscle, and for dedifferentiation of myofibers to alternative lineages with advancing age.

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7

Teramoto, Naomi, Hidetoshi Sugihara, Keitaro Yamanouchi, et al. "Pathological evaluation of rats carrying in-frame mutations in the dystrophin gene: a new model of Becker muscular dystrophy." Disease Models & Mechanisms 13, no. 9 (2020): dmm044701. http://dx.doi.org/10.1242/dmm.044701.

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ABSTRACTDystrophin, encoded by the DMD gene on the X chromosome, stabilizes the sarcolemma by linking the actin cytoskeleton with the dystrophin-glycoprotein complex (DGC). In-frame mutations in DMD cause a milder form of X-linked muscular dystrophy, called Becker muscular dystrophy (BMD), characterized by the reduced expression of truncated dystrophin. So far, no animal model with in-frame mutations in Dmd has been established. As a result, the effect of in-frame mutations on the dystrophin expression profile and disease progression of BMD remains unclear. In this study, we established a nove

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8

Spaulding, HR, C. Ballmann, JC Quindry, MB Hudson, and JT Selsby. "Autophagy in the heart is enhanced and independent of disease progression in mus musculus dystrophinopathy models." JRSM Cardiovascular Disease 8 (January 2019): 204800401987958. http://dx.doi.org/10.1177/2048004019879581.

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Background Duchenne muscular dystrophy is a muscle wasting disease caused by dystrophin gene mutations resulting in dysfunctional dystrophin protein. Autophagy, a proteolytic process, is impaired in dystrophic skeletal muscle though little is known about the effect of dystrophin deficiency on autophagy in cardiac muscle. We hypothesized that with disease progression autophagy would become increasingly dysfunctional based upon indirect autophagic markers. Methods Markers of autophagy were measured by western blot in 7-week-old and 17-month-old control (C57) and dystrophic (mdx) hearts. Results

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9

Zabłocka, Barbara, Dariusz C. Górecki, and Krzysztof Zabłocki. "Disrupted Calcium Homeostasis in Duchenne Muscular Dystrophy: A Common Mechanism behind Diverse Consequences." International Journal of Molecular Sciences 22, no. 20 (2021): 11040. http://dx.doi.org/10.3390/ijms222011040.

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Duchenne muscular dystrophy (DMD) leads to disability and death in young men. This disease is caused by mutations in the DMD gene encoding diverse isoforms of dystrophin. Loss of full-length dystrophins is both necessary and sufficient for causing degeneration and wasting of striated muscles, neuropsychological impairment, and bone deformities. Among this spectrum of defects, abnormalities of calcium homeostasis are the common dystrophic feature. Given the fundamental role of Ca2+ in all cells, this biochemical alteration might be underlying all the DMD abnormalities. However, its mechanism is

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10

Zabłocka, Barbara, Dariusz C. Górecki, and Krzysztof Zabłocki. "Disrupted Calcium Homeostasis in Duchenne Muscular Dystrophy: A Common Mechanism behind Diverse Consequences." International Journal of Molecular Sciences 22, no. 20 (2021): 11040. http://dx.doi.org/10.3390/ijms222011040.

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Duchenne muscular dystrophy (DMD) leads to disability and death in young men. This disease is caused by mutations in the DMD gene encoding diverse isoforms of dystrophin. Loss of full-length dystrophins is both necessary and sufficient for causing degeneration and wasting of striated muscles, neuropsychological impairment, and bone deformities. Among this spectrum of defects, abnormalities of calcium homeostasis are the common dystrophic feature. Given the fundamental role of Ca2+ in all cells, this biochemical alteration might be underlying all the DMD abnormalities. However, its mechanism is

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11

Ibrahim Sory, P., T. Sidi, L. Guida, et al. "Dystrophie Musculaire de Duchenne: Aspects cliniques, biologiques et évolutifs à propos de cinq cas dans le service de Rhumatologie au CHU du Point G." Rhumatologie Africaine Francophone 6, no. 2 (2024): 18–23. http://dx.doi.org/10.62455/raf.v6i2.53.

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Résumé  La dystrophie musculaire de Duchenne (DMD) due à la non expression de la dystrophine est liée au chromosome X. Décrite au 19e siècle, est la plus courante dystrophie musculaire de l’enfant [1, 2]. L’incidence est estimée à 30 cas pour 100 000 naissances [1, 2]. But- étudier les caractères cliniques, biologiques et évolutifs de la dystrophie musculaire de Duchenne. Patients et Méthodes : Il s’est agi d’une étude rétrospective portant sur 5 dossiers de DMD, colligés en 7 ans. Résultats Nous rapportons cinq dossiers de garçons colligés entre 2005 et 201

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12

Koenig, Xaver, Janine Ebner, and Karlheinz Hilber. "Voltage-Dependent Sarcolemmal Ion Channel Abnormalities in the Dystrophin-Deficient Heart." International Journal of Molecular Sciences 19, no. 11 (2018): 3296. http://dx.doi.org/10.3390/ijms19113296.

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Mutations in the gene encoding for the intracellular protein dystrophin cause severe forms of muscular dystrophy. These so-called dystrophinopathies are characterized by skeletal muscle weakness and degeneration. Dystrophin deficiency also gives rise to considerable complications in the heart, including cardiomyopathy development and arrhythmias. The current understanding of the pathomechanisms in the dystrophic heart is limited, but there is growing evidence that dysfunctional voltage-dependent ion channels in dystrophin-deficient cardiomyocytes play a significant role. Herein, we summarize t

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13

Pelosi, Laura, Laura Forcina, Carmine Nicoletti, Bianca Maria Scicchitano, and Antonio Musarò. "Increased Circulating Levels of Interleukin-6 Induce Perturbation in Redox-Regulated Signaling Cascades in Muscle of Dystrophic Mice." Oxidative Medicine and Cellular Longevity 2017 (2017): 1–10. http://dx.doi.org/10.1155/2017/1987218.

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Duchenne muscular dystrophy (DMD) is an X-linked genetic disease in which dystrophin gene is mutated, resulting in dysfunctional or absent dystrophin protein. The pathology of dystrophic muscle includes degeneration, necrosis with inflammatory cell invasion, regeneration, and fibrous and fatty changes. Nevertheless, the mechanisms by which the absence of dystrophin leads to muscle degeneration remain to be fully elucidated. An imbalance between oxidant and antioxidant systems has been proposed as a secondary effect of DMD. However, the significance and precise extent of the perturbation in red

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14

Barnabei, Matthew S., Joshua M. Martindale, DeWayne Townsend, and Joseph M. Metzger. "Exercise and Muscular Dystrophy: Implications and Analysis of Effects on Musculoskeletal and Cardiovascular Systems." Comprehensive Physiology 1, no. 3 (2011): 1353–63. https://doi.org/10.1002/j.2040-4603.2011.tb00368.x.

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AbstractThe muscular dystrophies are a heterogeneous collection of progressive, inherited diseases of muscle weakness and degeneration. Although these diseases can vary widely in their etiology and presentation, nearly all muscular dystrophies cause exercise intolerance to some degree. Here, we focus on Duchenne muscular dystrophy (DMD), the most common form of muscular dystrophy, as a paradigm for the effects of muscle disease on exercise capacity. First described in the mid‐1800s, DMD is a rapidly progressive and lethal muscular dystrophy caused by mutations in the dystrophin gene. Dystrophi

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15

Blake, Derek J., Andrew Weir, Sarah E. Newey, and Kay E. Davies. "Function and Genetics of Dystrophin and Dystrophin-Related Proteins in Muscle." Physiological Reviews 82, no. 2 (2002): 291–329. http://dx.doi.org/10.1152/physrev.00028.2001.

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The X-linked muscle-wasting disease Duchenne muscular dystrophy is caused by mutations in the gene encoding dystrophin. There is currently no effective treatment for the disease; however, the complex molecular pathology of this disorder is now being unravelled. Dystrophin is located at the muscle sarcolemma in a membrane-spanning protein complex that connects the cytoskeleton to the basal lamina. Mutations in many components of the dystrophin protein complex cause other forms of autosomally inherited muscular dystrophy, indicating the importance of this complex in normal muscle function. Altho

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16

Meyers, Tatyana A., Jackie A. Heitzman, and DeWayne Townsend. "DMD carrier model with mosaic dystrophin expression in the heart reveals complex vulnerability to myocardial injury." Human Molecular Genetics 29, no. 6 (2020): 944–54. http://dx.doi.org/10.1093/hmg/ddaa015.

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Abstract Duchenne muscular dystrophy (DMD) is a devastating neuromuscular disease that causes progressive muscle wasting and cardiomyopathy. This X-linked disease results from mutations of the DMD allele on the X-chromosome resulting in the loss of expression of the protein dystrophin. Dystrophin loss causes cellular dysfunction that drives the loss of healthy skeletal muscle and cardiomyocytes. As gene therapy strategies strive toward dystrophin restoration through micro-dystrophin delivery or exon skipping, preclinical models have shown that incomplete restoration in the heart results in het

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17

Betts, Corinne A., Aarti Jagannath, Tirsa LE van Westering, et al. "Dystrophin involvement in peripheral circadian SRF signalling." Life Science Alliance 4, no. 10 (2021): e202101014. http://dx.doi.org/10.26508/lsa.202101014.

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Absence of dystrophin, an essential sarcolemmal protein required for muscle contraction, leads to the devastating muscle-wasting disease Duchenne muscular dystrophy. Dystrophin has an actin-binding domain, which binds and stabilises filamentous-(F)-actin, an integral component of the RhoA-actin-serum-response-factor-(SRF) pathway. This pathway plays a crucial role in circadian signalling, whereby the suprachiasmatic nucleus (SCN) transmits cues to peripheral tissues, activating SRF and transcription of clock-target genes. Given dystrophin binds F-actin and disturbed SRF-signalling disrupts clo

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18

Vieira, Natassia M., Janelle M. Spinazzola, Matthew S. Alexander та ін. "Repression of phosphatidylinositol transfer protein α ameliorates the pathology of Duchenne muscular dystrophy". Proceedings of the National Academy of Sciences 114, № 23 (2017): 6080–85. http://dx.doi.org/10.1073/pnas.1703556114.

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Duchenne muscular dystrophy (DMD) is a progressive muscle wasting disease caused by X-linked inherited mutations in the DYSTROPHIN (DMD) gene. Absence of dystrophin protein from the sarcolemma causes severe muscle degeneration, fibrosis, and inflammation, ultimately leading to cardiorespiratory failure and premature death. Although there are several promising strategies under investigation to restore dystrophin protein expression, there is currently no cure for DMD, and identification of genetic modifiers as potential targets represents an alternative therapeutic strategy. In a Brazilian golde

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Law, D. J., D. L. Allen, and J. G. Tidball. "Talin, vinculin and DRP (utrophin) concentrations are increased at mdx myotendinous junctions following onset of necrosis." Journal of Cell Science 107, no. 6 (1994): 1477–83. http://dx.doi.org/10.1242/jcs.107.6.1477.

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Duchenne muscular dystrophy (DMD) and the myopathy seen in the mdx mouse both result from absence of the protein dystrophin. Structural similarities between dystrophin and other cytoskeletal proteins, its enrichment at myotendinous junctions, and its indirect association with laminin mediated by a transmembrane glycoprotein complex suggest that one of dystrophin's functions in normal muscle is to form one of the links between the actin cytoskeleton and the extracellular matrix. Unlike Duchenne muscular dystrophy patients, mdx mice suffer only transient muscle necrosis, and are able to regenera

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20

Bergman, Robert L., Karen D. Inzana, William E. Monroe, et al. "Dystrophin-Deficient Muscular Dystrophy in a Labrador Retriever." Journal of the American Animal Hospital Association 38, no. 3 (2002): 255–61. http://dx.doi.org/10.5326/0380255.

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Sex-linked muscular dystrophy associated with dystrophin deficiency has been reported in several breeds of dogs and is best characterized in the golden retriever. In this case report, a young, male Labrador retriever with dystrophin-deficient muscular dystrophy is presented. Clinical signs included generalized weakness, lingual hypertrophy, and dysphagia. Electromyographic abnormalities including complex repetitive discharges were present. Serum creatine kinase concentration was dramatically elevated. Histopathological changes within a muscle biopsy specimen confirmed a dystrophic myopathy, an

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21

Bellayou, Hanane, Khalil Hamzi, Mohamed Abdou Rafai, et al. "Duchenne and Becker Muscular Dystrophy: Contribution of a Molecular and Immunohistochemical Analysis in Diagnosis in Morocco." Journal of Biomedicine and Biotechnology 2009 (2009): 1–5. http://dx.doi.org/10.1155/2009/325210.

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Duchenne muscular dystrophy (DMD) and Becker muscular dystrophy (BMD) are X-linked recessive disorders caused by mutations of the DMD gene located at Xp21. In DMD patients, dystrophin is virtually absent; whereas BMD patients have 10% to 40% of the normal amount. Deletions in the dystrophin gene represent 65% of mutations in DMD/BMD patients. To explain the contribution of immunohistochemical and genetic analysis in the diagnosis of these dystrophies, we present 10 cases of DMD/BMD with particular features. We have analyzed the patients with immunohistochemical staining and PCR multiplex to sc

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Bernier-Parker, Nathan, Trevor W. Moore, Laura B. Stainback, et al. "Dystrophin-Deficient Muscular Dystrophy in an Australian Cattle Dog (Blue Heeler)." Journal of the American Animal Hospital Association 61, no. 4 (2025): 107–10. https://doi.org/10.5326/jaaha-ms-7480.

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ABSTRACT X-linked dystrophin-deficient muscular dystrophy is associated with a mutation of the DYS gene located on the X chromosome. To date, dystrophinopathy has been identified in 16 different dog breeds with 20 different variants confirmed. In this report, a 9 mo old male Australian cattle dog was evaluated for progressive generalized weakness and dysphagia beginning at 4 mo of age. A markedly elevated creatine kinase activity was noted on blood chemistry, and muscle biopsies confirmed a dystrophic phenotype. Dystrophin deficiency was identified by immunohistochemistry. In this report we id

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Gumerson, Jessica D., and Daniel E. Michele. "The Dystrophin-Glycoprotein Complex in the Prevention of Muscle Damage." Journal of Biomedicine and Biotechnology 2011 (2011): 1–13. http://dx.doi.org/10.1155/2011/210797.

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Muscular dystrophies are genetically diverse but share common phenotypic features of muscle weakness, degeneration, and progressive decline in muscle function. Previous work has focused on understanding how disruptions in the dystrophin-glycoprotein complex result in muscular dystrophy, supporting a hypothesis that the muscle sarcolemma is fragile and susceptible to contraction-induced injury in multiple forms of dystrophy. Although benign in healthy muscle, contractions in dystrophic muscle may contribute to a higher degree of muscle damage which eventually overwhelms muscle regeneration capa

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Spiro, Alfred J. "Muscular Dystrophy." Pediatrics In Review 16, no. 11 (1995): 437. http://dx.doi.org/10.1542/pir.16.11.437.

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Several varieties of muscular dystrophy can be distinguished on clinical, genetic, morphologic, and physiologic grounds. The classification includes Duchenne and Becker muscular dystrophies, both X-linked disorders; facioscapulohumeral muscular dystrophy, which is autosomal dominant; and limb-girdle muscular dystrophy, generally autosomal recessive. Duchenne muscular dystrophy (DMD), which occurs in approximately 1 in 3500 live male births, has no recognizable signs or symptoms at birth. However, markedly elevated serum creatine kinase always is demonstrable, even at birth. A molecular diagnos

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Ohlendieck, K., and K. P. Campbell. "Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice." Journal of Cell Biology 115, no. 6 (1991): 1685–94. http://dx.doi.org/10.1083/jcb.115.6.1685.

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Dystrophin, the protein product of the human Duchenne muscular dystrophy gene, exists in skeletal muscle as a large oligomeric complex that contains four glycoproteins of 156, 50, 43, and 35 kD and a protein of 59 kD. Here, we investigated the relative abundance of each of the components of the dystrophin-glycoprotein complex in skeletal muscle from normal and mdx mice, which are missing dystrophin. Immunoblot analysis using total muscle membranes from control and mdx mice of ages 1 d to 30 wk found that all of the dystrophin-associated proteins were greatly reduced (80-90%) in mdx mouse skele

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Echigoya, Yusuke, Akinori Nakamura, Tetsuya Nagata, et al. "Effects of systemic multiexon skipping with peptide-conjugated morpholinos in the heart of a dog model of Duchenne muscular dystrophy." Proceedings of the National Academy of Sciences 114, no. 16 (2017): 4213–18. http://dx.doi.org/10.1073/pnas.1613203114.

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Duchenne muscular dystrophy (DMD) is a lethal genetic disorder caused by an absence of the dystrophin protein in bodywide muscles, including the heart. Cardiomyopathy is a leading cause of death in DMD. Exon skipping via synthetic phosphorodiamidate morpholino oligomers (PMOs) represents one of the most promising therapeutic options, yet PMOs have shown very little efficacy in cardiac muscle. To increase therapeutic potency in cardiac muscle, we tested a next-generation morpholino: arginine-rich, cell-penetrating peptide-conjugated PMOs (PPMOs) in the canine X-linked muscular dystrophy in Japa

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Corrado, K., J. A. Rafael, P. L. Mills, et al. "Transgenic mdx mice expressing dystrophin with a deletion in the actin-binding domain display a "mild Becker" phenotype." Journal of Cell Biology 134, no. 4 (1996): 873–84. http://dx.doi.org/10.1083/jcb.134.4.873.

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The functional significance of the actin-binding domain of dystrophin, the protein lacking in patients with Duchenne muscular dystrophy, has remained elusive. Patients with deletions of this domain (domain I) typically express low levels of the truncated protein. Whether the moderate to severe phenotypes associated with such deletions result from loss of an essential function, or from reduced levels of a functional protein, is unclear. To address this question, we have generated transgenic mice that express wild-type levels of a dystrophin deleted for the majority of the actin-binding domain.

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Spinazzola, Janelle M., Matthias R. Lambert, Devin E. Gibbs, et al. "Effect of serotonin modulation on dystrophin-deficient zebrafish." Biology Open 9, no. 8 (2020): bio053363. http://dx.doi.org/10.1242/bio.053363.

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ABSTRACTDuchenne muscular dystrophy (DMD) is a progressive muscle-wasting disease caused by mutation of the dystrophin gene. Pharmacological therapies that function independently of dystrophin and complement strategies aimed at dystrophin restoration could significantly improve patient outcomes. Previous observations have suggested that serotonin pathway modulation ameliorates dystrophic pathology, and re-application of serotonin modulators already used clinically would potentially hasten availability to DMD patients. In our study, we used dystrophin-deficient sapje and sapje-like zebrafish mo

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Guiraud, Simon, Benjamin Edwards, Arran Babbs, et al. "The potential of utrophin and dystrophin combination therapies for Duchenne muscular dystrophy." Human Molecular Genetics 28, no. 13 (2019): 2189–200. http://dx.doi.org/10.1093/hmg/ddz049.

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Abstract Duchenne muscular dystrophy (DMD) is a lethal neuromuscular disorder caused by loss of dystrophin. Several therapeutic modalities are currently in clinical trials but none will achieve maximum functional rescue and full disease correction. Therefore, we explored the potential of combining the benefits of dystrophin with increases of utrophin, an autosomal paralogue of dystrophin. Utrophin and dystrophin can be co-expressed and co-localized at the same muscle membrane. Wild-type (wt) levels of dystrophin are not significantly affected by a moderate increase of utrophin whereas higher l

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Hilton, Stephanie, Matthias Christen, Thomas Bilzer, Vidhya Jagannathan, Tosso Leeb, and Urs Giger. "Dystrophin (DMD) Missense Variant in Cats with Becker-Type Muscular Dystrophy." International Journal of Molecular Sciences 24, no. 4 (2023): 3192. http://dx.doi.org/10.3390/ijms24043192.

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Muscular dystrophy due to dystrophin deficiency in humans is phenotypically divided into a severe Duchenne and milder Becker type. Dystrophin deficiency has also been described in a few animal species, and few DMD gene variants have been identified in animals. Here, we characterize the clinical, histopathological, and molecular genetic aspects of a family of Maine Coon crossbred cats with clinically mild and slowly progressive muscular dystrophy. Two young adult male littermate cats exhibited abnormal gait and muscular hypertrophy with macroglossia. Serum creatine kinase activities were highly

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Spaulding, Hannah R., Tiffany Quindry, Kayleen Hammer, John C. Quindry, and Joshua T. Selsby. "Nutraceutical and pharmaceutical cocktails did not improve muscle function or reduce histological damage in D2-mdx mice." Journal of Applied Physiology 127, no. 4 (2019): 1058–66. http://dx.doi.org/10.1152/japplphysiol.00162.2019.

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Progressive muscle injury and weakness are hallmarks of Duchenne muscular dystrophy. We showed previously that quercetin (Q) partially protected dystrophic limb muscles from disease-related injury. As quercetin activates PGC-1α through Sirtuin-1, an NAD+-dependent deacetylase, the depleted NAD+ in dystrophic skeletal muscle may limit quercetin efficacy; hence, supplementation with the NAD+ donor, nicotinamide riboside (NR), may facilitate quercetin efficacy. Lisinopril (Lis) protects skeletal muscle and improves cardiac function in dystrophin-deficient mice; therefore, it was included in this

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Wehling, Michelle, Melissa J. Spencer, and James G. Tidball. "A nitric oxide synthase transgene ameliorates muscular dystrophy in mdx mice." Journal of Cell Biology 155, no. 1 (2001): 123–32. http://dx.doi.org/10.1083/jcb.200105110.

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Dystrophin-deficient muscles experience large reductions in expression of nitric oxide synthase (NOS), which suggests that NO deficiency may influence the dystrophic pathology. Because NO can function as an antiinflammatory and cytoprotective molecule, we propose that the loss of NOS from dystrophic muscle exacerbates muscle inflammation and fiber damage by inflammatory cells. Analysis of transgenic mdx mice that were null mutants for dystrophin, but expressed normal levels of NO in muscle, showed that the normalization of NO production caused large reductions in macrophage concentrations in t

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Nogami, Ken'ichiro, Yusuke Maruyama, Fusako Sakai-Takemura, et al. "Pharmacological activation of SERCA ameliorates dystrophic phenotypes in dystrophin-deficient mdx mice." Human Molecular Genetics 30, no. 11 (2021): 1006–19. http://dx.doi.org/10.1093/hmg/ddab100.

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Abstract Duchenne muscular dystrophy (DMD) is an X-linked genetic disorder characterized by progressive muscular weakness because of the loss of dystrophin. Extracellular Ca2+ flows into the cytoplasm through membrane tears in dystrophin-deficient myofibers, which leads to muscle contracture and necrosis. Sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) takes up cytosolic Ca2+ into the sarcoplasmic reticulum, but its activity is decreased in dystrophic muscle. Here, we show that an allosteric SERCA activator, CDN1163, ameliorates dystrophic phenotypes in dystrophin-deficient mdx mice. The admin

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Sazani, Peter, Kirk P. Van Ness, Doreen L. Weller, Duane Poage, Keith Nelson, and and Stephen B. Shrewsbury. "Chemical and Mechanistic Toxicology Evaluation of Exon Skipping Phosphorodiamidate Morpholino Oligomers in mdx Mice." International Journal of Toxicology 30, no. 3 (2011): 322–33. http://dx.doi.org/10.1177/1091581811403504.

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AVI-4658 is a phosphorodiamidate morpholino oligomer (PMO) designed to induce skipping of dystrophin exon 51 and restore its expression in patients with Duchenne muscular dystrophy (DMD). Preclinically, restoration of dystrophin in the dystrophic mdx mouse model requires skipping of exon 23, achieved with the mouse-specific PMO, AVI-4225. Herein, we report the potential toxicological consequences of exon skipping and dystrophin restoration in mdx mice using AVI-4225. We also evaluated the toxicological effects of AVI-4658 in both mdx and wild-type mice. In both studies, animals were dosed once

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EBIHARA, SATORU, GHIABE-HENRI GUIBINGA, RENALD GILBERT, et al. "Differential effects of dystrophin and utrophin gene transfer in immunocompetent muscular dystrophy (mdx) mice." Physiological Genomics 3, no. 3 (2000): 133–44. http://dx.doi.org/10.1152/physiolgenomics.2000.3.3.133.

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Ebihara, Satoru, Ghiabe-Henri Guibinga, Renald Gilbert, Josephine Nalbantoglu, Bernard Massie, George Karpati, and Basil J. Petrof. Differential effects of dystrophin and utrophin gene transfer in immunocompetent muscular dystrophy (mdx) mice. Physiol Genomics 3: 133–144, 2000.—Duchenne muscular dystrophy (DMD) is a fatal disease caused by defects in the gene encoding dystrophin. Dystrophin is a cytoskeletal protein, which together with its associated protein complex, helps to protect the sarcolemma from mechanical stresses associated with muscle contraction. Gene therapy efforts aimed at supp

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Koenig, Xaver, Lena Rubi, Gerald J. Obermair, et al. "Enhanced currents through L-type calcium channels in cardiomyocytes disturb the electrophysiology of the dystrophic heart." American Journal of Physiology-Heart and Circulatory Physiology 306, no. 4 (2014): H564—H573. http://dx.doi.org/10.1152/ajpheart.00441.2013.

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Duchenne muscular dystrophy (DMD), induced by mutations in the gene encoding for the cytoskeletal protein dystrophin, is an inherited disease characterized by progressive muscle weakness. Besides the relatively well characterized skeletal muscle degenerative processes, DMD is also associated with cardiac complications. These include cardiomyopathy development and cardiac arrhythmias. The current understanding of the pathomechanisms in the heart is very limited, but recent research indicates that dysfunctional ion channels in dystrophic cardiomyocytes play a role. The aim of the present study w

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Beckers, Evy, Ine Cornelis, Sofie F. M. Bhatti, et al. "A Nonsense Variant in the DMD Gene Causes X-Linked Muscular Dystrophy in the Maine Coon Cat." Animals 12, no. 21 (2022): 2928. http://dx.doi.org/10.3390/ani12212928.

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(1) Feline dystrophin-deficient muscular dystrophy (ddMD) is a fatal disease characterized by progressive weakness and degeneration of skeletal muscles and is caused by variants in the DMD gene. To date, only two feline causal variants have been identified. This study reports two cases of male Maine coon siblings that presented with muscular hypertrophy, growth retardation, weight loss, and vomiting. (2) Both cats were clinically examined and histopathology and immunofluorescent staining of the affected muscle was performed. DMD mRNA was sequenced to identify putative causal variants. (3) Both

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Menke, A., and H. Jockusch. "Extent of shock-induced membrane leakage in human and mouse myotubes depends on dystrophin." Journal of Cell Science 108, no. 2 (1995): 727–33. http://dx.doi.org/10.1242/jcs.108.2.727.

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A lack of the cytoskeletal protein dystrophin causes muscle fiber necrosis in Duchenne/Becker muscular dystrophies (DMD/BMD) and in murine X-linked muscular dystrophy (MDX). However, no overt disease symptoms are observed in dystrophin-less cultured myotubes, and the biological function of dystrophin in normal muscle cells is still unknown. In this work, we have extended our studies on a model system, using hypoosmotic shock to determine stress resistance of muscle cells. In frozen sections of control human and mouse myotubes, dystrophin was shown to be localized at the cell periphery as in ma

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Kochergin-Nikitskiy, K. S., S. A. Smirnikhina, and A. V. Lavrov. "Stages of research and development of therapeutic approaches for Duchenne myodystrophy. Part II: etiotropic approaches." Neuromuscular Diseases 14, no. 2 (2024): 44–52. http://dx.doi.org/10.17650/2222-8721-2024-14-2-44-52.

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Duchenne muscular dystrophy is one of the most common inherited muscular dystrophies. The cause of this disease with an X‑linked recessive type of inheritance is mutations in the DMD gene, leading to the absence of the dystrophin protein this gene encodes or its impaired function. Loss of dystrophin leads to severe degenerative processes in patients, especially in muscle tissue, with impaired muscle function, loss of ability to move independently, respiratory failure, cardiomyopathies, etc.The collective efforts of many researchers over the years since the 19th century, when the diseases was d

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Murphy, Sandra, Margit Zweyer, Rustam R. Mundegar, Dieter Swandulla та Kay Ohlendieck. "Chemical crosslinking analysis of β-dystroglycan in dystrophin-deficient skeletal muscle". HRB Open Research 1 (30 травня 2018): 17. http://dx.doi.org/10.12688/hrbopenres.12846.1.

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Background: In Duchenne muscular dystrophy, primary abnormalities in the membrane cytoskeletal protein dystrophin trigger the loss of sarcolemmal linkage between the extracellular matrix component laminin-211 and the intracellular cortical actin membrane cytoskeleton. The disintegration of the dystrophin-associated glycoprotein complex renders the plasma membrane of contractile fibres more susceptible to micro-rupturing, which is associated with abnormal calcium handling and impaired cellular signalling in dystrophinopathy. Methods: The oligomerisation pattern of β-dystroglycan, an integral me

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Holland, Ashling, and Kay Ohlendieck. "Proteomic Profiling of the Dystrophin-DeficientmdxPhenocopy of Dystrophinopathy-Associated Cardiomyopathy." BioMed Research International 2014 (2014): 1–15. http://dx.doi.org/10.1155/2014/246195.

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Cardiorespiratory complications are frequent symptoms of Duchenne muscular dystrophy, a neuromuscular disorder caused by primary abnormalities in the dystrophin gene. Loss of cardiac dystrophin initially leads to changes in dystrophin-associated glycoproteins and subsequently triggers secondarily sarcolemmal disintegration, fibre necrosis, fibrosis, fatty tissue replacement, and interstitial inflammation. This results in progressive cardiac disease, which is the cause of death in a considerable number of patients afflicted with X-linked muscular dystrophy. In order to better define the molecul

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Wells, Dominic J., Aurora Ferrer, and Kim E. Wells. "Immunological hurdles in the path to gene therapy for Duchenne muscular dystrophy." Expert Reviews in Molecular Medicine 4, no. 23 (2002): 1–23. http://dx.doi.org/10.1017/s146239940200515x.

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Patients with Duchenne muscular dystrophy (DMD), an X-linked lethal muscle-wasting disease, have abnormal expression of the protein dystrophin within their muscle fibres. In the mdx mouse model of this condition, both germline and neonatal somatic gene transfers of dystrophin cDNAs have demonstrated the potential of gene therapy in treating DMD. However, in many DMD patients, there appears to be no dystrophin expression when muscle biopsies are immunostained or western blots are performed. This raises the possibility that the expression of dystrophin following gene transfer might trigger a des

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Iwata, Yuko, Yuki Katanosaka, Yuji Arai, Kazuo Komamura, Kunio Miyatake, and Munekazu Shigekawa. "A novel mechanism of myocyte degeneration involving the Ca2+-permeable growth factor–regulated channel." Journal of Cell Biology 161, no. 5 (2003): 957–67. http://dx.doi.org/10.1083/jcb.200301101.

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Disruption of the dystrophin–glycoprotein complex caused by genetic defects of dystrophin or sarcoglycans results in muscular dystrophy and/or cardiomyopathy in humans and animal models. However, the key early molecular events leading to myocyte degeneration remain elusive. Here, we observed that the growth factor–regulated channel (GRC), which belongs to the transient receptor potential channel family, is elevated in the sarcolemma of skeletal and/or cardiac muscle in dystrophic human patients and animal models deficient in dystrophin or δ-sarcoglycan. However, total cell GRC does not differ

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Morotti, Marta, Alessandro Gaeta, Cristina Limatola, Myriam Catalano, Maria Amalia Di Castro, and Francesca Grassi. "Early Developmental Changes of Muscle Acetylcholine Receptors Are Little Influenced by Dystrophin Absence in mdx Mouse." Life 12, no. 11 (2022): 1861. http://dx.doi.org/10.3390/life12111861.

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Dystrophin is a cytoskeletal protein contributing to the organization of the neuromuscular junction. In Duchenne muscular dystrophy, due to dystrophin absence, the distribution of endplate acetylcholine receptors (AChRs) becomes disorganized. It is still debated whether this is due to the absence of dystrophin or to the repeated damage/regeneration cycles typical of dystrophic muscle. We addressed this controversy studying the endplate in the first 3 postnatal weeks, when muscle damage in dystrophic (mdx) mice is minimal. By synaptic and extra-synaptic patch-clamp recordings in acutely dissoci

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Hack, Andrew A., Chantal T. Ly, Fang Jiang та ін. "γ-Sarcoglycan Deficiency Leads to Muscle Membrane Defects and Apoptosis Independent of Dystrophin". Journal of Cell Biology 142, № 5 (1998): 1279–87. http://dx.doi.org/10.1083/jcb.142.5.1279.

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γ-Sarcoglycan is a transmembrane, dystrophin-associated protein expressed in skeletal and cardiac muscle. The murine γ-sarcoglycan gene was disrupted using homologous recombination. Mice lacking γ-sarcoglycan showed pronounced dystrophic muscle changes in early life. By 20 wk of age, these mice developed cardiomyopathy and died prematurely. The loss of γ-sarcoglycan produced secondary reduction of β- and δ-sarcoglycan with partial retention of α- and ε-sarcoglycan, suggesting that β-, γ-, and δ-sarcoglycan function as a unit. Importantly, mice lacking γ-sarco- glycan showed normal dystrophin c

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Lu, Q. L., G. E. Morris, S. D. Wilton, et al. "Massive Idiosyncratic Exon Skipping Corrects the Nonsense Mutation in Dystrophic Mouse Muscle and Produces Functional Revertant Fibers by Clonal Expansion." Journal of Cell Biology 148, no. 5 (2000): 985–96. http://dx.doi.org/10.1083/jcb.148.5.985.

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Conventionally, nonsense mutations within a gene preclude synthesis of a full-length functional protein. Obviation of such a blockage is seen in the mdx mouse, where despite a nonsense mutation in exon 23 of the dystrophin gene, occasional so-called revertant muscle fibers are seen to contain near-normal levels of its protein product. Here, we show that reversion of dystrophin expression in mdx mice muscle involves unprecedented massive loss of up to 30 exons. We detected several alternatively processed transcripts that could account for some of the revertant dystrophins and could not detect g

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Mázala, Davi A. G., Robert W. Grange, and Eva R. Chin. "The role of proteases in excitation-contraction coupling failure in muscular dystrophy." American Journal of Physiology-Cell Physiology 308, no. 1 (2015): C33—C40. http://dx.doi.org/10.1152/ajpcell.00267.2013.

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Duchenne muscular dystrophy (DMD) is one of the most frequent types of muscular dystrophy. Alterations in intracellular calcium (Ca2+) handling are thought to contribute to the disease severity in DMD, possibly due to the activation of Ca2+-activated proteases. The purpose of this study was twofold: 1) to determine whether prolonged excitation-contraction (E-C) coupling disruption following repeated contractions is greater in animals lacking both dystrophin and utrophin ( mdx/Utr−/−) compared with mice lacking only dystrophin ( mdx); and 2) to assess whether protease inhibition can prevent E-C

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Watchko, Jon F., Terrence L. O'Day, and Eric P. Hoffman. "Functional characteristics of dystrophic skeletal muscle: insights from animal models." Journal of Applied Physiology 93, no. 2 (2002): 407–17. http://dx.doi.org/10.1152/japplphysiol.01242.2001.

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Muscular dystrophies are a clinically and genetically heterogeneous group of disorders that show myofiber degeneration and regeneration. Identification of animal models of muscular dystrophy has been instrumental in research on the pathogenesis, pathophysiology, and treatment of these disorders. We review our understanding of the functional status of dystrophic skeletal muscle from selected animal models with a focus on 1) the mdx mouse model of Duchenne muscular dystrophy, 2) the Bio 14.6 δ-sarcoglycan-deficient hamster model of limb-girdle muscular dystrophy, and 3) transgenic null mutant mu

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Niebrój-Dobosz, Irena, and Irena Hausmanowa-Petrusewicz. "The involvement of oxidative stress in determining the severity and progress of pathological processes in dystrophin-deficient muscles." Acta Biochimica Polonica 52, no. 2 (2005): 449–52. http://dx.doi.org/10.18388/abp.2005_3458.

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In both forms of muscular dystrophy, the severe Duchenne's muscular dystrophy (DMD) with lifespan shortened to about 20 years and the milder Becker dystrophy (BDM) with normal lifespan, the gene defect is located at chromosome locus Xp21. The location is the same in the experimental model of DMD in the mdx mice. As the result of the gene defect a protein called dystrophin is either not synthesized, or is produced in traces. Although the structure of this protein is rather well established there are still many controversies about the dystrophin function. The most accepted suggestion supposes th

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Akanksha, Mishra, Sairkar Pramod, Silawat Nipun, Maruf Khan Mohd., and Kothari Anil. "Structural Homology Modeling of C-Terminal Domain of the Dystrophin Protein: An in-Silico Approach." Structural Homology Modeling of C-Terminal Domain of the Dystrophin Protein: An in-Silico Approach 9, no. 1 (2024): 8. https://doi.org/10.5281/zenodo.10639763.

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Dystrophin is one of the most significant and well-researched cytoskeletal proteins that is prominently expressed in skeletal and cardiac muscles. It is a large 400-kD protein, which is encoded by the largest gene in the human body- DMD gene. A significant decrease in dystrophin levels in muscles results in a gradual and severe skeletal muscular weakening. Lack of dystrophin results in muscular dystrophies such as DMD (Duchenne muscular dystrophy) and BMD (Becker muscular dystrophy. Understanding the dystrophin protein's structure is crucial for developing a cure for the disease. Comprehensive

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