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Journal articles on the topic 'Genetics in muscular dystrophy'

Author: Grafiati

Published: 4 June 2021

Last updated: 15 February 2022

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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 (October 20, 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. In contrast, mdx mice, a dystrophin-deficient animal model for Duchenne muscular dystrophy, showed significant Evans blue accumulation in skeletal muscle fibers. We also studied Evans blue dispersion in transgenic mice bearing different dystrophin mutations, and we demonstrated that cytoskeletal and sarcolemmal attachment of dystrophin might be a necessary requirement to prevent serious fiber damage. The extent of dye incorporation in transgenic mice correlated with the phenotypic severity of similar dystrophin mutations in humans. We furthermore assessed Evans blue incorporation in skeletal muscle of the dystrophia muscularis (dy/dy) mouse and its milder allelic variant, the dy2J/dy2J mouse, animal models for congenital muscular dystrophy. Surprisingly, these mice, which have defects in the laminin α2-chain, an extracellular ligand of the DGC, showed little Evans blue accumulation in their skeletal muscles. Taken together, these results suggest that the pathogenic mechanisms in congenital muscular dystrophy are different from those in Duchenne muscular dystrophy, although the primary defects originate in two components associated with the same protein complex.

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2

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 (April 1, 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. Although the precise function of dystrophin is unknown, the lack of protein causes membrane destabilization and the activation of multiple pathophysiological processes, many of which converge on alterations in intracellular calcium handling. Dystrophin is also the prototype of a family of dystrophin-related proteins, many of which are found in muscle. This family includes utrophin and α-dystrobrevin, which are involved in the maintenance of the neuromuscular junction architecture and in muscle homeostasis. New insights into the pathophysiology of dystrophic muscle, the identification of compensating proteins, and the discovery of new binding partners are paving the way for novel therapeutic strategies to treat this fatal muscle disease. This review discusses the role of the dystrophin complex and protein family in muscle and describes the physiological processes that are affected in Duchenne muscular dystrophy.

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3

Sitzia, Clementina, Andrea Farini, Federica Colleoni, Francesco Fortunato, Paola Razini, Silvia Erratico, Alessandro Tavelli, et al. "Improvement of Endurance of DMD Animal Model Using Natural Polyphenols." BioMed Research International 2015 (2015): 1–17. http://dx.doi.org/10.1155/2015/680615.

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Duchenne muscular dystrophy (DMD), the most common form of muscular dystrophy, is characterized by muscular wasting caused by dystrophin deficiency that ultimately ends in force reduction and premature death. In addition to primary genetic defect, several mechanisms contribute to DMD pathogenesis. Recently, antioxidant supplementation was shown to be effective in the treatment of multiple diseases including muscular dystrophy. Different mechanisms were hypothesized such as reduced hydroxyl radicals, nuclear factor-κB deactivation, and NO protection from inactivation. Following these promising evidences, we investigated the effect of the administration of a mix of dietary natural polyphenols (ProAbe) on dystrophic mdx mice in terms of muscular architecture and functionality. We observed a reduction of muscle fibrosis deposition and myofiber necrosis together with an amelioration of vascularization. More importantly, the recovery of the morphological features of dystrophic muscle leads to an improvement of the endurance of treated dystrophic mice. Our data confirmed that ProAbe-based diet may represent a strategy to coadjuvate the treatment of DMD.

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4

Teramoto, Naomi, Hidetoshi Sugihara, Keitaro Yamanouchi, Katsuyuki Nakamura, Koichi Kimura, Tomoko Okano, Takanori Shiga, 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 (August 28, 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 novel rat model carrying in-frame Dmd gene mutations (IF rats) and evaluated the pathology. We found that IF rats exhibited reduced expression of truncated dystrophin in a proteasome-independent manner. This abnormal dystrophin expression caused dystrophic changes in muscle tissues but did not lead to functional deficiency. We also found that the expression of additional dystrophin named dpX, which forms the DGC in the sarcolemma, was associated with the appearance of truncated dystrophin. In conclusion, the outcomes of this study contribute to the further understanding of BMD pathology and help elucidate the efficiency of dystrophin recovery treatments in Duchenne muscular dystrophy, a more severe form of X-linked muscular dystrophy.

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5

Nogami, Ken'ichiro, Yusuke Maruyama, Fusako Sakai-Takemura, Norio Motohashi, Ahmed Elhussieny, Michihiro Imamura, Satoshi Miyashita, et al. "Pharmacological activation of SERCA ameliorates dystrophic phenotypes in dystrophin-deficient mdx mice." Human Molecular Genetics 30, no. 11 (April 5, 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 administration of CDN1163 prevented exercise-induced muscular damage and restored mitochondrial function. In addition, treatment with CDN1163 for 7 weeks enhanced muscular strength and reduced muscular degeneration and fibrosis in mdx mice. Our findings provide preclinical proof-of-concept evidence that pharmacological activation of SERCA could be a promising therapeutic strategy for DMD. Moreover, CDN1163 improved muscular strength surprisingly in wild-type mice, which may pave the new way for the treatment of muscular dysfunction.

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6

Sun, Chengmei, Luoan Shen, Zheng Zhang, and Xin Xie. "Therapeutic Strategies for Duchenne Muscular Dystrophy: An Update." Genes 11, no. 8 (July 23, 2020): 837. http://dx.doi.org/10.3390/genes11080837.

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Neuromuscular disorders encompass a heterogeneous group of conditions that impair the function of muscles, motor neurons, peripheral nerves, and neuromuscular junctions. Being the most common and most severe type of muscular dystrophy, Duchenne muscular dystrophy (DMD), is caused by mutations in the X-linked dystrophin gene. Loss of dystrophin protein leads to recurrent myofiber damage, chronic inflammation, progressive fibrosis, and dysfunction of muscle stem cells. Over the last few years, there has been considerable development of diagnosis and therapeutics for DMD, but current treatments do not cure the disease. Here, we review the current status of DMD pathogenesis and therapy, focusing on mutational spectrum, diagnosis tools, clinical trials, and therapeutic approaches including dystrophin restoration, gene therapy, and myogenic cell transplantation. Furthermore, we present the clinical potential of advanced strategies combining gene editing, cell-based therapy with tissue engineering for the treatment of muscular dystrophy.

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7

Foncuberta, M., F. Lubieniecki, L. Gravina, L. González Quereda, P. Gallano, L. Chertkoff, and S. Monges. "DUCHENNE MUSCULAR DYSTROPHY - GENETICS." Neuromuscular Disorders 28 (October 2018): S96—S97. http://dx.doi.org/10.1016/j.nmd.2018.06.260.

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8

Neri, M., A. Mauro, F. Gualandi, C. Bruno, F. Santorelli, S. Tedeschi, A. D'Amico, et al. "DUCHENNE MUSCULAR DYSTROPHY - GENETICS." Neuromuscular Disorders 28 (October 2018): S97. http://dx.doi.org/10.1016/j.nmd.2018.06.261.

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9

Lara, S., V. Saez, P. Santander, G. Fariña, M. Troncoso, and G. Legaza. "DUCHENNE MUSCULAR DYSTROPHY - GENETICS." Neuromuscular Disorders 28 (October 2018): S97. http://dx.doi.org/10.1016/j.nmd.2018.06.262.

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10

Schottlaender, L., J. Domingos, L. D'Argenzio, I. Zaharieva, P. Ala, A. Manzur, J. Bourke, J. Morgan, and F. Muntoni. "DUCHENNE MUSCULAR DYSTROPHY - GENETICS." Neuromuscular Disorders 28 (October 2018): S97. http://dx.doi.org/10.1016/j.nmd.2018.06.263.

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11

Sampaio, H., D. Kariyawasam, M. Buckley, D. Mowat, J. Robinson, P. Taylor, K. Jones, and M. Farrar. "DUCHENNE MUSCULAR DYSTROPHY - GENETICS." Neuromuscular Disorders 28 (October 2018): S97—S98. http://dx.doi.org/10.1016/j.nmd.2018.06.264.

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12

Al Zaidy, S., E. Camino, N. Miller, K. Lehman, L. Lowes, L. Alfano, M. Iammarino, et al. "DUCHENNE MUSCULAR DYSTROPHY - GENETICS." Neuromuscular Disorders 28 (October 2018): S98. http://dx.doi.org/10.1016/j.nmd.2018.06.265.

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13

Solheim, T., F. Fornander, R. Møgelvang, N. Poulsen, A. Andersen, A. Eisum, M. Duno, H. Bundgaard, and J. Vissing. "DUCHENNE MUSCULAR DYSTROPHY - GENETICS." Neuromuscular Disorders 28 (October 2018): S98. http://dx.doi.org/10.1016/j.nmd.2018.06.266.

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14

Mah, M., L. Cripe, S. Al-Zaidy, E. Camino, M. Slawinski, J. Jackson, J. Mendell, and K. Hor. "DUCHENNE MUSCULAR DYSTROPHY - GENETICS." Neuromuscular Disorders 28 (October 2018): S98—S99. http://dx.doi.org/10.1016/j.nmd.2018.06.267.

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15

Passos, S., P. Tavares, T. Rezende, L. Souza, T. Rosa, C. Iwabe-Marchese, A. Nucci, and M. França. "DUCHENNE MUSCULAR DYSTROPHY - GENETICS." Neuromuscular Disorders 28 (October 2018): S99. http://dx.doi.org/10.1016/j.nmd.2018.06.268.

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16

van Duyvenvoorde, H., D. van Heusden, M. Hoffer, and H. Ginjaar. "DUCHENNE MUSCULAR DYSTROPHY - GENETICS." Neuromuscular Disorders 28 (October 2018): S99. http://dx.doi.org/10.1016/j.nmd.2018.06.269.

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17

Poyatos, J., C. Gomis, N. Muelas, P. Marti, and J. Vilchez. "DUCHENNE MUSCULAR DYSTROPHY - GENETICS." Neuromuscular Disorders 28 (October 2018): S99. http://dx.doi.org/10.1016/j.nmd.2018.06.270.

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18

Luce, L., M. Carcione, C. Mazzanti, L. Mesa, A. Dubrovsky, and F. Giliberto. "DUCHENNE MUSCULAR DYSTROPHY - GENETICS." Neuromuscular Disorders 28 (October 2018): S99—S100. http://dx.doi.org/10.1016/j.nmd.2018.06.271.

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19

Ille, A., W. M. Schmidt, M. Gosk-Tomek, S. Weiss, M. Freilinger, R. E. Bittner, and G. Bernert. "DUCHENNE MUSCULAR DYSTROPHY - GENETICS." Neuromuscular Disorders 28 (October 2018): S100. http://dx.doi.org/10.1016/j.nmd.2018.06.272.

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20

Min, Yi-Li, Rhonda Bassel-Duby, and Eric N. Olson. "CRISPR Correction of Duchenne Muscular Dystrophy." Annual Review of Medicine 70, no. 1 (January 27, 2019): 239–55. http://dx.doi.org/10.1146/annurev-med-081117-010451.

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The ability to efficiently modify the genome using CRISPR technology has rapidly revolutionized biology and genetics and will soon transform medicine. Duchenne muscular dystrophy (DMD) represents one of the first monogenic disorders that has been investigated with respect to CRISPR-mediated correction of causal genetic mutations. DMD results from mutations in the gene encoding dystrophin, a scaffolding protein that maintains the integrity of striated muscles. Thousands of different dystrophin mutations have been identified in DMD patients, who suffer from a loss of ambulation followed by respiratory insufficiency, heart failure, and death by the third decade of life. Using CRISPR to bypass DMD mutations, dystrophin expression has been efficiently restored in human cells and mouse models of DMD. Here, we review recent progress toward the development of possible CRISPR therapies for DMD and highlight opportunities and potential obstacles in attaining this goal.

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21

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 (May 25, 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 that it stabilizes sarcolemma in the course of the contraction-relaxation cycle. Solving the problem of dystrophin function is a prerequisite for introduction of an effective therapy. Among the different factors which might be responsible for the appearance and progress of dystrophic changes in muscles there is an excessive action of oxidative stress. In this review data indicating the influence of oxidative stress on the severity of the pathologic processes in dystrophy are discussed. Several pieces of data indicating the action of oxidative damage to different macromolecules in DMD/BDM are presented. Special attention is devoted to the degree of oxidative damage to muscle proteins, the activity of neuronal nitric oxide synthase (nNOS) and their involvement in defining the severity of the dystrophic processes. It is indicated that the severity of the morbid process is related to the degree of oxidative damage to muscle proteins and the decrease of the nNOS activity in muscles. Estimation of the degree of the destructive action of oxidative stress in muscular dystrophy may be a useful marker facilitating introduction of an effective antioxidant therapy and regulation of nNOS activity.

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22

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 redox signaling cascades is poorly understood. We report that mdx dystrophic mice are able to activate a compensatory antioxidant response at the presymptomatic stage of the disease. In contrast, increased circulating levels of IL-6 perturb the redox signaling cascade, even prior to the necrotic stage, leading to severe features and progressive nature of muscular dystrophy.

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23

Bushby, K. "Duchenne Muscular Dystrophy." Journal of Medical Genetics 31, no. 6 (June 1, 1994): 506. http://dx.doi.org/10.1136/jmg.31.6.506.

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24

Bundey, S. "Duchenne Muscular Dystrophy." Journal of Medical Genetics 25, no. 2 (February 1, 1988): 140. http://dx.doi.org/10.1136/jmg.25.2.140.

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25

Bundey, S. "Duchenne Muscular Dystrophy." Journal of Medical Genetics 26, no. 6 (June 1, 1989): 416. http://dx.doi.org/10.1136/jmg.26.6.416.

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26

Millichap, J. Gordon. "Genetics of Fukuyama Muscular Dystrophy." Pediatric Neurology Briefs 8, no. 11 (November 1, 1994): 88. http://dx.doi.org/10.15844/pedneurbriefs-8-11-13.

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27

Millichap, J. Gordon. "Genetics of Facioscapulohumeral Muscular Dystrophy." Pediatric Neurology Briefs 5, no. 11 (November 1, 1991): 81. http://dx.doi.org/10.15844/pedneurbriefs-5-11-1.

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28

Worton, R. G., and M. W. Thompson. "Genetics of Duchenne Muscular Dystrophy." Annual Review of Genetics 22, no. 1 (December 1988): 601–29. http://dx.doi.org/10.1146/annurev.ge.22.120188.003125.

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29

Davies, Kay E. "Duchenne muscular dystrophy." Trends in Genetics 3 (January 1987): 231–32. http://dx.doi.org/10.1016/0168-9525(87)90244-7.

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30

Carberry, Steven, Margit Zweyer, Dieter Swandulla, and Kay Ohlendieck. "Profiling of Age-Related Changes in theTibialis AnteriorMuscle Proteome of the mdx Mouse Model of Dystrophinopathy." Journal of Biomedicine and Biotechnology 2012 (2012): 1–11. http://dx.doi.org/10.1155/2012/691641.

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X-linked muscular dystrophy is a highly progressive disease of childhood and characterized by primary genetic abnormalities in the dystrophin gene. Senescent mdx specimens were used for a large-scale survey of potential age-related alterations in the dystrophic phenotype, because the established mdx animal model of dystrophinopathy exhibits progressive deterioration of muscle tissue with age. Since the mdxtibialis anteriormuscle is a frequently used model system in muscular dystrophy research, we employed this particular muscle to determine global changes in the dystrophic skeletal muscle proteome. The comparison of mdx mice aged 8 weeks versus 22 months by mass-spectrometry-based proteomics revealed altered expression levels in 8 distinct protein species. Increased levels were shown for carbonic anhydrase, aldolase, and electron transferring flavoprotein, while the expressions of pyruvate kinase, myosin, tropomyosin, and the small heat shock protein Hsp27 were found to be reduced in aged muscle. Immunoblotting confirmed age-dependent changes in the density of key muscle proteins in mdx muscle. Thus, segmental necrosis in mdxtibialis anteriormuscle appears to trigger age-related protein perturbations due to dystrophin deficiency. The identification of novel indicators of progressive muscular dystrophy might be useful for the establishment of a muscle subtype-specific biomarker signature of dystrophinopathy.

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31

Srivastava, Pallavi, Kiran Preet Malhotra, Nuzhat Husain, Hardeep Singh Malhotra, Dinkar Kulshreshtha, and Akanksha Anand. "Diagnosing Muscular Dystrophies: Comparison of Techniques and Their Cost Effectiveness: A Multi-institutional Study." Journal of Neurosciences in Rural Practice 11, no. 03 (June 12, 2020): 420–29. http://dx.doi.org/10.1055/s-0040-1713301.

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Abstract Background The diagnosis of muscular dystrophies involves clinical discretion substantiated by dystrophic changes on muscle biopsy. The different subtypes of muscular dystrophy can be diagnosed using techniques to identify the loss of protein or molecular alterations. Materials and Methods Clinically suspicious cases confirmed to have muscular dystrophy on muscle biopsy seen at two tertiary care centers in North India were enrolled for the study. Immunohistochemistry (IHC) for dystrophin, merosin, sarcoglycan, emerin, and dysferlin proteins was performed. The spectrum of muscular dystrophies diagnosed was analyzed. Cost of diagnosing the cases using IHC was estimated and compared with that of standard molecular tests available for the diagnosis of muscular dystrophies. Statistics Descriptive statistics were used for data analysis. Mean and standard deviations were used for continuous variables, whereas categorical variables were analyzed using frequency percentage. Results A total of 47 cases of muscular dystrophies were studied. This included nine cases of Duchenne, three cases of Becker’s dystrophy, and one dystrophinopathy carrier. One case of α, seven cases of β, and two cases of δ sarcoglycanopathy, along with two cases of facioscapulohumeral dystrophy and a single case of dysferlinopathy were detected. Genetic studies were required for a subset of 16 cases. The cost of using muscle biopsy and IHC was substantially lower than that of molecular methods for the identification of muscular dystrophy subtypes. Conclusion We detailed an algorithmic approach for diagnosing muscular dystrophies using muscle biopsy. The prevalence of biopsy proven muscular dystrophies from two tertiary care centers in North India is compared with that from other centers. Genetic studies are currently of limited availability in India and are more expensive as compared with biopsy and IHC. Using these methodologies sequentially with a “biopsy first approach” may be the prudent approach for low-income countries.

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Chen, Yi-Wen, Po Zhao, Rehannah Borup, and Eric P. Hoffman. "Expression Profiling in the Muscular Dystrophies." Journal of Cell Biology 151, no. 6 (December 11, 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. One developmentally regulated gene characterized in detail, α-cardiac actin, showed abnormal persistent expression after birth in 60% of Duchenne dystrophy myofibers. The majority of myofibers (∼80%) remained strongly positive for this protein throughout the course of the disease. Other developmentally regulated genes that showed widespread overexpression in these muscular dystrophies included embryonic myosin heavy chain, versican, acetylcholine receptor α-1, secreted protein, acidic and rich in cysteine/osteonectin, and thrombospondin 4. We hypothesize that the abnormal Ca2+ influx in dystrophin- and α-sarcoglycan–deficient myofibers leads to altered developmental programming of developing and regenerating myofibers. The finding of upregulation of HLA-DR and factor XIIIa led to the novel identification of activated dendritic cell infiltration in dystrophic muscle; these cells mediate immune responses and likely induce microenvironmental changes in muscle. We also document a general metabolic crisis in dystrophic muscle, with large scale downregulation of nuclear-encoded mitochondrial gene expression. Finally, our expression profiling results show that primary genetic defects can be identified by a reduction in the corresponding RNA.

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Guiraud, Simon, Benjamin Edwards, Arran Babbs, Sarah E. Squire, Adam Berg, Lee Moir, Matthew J. Wood, and Kay E. Davies. "The potential of utrophin and dystrophin combination therapies for Duchenne muscular dystrophy." Human Molecular Genetics 28, no. 13 (March 5, 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 levels of utrophin reduce wt dystrophin, suggesting a finite number of actin binding sites at the sarcolemma. Thus, utrophin upregulation strategies may be applied to the more mildly affected Becker patients with lower dystrophin levels. Whereas increased dystrophin in wt animals does not offer functional improvement, overexpression of utrophin in wt mice results in a significant supra-functional benefit over wt. These findings highlight an additive benefit of the combined therapy and potential new unique roles of utrophin. Finally, we show a 30% restoration of wt dystrophin levels, using exon-skipping, together with increased utrophin levels restores dystrophic muscle function to wt levels offering greater therapeutic benefit than either single approach alone. Thus, this combination therapy results in additive functional benefit and paves the way for potential future combinations of dystrophin- and utrophin-based strategies.

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34

Chamberlain, Jeffrey S. "Duchenne muscular dystrophy." Current Opinion in Genetics & Development 1, no. 1 (June 1991): 11–14. http://dx.doi.org/10.1016/0959-437x(91)80033-i.

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35

Lim, Kenji Rowel Q., Quynh Nguyen, Kasia Dzierlega, Yiqing Huang, and Toshifumi Yokota. "CRISPR-Generated Animal Models of Duchenne Muscular Dystrophy." Genes 11, no. 3 (March 24, 2020): 342. http://dx.doi.org/10.3390/genes11030342.

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Duchenne muscular dystrophy (DMD) is a fatal X-linked recessive neuromuscular disorder most commonly caused by mutations disrupting the reading frame of the dystrophin (DMD) gene. DMD codes for dystrophin, which is critical for maintaining the integrity of muscle cell membranes. Without dystrophin, muscle cells receive heightened mechanical stress, becoming more susceptible to damage. An active body of research continues to explore therapeutic treatments for DMD as well as to further our understanding of the disease. These efforts rely on having reliable animal models that accurately recapitulate disease presentation in humans. While current animal models of DMD have served this purpose well to some extent, each has its own limitations. To help overcome this, clustered regularly interspaced short palindromic repeat (CRISPR)-based technology has been extremely useful in creating novel animal models for DMD. This review focuses on animal models developed for DMD that have been created using CRISPR, their advantages and disadvantages as well as their applications in the DMD field.

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36

Hilton-Jones, D. "Muscular Dystrophy--The Facts." Journal of Medical Genetics 32, no. 7 (July 1, 1995): 581. http://dx.doi.org/10.1136/jmg.32.7.581.

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37

Statland, Jeffrey M., and Rabi Tawil. "Facioscapulohumeral Muscular Dystrophy." CONTINUUM: Lifelong Learning in Neurology 22, no. 6 (December 2016): 1916–31. http://dx.doi.org/10.1212/con.0000000000000399.

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Suelves, Mònica, Berta Vidal, Antonio L. Serrano, Marc Tjwa, Josep Roma, Roser López-Alemany, Aernout Luttun, et al. "uPA deficiency exacerbates muscular dystrophy in MDX mice." Journal of Cell Biology 178, no. 6 (September 4, 2007): 1039–51. http://dx.doi.org/10.1083/jcb.200705127.

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Duchenne muscular dystrophy (DMD) is a fatal and incurable muscle degenerative disorder. We identify a function of the protease urokinase plasminogen activator (uPA) in mdx mice, a mouse model of DMD. The expression of uPA is induced in mdx dystrophic muscle, and the genetic loss of uPA in mdx mice exacerbated muscle dystrophy and reduced muscular function. Bone marrow (BM) transplantation experiments revealed a critical function for BM-derived uPA in mdx muscle repair via three mechanisms: (1) by promoting the infiltration of BM-derived inflammatory cells; (2) by preventing the excessive deposition of fibrin; and (3) by promoting myoblast migration. Interestingly, genetic loss of the uPA receptor in mdx mice did not exacerbate muscular dystrophy in mdx mice, suggesting that uPA exerts its effects independently of its receptor. These findings underscore the importance of uPA in muscular dystrophy.

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Chausova, P. A., O. P. Ryzhkova, and A. V. Polyakov. "Clinical and genetic characteristics of congenital muscular dystrophies (Part 1)." Neuromuscular Diseases 10, no. 1 (June 3, 2020): 10–21. http://dx.doi.org/10.17650/2222-8721-2020-10-1-10-21.

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Congenital muscular dystrophy is an extremely heterogeneous group of hereditary neuromuscular diseases that are clinically characterized by muscular hypotonia, progressive muscle weakness, and dystrophic changes in the muscles. Overlapping clinical symptoms and many genes that have to be analyzed to determine the specific form of the disease in the patient make diagnosis difficult. The molecular genetic stage of diagnosis includes many different methods depending on the clinical hypothesis and their application has not lost its relevance even in the era of massive parallel sequencing. In addition to DNA sequence analysis, the analysis of muscle protein expression can also play a significant role in the diagnosis of congenital muscular dystrophy. In the review, we will consider the most important etiological, pathophysiological, clinical and laboratory data of the main forms of congenital muscular dystrophy known today.

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Mathews, Katherine D. "Muscular dystrophy overview: genetics and diagnosis." Neurologic Clinics 21, no. 4 (November 2003): 795–816. http://dx.doi.org/10.1016/s0733-8619(03)00065-3.

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Kunkel, L. M., A. P. Monaco, C. J. Bertelson, and C. A. Colletti. "Molecular Genetics of Duchenne Muscular Dystrophy." Cold Spring Harbor Symposia on Quantitative Biology 51 (January 1, 1986): 349–51. http://dx.doi.org/10.1101/sqb.1986.051.01.041.

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Kunkel, L. M. "The molecular genetics of muscular dystrophy." Genetics in Medicine 2, no. 1 (January 2000): 48. http://dx.doi.org/10.1097/00125817-200001000-00018.

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Wijmenga, Cisca, Rune R. Frants, Jane E. Hewitt, Judith C. T. van Deutekom, Michel van Geel, Tracy J. Wright, George W. Padberg, Marten H. Hofker, and Gert-Jan B. van Ommen. "Molecular genetics of facioscapulohumeral muscular dystrophy." Neuromuscular Disorders 3, no. 5-6 (January 1993): 487–91. http://dx.doi.org/10.1016/0960-8966(93)90102-p.

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Vieira, Natassia M., Janelle M. Spinazzola, Matthew S. Alexander, Yuri B. Moreira, Genri Kawahara, Devin E. Gibbs, Lillian C. Mead, Sergio Verjovski-Almeida, Mayana Zatz, and Louis M. Kunkel. "Repression of phosphatidylinositol transfer protein α ameliorates the pathology of Duchenne muscular dystrophy." Proceedings of the National Academy of Sciences 114, no. 23 (May 22, 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 golden retriever muscular dystrophy (GRMD) dog colony, two related dogs demonstrated strikingly mild dystrophic phenotypes compared with those typically observed in severely affected GRMD dogs despite lacking dystrophin. Microarray analysis of these “escaper” dogs revealed reduced expression of phosphatidylinositol transfer protein-α (PITPNA) in escaper versus severely affected GRMD dogs. Based on these findings, we decided to pursue investigation of modulation of PITPNA expression on dystrophic pathology in GRMD dogs, dystrophin-deficient sapje zebrafish, and human DMD myogenic cells. In GRMD dogs, decreased expression of Pitpna was associated with increased phosphorylated Akt (pAkt) expression and decreased PTEN levels. PITPNA knockdown by injection of morpholino oligonucleotides in sapje zebrafish also increased pAkt, rescued the abnormal muscle phenotype, and improved long-term sapje mutant survival. In DMD myotubes, PITPNA knockdown by lentiviral shRNA increased pAkt and increased myoblast fusion index. Overall, our findings suggest PIPTNA as a disease modifier that accords benefits to the abnormal signaling, morphology, and function of dystrophic skeletal muscle, and may be a target for DMD and related neuromuscular diseases.

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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." Physiological Genomics 3, no. 3 (September 8, 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 supplying a normal dystrophin gene to DMD muscles could be hampered by host immune system recognition of dystrophin as a “foreign” protein. In contrast, a closely related protein called utrophin is not foreign to DMD patients and is able to compensate for dystrophin deficiency when overexpressed throughout development in transgenic mice. However, the issue of which of the two candidate molecules is superior for DMD therapy has remained an open question. In this study, dystrophin and utrophin gene transfer effects on dystrophic muscle function were directly compared in the murine (mdx) model of DMD using E1/E3-deleted adenovirus vectors containing either a dystrophin (AdV-Dys) or a utrophin (AdV-Utr) transgene. In immunologically immature neonatal animals, AdV-Dys and AdV-Utr improved tibialis anterior muscle histopathology, force-generating capacity, and the ability to resist injury caused by high-stress contractions to an equivalent degree. By contrast, only AdV-Utr was able to achieve significant improvement in force generation and the ability to resist stress-induced injury in the soleus muscle of immunocompetent mature mdx animals. In addition, in mature mdx mice, there was significantly greater transgene persistence and reduced inflammation with utrophin compared to dystrophin gene transfer. We conclude that dystrophin and utrophin are largely equivalent in their intrinsic abilities to prevent the development of muscle necrosis and weakness when expressed in neonatal mdx animals with an immature immune system. However, because immunity against dystrophin places an important limitation on the efficacy of dystrophin gene replacement in an immunocompetent mature host, the use of utrophin as an alternative to dystrophin gene transfer in this setting appears to offer a significant therapeutic advantage.

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Saotome, Masao, Yuji Yoshitomi, Shunichi Kojima, and Morio Kuramochi. "Dilated Cardiomyopathy of Becker-Type Muscular Dystrophy with Exon 4 Deletion." Angiology 52, no. 5 (May 2001): 343–47. http://dx.doi.org/10.1177/000331970105200508.

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The authors report a 47-year-old man with Becker-type muscular dystrophy presenting with dilated cardiomyopathy. Left ventriculography showed diffuse severe hypokinesia: left ventric ular end-diastolic volume index 193 mL/m2, left ventricular end-systolic volume index 143 mL/m 2, and left ventricular ejection fraction 26%. Skeletal muscle biopsy demonstrated a dystrophic process. Genetic analysis revealed a deletion of exon 4. There was a difference in immunos taining pattern between skeletal muscles and cardiac muscles. Severe cardiac dysfunction in this case may be associated with the damage in dystrophin-deficient fibers.

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Lombardo, Salvo Danilo, Emanuela Mazzon, Katia Mangano, Maria Sofia Basile, Eugenio Cavalli, Santa Mammana, Paolo Fagone, Ferdinando Nicoletti, and Maria Cristina Petralia. "Transcriptomic Analysis Reveals Involvement of the Macrophage Migration Inhibitory Factor Gene Network in Duchenne Muscular Dystrophy." Genes 10, no. 11 (November 18, 2019): 939. http://dx.doi.org/10.3390/genes10110939.

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Duchenne muscular dystrophy (DMD) is a progressive hereditary muscular disease with X-linked recessive inheritance, that leads patients to premature death. The loss of dystrophin determines membrane instability, causing cell damage and inflammatory response. Macrophage migration inhibitory factor (MIF) is a cytokine that exerts pleiotropic properties and is implicated in the pathogenesis of a variety of diseases. Recently, converging data from independent studies have pointed to a possible role of MIF in dystrophic muscle disorders, including DMD. In the present study, we have investigated the modulation of MIF and MIF-related genes in degenerative muscle disorders, by making use of publicly available whole-genome expression datasets. We show here a significant enrichment of MIF and related genes in muscle samples from DMD patients, as well as from patients suffering from Becker’s disease and limb-girdle muscular dystrophy type 2B. On the other hand, transcriptomic analysis of in vitro differentiated myotubes from healthy controls and DMD patients revealed no significant alteration in the expression levels of MIF-related genes. Finally, by analyzing DMD samples as a time series, we show that the modulation of the genes belonging to the MIF network is an early event in the DMD muscle and does not change with the increasing age of the patients, Overall, our analysis suggests that MIF may play a role in vivo during muscle degeneration, likely promoting inflammation and local microenvironment reaction.

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Pandya, Shree, Wendy M. King, and Rabi Tawil. "Facioscapulohumeral Dystrophy." Physical Therapy 88, no. 1 (January 1, 2008): 105–13. http://dx.doi.org/10.2522/ptj.20070104.

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Facioscapulohumeral dystrophy (FSHD) is the third most common inherited muscular dystrophy after Duchenne dystrophy and myotonic dystrophy. Over the last decade, major advances have occurred in the understanding of the genetics of this disorder. Despite these advances, the exact mechanisms that lead to atrophy and weakness secondary to the genetic defect are still not understood. The purposes of this article are to increase awareness of FSHD among clinicians; to provide an update regarding the genetics, clinical features, natural history, and current management of FSHD; and to discuss opportunities for research.

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Park, Eun-Woo, Ye-Jee Shim, Jung-Sook Ha, Jin-Hong Shin, Soyoung Lee, and Jang-Hyuk Cho. "Diagnosis of Duchenne Muscular Dystrophy in a Presymptomatic Infant Using Next-Generation Sequencing and Chromosomal Microarray Analysis: A Case Report." Children 8, no. 5 (May 11, 2021): 377. http://dx.doi.org/10.3390/children8050377.

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Duchenne muscular dystrophy is a progressive and lethal X-linked recessive neuromuscular disease caused by mutations in the dystrophin gene. It has a high rate of diagnostic delay; early diagnosis and treatment are often not possible due to delayed recognition of muscle weakness and lack of effective treatments. Current treatments based on genetic therapy can improve clinical results, but treatment must begin as early as possible before significant muscle damage. Therefore, early diagnosis and rehabilitation of Duchenne muscular dystrophy are needed before symptom aggravation. Creatine kinase is a diagnostic marker of neuromuscular disorders. Herein, the authors report a case of an infant patient with Duchenne muscular dystrophy with a highly elevated creatine kinase level but no obvious symptoms of muscle weakness. The patient was diagnosed with Duchenne muscular dystrophy via next-generation sequencing and chromosomal microarray analysis to identify possible inherited metabolic and neuromuscular diseases related to profound hyperCKemia. The patient is enrolled in a rehabilitation program and awaits the approval of the genetic treatment in Korea. This is the first report of an infantile presymptomatic Duchenne muscular dystrophy diagnosis using next-generation sequencing and chromosomal microarray analysis.

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Swaggart, Kayleigh A., Ahlke Heydemann, Abraham A. Palmer, and Elizabeth M. McNally. "Distinct genetic regions modify specific muscle groups in muscular dystrophy." Physiological Genomics 43, no. 1 (January 2011): 24–31. http://dx.doi.org/10.1152/physiolgenomics.00172.2010.

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Phenotypic expression in the muscular dystrophies is variable, even with the identical mutation, providing strong evidence that genetic modifiers influence outcome. To identify genetic modifier loci, we used quantitative trait locus mapping in two differentially affected mouse strains with muscular dystrophy. Using the Sgcg model of limb girdle muscular dystrophy that lacks the dystrophin-associated protein γ-sarcoglycan, we evaluated chromosomal regions that segregated with two distinct quantifiable characteristics of muscular dystrophy, membrane permeability and fibrosis. We previously identified a single major locus on murine chromosome 7 that influences both traits of membrane permeability and fibrosis in the quadriceps muscle. Using a larger cohort, we now found that this same interval strongly associated with both traits in all limb skeletal muscle groups studied, including the gastrocnemius/soleus, gluteus/hamstring, and triceps muscles. In contrast, the muscles of the trunk were modified by distinct genetic loci, possibly reflecting the embryological origins and physiological stressors unique to these muscle groups. A locus on chromosome 18 was identified that modified membrane permeability of the abdominal muscles, and a locus on chromosome 3 was found that regulated diaphragm and abdominal muscle fibrosis. Fibrosis in the heart associated with a region on chromosome 9 and likely reflects differential function between cardiac and skeletal muscle. These data underscore the complexity of inheritance and penetrance of single-gene disorders.

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