Log in

Relevant bibliographies by topics / Dystrophic muscle / Journal articles

To see the other types of publications on this topic, follow the link: Dystrophic muscle.

Journal articles on the topic 'Dystrophic muscle'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Dystrophic muscle.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

2

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

3

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

4

Whitehead, Nicholas P., Min Jeong Kim, Kenneth L. Bible, Marvin E. Adams, and Stanley C. Froehner. "A new therapeutic effect of simvastatin revealed by functional improvement in muscular dystrophy." Proceedings of the National Academy of Sciences 112, no. 41 (2015): 12864–69. http://dx.doi.org/10.1073/pnas.1509536112.

Full text

Abstract:

Duchenne muscular dystrophy (DMD) is a lethal, degenerative muscle disease with no effective treatment. DMD muscle pathogenesis is characterized by chronic inflammation, oxidative stress, and fibrosis. Statins, cholesterol-lowering drugs, inhibit these deleterious processes in ischemic diseases affecting skeletal muscle, and therefore have potential to improve DMD. However, statins have not been considered for DMD, or other muscular dystrophies, principally because skeletal-muscle-related symptoms are rare, but widely publicized, side effects of these drugs. Here we show positive effects of st

APA, Harvard, Vancouver, ISO, and other styles

5

Ng, Rainer, Joseph M. Metzger, Dennis R. Claflin, and John A. Faulkner. "Poloxamer 188 reduces the contraction-induced force decline in lumbrical muscles from mdx mice." American Journal of Physiology-Cell Physiology 295, no. 1 (2008): C146—C150. http://dx.doi.org/10.1152/ajpcell.00017.2008.

Full text

Abstract:

Duchenne Muscular Dystrophy is a genetic disease caused by the lack of the protein dystrophin. Dystrophic muscles are highly susceptible to contraction-induced injury, and following contractile activity, have disrupted plasma membranes that allow leakage of calcium ions into muscle fibers. Because of the direct relationship between increased intracellular calcium concentration and muscle dysfunction, therapeutic outcomes may be achieved through the identification and restriction of calcium influx pathways. Our purpose was to determine the contribution of sarcolemmal lesions to the force defici

APA, Harvard, Vancouver, ISO, and other styles

6

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

7

Reid, Andrea L., Yimin Wang, Adrienne Samani, et al. "DOCK3 is a dosage-sensitive regulator of skeletal muscle and Duchenne muscular dystrophy-associated pathologies." Human Molecular Genetics 29, no. 17 (2020): 2855–71. http://dx.doi.org/10.1093/hmg/ddaa173.

Full text

Abstract:

Abstract DOCK3 is a member of the DOCK family of guanine nucleotide exchange factors that regulate cell migration, fusion and viability. Previously, we identified a dysregulated miR-486/DOCK3 signaling cascade in dystrophin-deficient muscle, which resulted in the overexpression of DOCK3; however, little is known about the role of DOCK3 in muscle. Here, we characterize the functional role of DOCK3 in normal and dystrophic skeletal muscle. Utilizing Dock3 global knockout (Dock3 KO) mice, we found that the haploinsufficiency of Dock3 in Duchenne muscular dystrophy mice improved dystrophic muscle

APA, Harvard, Vancouver, ISO, and other styles

8

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

9

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

10

Reggio, Alessio, Marco Rosina, Natalie Krahmer, et al. "Metabolic reprogramming of fibro/adipogenic progenitors facilitates muscle regeneration." Life Science Alliance 3, no. 3 (2020): e202000646. http://dx.doi.org/10.26508/lsa.202000660.

Full text

Abstract:

In Duchenne muscular dystrophy (DMD), the absence of the dystrophin protein causes a variety of poorly understood secondary effects. Notably, muscle fibers of dystrophic individuals are characterized by mitochondrial dysfunctions, as revealed by a reduced ATP production rate and by defective oxidative phosphorylation. Here, we show that in a mouse model of DMD (mdx), fibro/adipogenic progenitors (FAPs) are characterized by a dysfunctional mitochondrial metabolism which correlates with increased adipogenic potential. Using high-sensitivity mass spectrometry–based proteomics, we report that a sh

APA, Harvard, Vancouver, ISO, and other styles

11

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

12

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

13

Schertzer, Jonathan D., Chris van der Poel, Thea Shavlakadze, Miranda D. Grounds, and Gordon S. Lynch. "Muscle-specific overexpression of IGF-I improves E-C coupling in skeletal muscle fibers from dystrophic mdx mice." American Journal of Physiology-Cell Physiology 294, no. 1 (2008): C161—C168. http://dx.doi.org/10.1152/ajpcell.00399.2007.

Full text

Abstract:

Duchenne muscular dystrophy (DMD) is a lethal X-linked disease caused by the absence of functional dystrophin. Abnormal excitation-contraction (E-C) coupling has been reported in dystrophic muscle fibers from mdx mice, and alterations in E-C coupling components may occur as a direct result of dystrophin deficiency. We hypothesized that muscle-specific overexpression of insulin-growth factor-1 (IGF-I) would reduce E-C coupling failure in mdx muscle. Mechanically skinned extensor digitorum longus muscle fibers from mdx mice displayed a faster decline in depolarization-induced force responses (DI

APA, Harvard, Vancouver, ISO, and other styles

14

Amirouche, Adel, Vanessa E. Jahnke, John A. Lunde, Nathalie Koulmann, Damien G. Freyssenet, and Bernard J. Jasmin. "Muscle-specific microRNA-206 targets multiple components in dystrophic skeletal muscle representing beneficial adaptations." American Journal of Physiology-Cell Physiology 312, no. 3 (2017): C209—C221. http://dx.doi.org/10.1152/ajpcell.00185.2016.

Full text

Abstract:

Over the last several years, converging lines of evidence have indicated that miR-206 plays a pivotal role in promoting muscle differentiation and regeneration, thereby potentially impacting positively on the progression of neuromuscular disorders, including Duchenne muscular dystrophy (DMD). Despite several studies showing the regulatory function of miR-206 on target mRNAs in skeletal muscle cells, the effects of overexpression of miR-206 in dystrophic muscles remain to be established. Here, we found that miR-206 overexpression in mdx mouse muscles simultaneously targets multiple mRNAs and pr

APA, Harvard, Vancouver, ISO, and other styles

15

Howlett, S. E., C. R. Triggle, and T. B. Hoekman. "Effects of noradrenaline, serotonin, and selected antagonists on the vascular smooth muscle of normal and dystrophic chickens." Canadian Journal of Physiology and Pharmacology 64, no. 5 (1986): 545–49. http://dx.doi.org/10.1139/y86-090.

Full text

Abstract:

The pathogenesis of the human muscular dystrophies is unknown, and several competing hypotheses have been proposed. The vascular hypothesis states that muscle fibre necrosis occurs in dystrophy as a result of transient muscle ischemia. Although abnormalities of the vascular system may be demonstrated in dystrophy, their role in pathogenesis remains obscure. The responses to serotonin (5-HT) and noradrenaline (NA) were examined in isolated ischiatic artery preparations from normal and genetically dystrophic chickens. The tension generated in response to 5-HT was greater in arteries from normal

APA, Harvard, Vancouver, ISO, and other styles

16

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

17

Dorchies, Olivier M., Stéphanie Wagner, Ophélie Vuadens, et al. "Green tea extract and its major polyphenol (−)-epigallocatechin gallate improve muscle function in a mouse model for Duchenne muscular dystrophy." American Journal of Physiology-Cell Physiology 290, no. 2 (2006): C616—C625. http://dx.doi.org/10.1152/ajpcell.00425.2005.

Full text

Abstract:

Duchenne muscular dystrophy is a frequent muscular disorder caused by mutations in the gene encoding dystrophin, a cytoskeletal protein that contributes to the stabilization of muscle fiber membrane during muscle activity. Affected individuals show progressive muscle wasting that generally causes death by age 30. In this study, the dystrophic mdx 5Cv mouse model was used to investigate the effects of green tea extract, its major component (−)-epigallocatechin gallate, and pentoxifylline on dystrophic muscle quality and function. Three-week-old mdx 5Cv mice were fed for either 1 or 5 wk a contr

APA, Harvard, Vancouver, ISO, and other styles

18

Anderson, Judy E. "Myotube phospholipid synthesis and sarcolemmal ATPase activity in dystrophic (mdx) mouse muscle." Biochemistry and Cell Biology 69, no. 12 (1991): 835–41. http://dx.doi.org/10.1139/o91-124.

Full text

Abstract:

Phospholipid incorporation of 32P by primary myotube cultures and the tissue activity of sarcolemmal Na+/K+-transporting ATPase were studied to determine whether the absence of dystrophin from dystrophic (mdx) muscle would affect membrane lipid synthesis and membrane function. The incorporation of 32P by phospholipid as a ratio with total protein was greater in cultured dystrophic cells compared with control cells. The mdx cells also incorporated more 32P than control cells into phosphatidylethanolamine, which is thought to increase prior to myoblast fusion, and less into phosphatidylserine, p

APA, Harvard, Vancouver, ISO, and other styles

19

Culligan, Kevin, Niamh Banville, Paul Dowling, and Kay Ohlendieck. "Drastic reduction of calsequestrin-like proteins and impaired calcium binding in dystrophic mdx muscle." Journal of Applied Physiology 92, no. 2 (2002): 435–45. http://dx.doi.org/10.1152/japplphysiol.00903.2001.

Full text

Abstract:

Although the reduction in dystrophin-associated glycoproteins is the primary pathophysiological consequence of the deficiency in dystrophin, little is known about the secondary abnormalities leading to x-linked muscular dystrophy. As abnormal Ca2+ handling may be involved in myonecrosis, we investigated the fate of key Ca2+ regulatory membrane proteins in dystrophic mdx skeletal muscle membranes. Whereas the expression of the ryanodine receptor, the dihydropyridine receptor, the Ca2+-ATPase, and calsequestrin was not affected, a drastic decline in calsequestrin-like proteins of 150–220 kDa was

APA, Harvard, Vancouver, ISO, and other styles

20

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

21

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

22

Hitaka, T., T. Mizutani, K. Watanabe, and T. Totsuka. "The high content of natural suppressor serine tRNA in dystrophic mouse muscle." Biochemical Journal 266, no. 1 (1990): 201–6. http://dx.doi.org/10.1042/bj2660201.

Full text

Abstract:

In order to gain an insight into the pathogenesis of mouse muscular dystrophy, we investigated the natural suppressor serine tRNA. The natural suppressor seryl-tRNA was distinguished from the other seryl-tRNAs on the basis of its specific property of being converted into phosphoseryl-tRNA by a tRNA kinase. On a wet-weight basis, the content of total tRNA in dystrophic muscles was 47% of that in normal muscles. Although the serine-accepting activities of tRNA were similar in muscles of 3-month-old dystrophic and normal mice, the ratio of [32P]phosphoseryl-tRNA (suppressor tRNA) to the total ser

APA, Harvard, Vancouver, ISO, and other styles

23

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

24

Srivastava, Niraj Kumar, Somnath Mukherjee, and Vijay Nath Mishra. "Metabolic Disturbance in Patients with Muscular Dystrophy and Reflection of Altered Enzyme Activity in Dystrophic Muscle: One Critical View." Journal of Biomedical Research & Environmental Sciences 1, no. 8 (2020): 393–403. http://dx.doi.org/10.37871/jbres1171.

Full text

Abstract:

Muscular dystrophies are inherited myogenic diseases and considered by progressive muscle wasting and weakness with variable distribution and severity. The essential characteristics of muscular dystrophies are selective involvement, significant wasting and weakness of muscles. The most common and frequent types of muscular dystrophies are Duchenne Muscular Dystrophy (DMD), Becker Muscular Dystrophy (BMD), Facioscapulohumeral Dystrophy (FSHD) and Limb Girdle Muscular Dystrophy (LGMD). Metabolic disturbance is observed in muscular dystrophy patients (DMD, BMD, FSHD and LGMD-2B). Alteration in th

APA, Harvard, Vancouver, ISO, and other styles

25

Hughes, K. J., A. Rodriguez, K. M. Flatt, et al. "Physical exertion exacerbates decline in the musculature of an animal model of Duchenne muscular dystrophy." Proceedings of the National Academy of Sciences 116, no. 9 (2019): 3508–17. http://dx.doi.org/10.1073/pnas.1811379116.

Full text

Abstract:

Duchenne muscular dystrophy (DMD) is a genetic disorder caused by loss of the protein dystrophin. In humans, DMD has early onset, causes developmental delays, muscle necrosis, loss of ambulation, and death. Current animal models have been challenged by their inability to model the early onset and severity of the disease. It remains unresolved whether increased sarcoplasmic calcium observed in dystrophic muscles follows or leads the mechanical insults caused by the muscle’s disrupted contractile machinery. This knowledge has important implications for patients, as potential physiotherapeutic tr

APA, Harvard, Vancouver, ISO, and other styles

26

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

27

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

28

van Westering, Tirsa L. E., Henrik J. Johansson, Britt Hanson, et al. "Mutation-independent Proteomic Signatures of Pathological Progression in Murine Models of Duchenne Muscular Dystrophy." Molecular & Cellular Proteomics 19, no. 12 (2020): 2047–67. http://dx.doi.org/10.1074/mcp.ra120.002345.

Full text

Abstract:

The absence of the dystrophin protein in Duchenne muscular dystrophy (DMD) results in myofiber fragility and a plethora of downstream secondary pathologies. Although a variety of experimental therapies are in development, achieving effective treatments for DMD remains exceptionally challenging, not least because the pathological consequences of dystrophin loss are incompletely understood. Here we have performed proteome profiling in tibialis anterior muscles from two murine DMD models (mdx and mdx52) at three ages (8, 16, and 80 weeks of age), all n = 3. High-resolution isoelectric focusing li

APA, Harvard, Vancouver, ISO, and other styles

29

Sarkozy, Anna, Mariacristina Scoto, Francesco Muntoni, and Joana Domingos. "Dystrophinopathies and Limb-Girdle Muscular Dystrophies." Neuropediatrics 48, no. 04 (2017): 262–72. http://dx.doi.org/10.1055/s-0037-1601860.

Full text

Abstract:

AbstractMuscular dystrophies are a heterogeneous group of inherited diseases. The natural history of these disorders along with their management have changed mainly due to a better understanding of their pathophysiology, the evolution of standards of care, and new treatment options. Dystrophinopathies include both Duchenne's and Becker's muscular dystrophies, but in reality they are a spectrum of muscle diseases caused by mutations in the gene that encodes the protein dystrophin. Duchenne's muscular dystrophy is the most common form of inherited muscle disease of childhood. The current standar

APA, Harvard, Vancouver, ISO, and other styles

30

Iyer, Shama R., Sameer B. Shah, Christopher W. Ward, et al. "Differential YAP nuclear signaling in healthy and dystrophic skeletal muscle." American Journal of Physiology-Cell Physiology 317, no. 1 (2019): C48—C57. http://dx.doi.org/10.1152/ajpcell.00432.2018.

Full text

Abstract:

Mechanical forces regulate muscle development, hypertrophy, and homeostasis. Force-transmitting structures allow mechanotransduction at the sarcolemma, cytoskeleton, and nuclear envelope. There is growing evidence that Yes-associated protein (YAP) serves as a nuclear relay of mechanical signals and can induce a range of downstream signaling cascades. Dystrophin is a sarcolemma-associated protein, and its absence underlies the pathology in Duchenne muscular dystrophy. We tested the hypothesis that the absence of dystrophin in muscle would result in reduced YAP signaling in response to loading.

APA, Harvard, Vancouver, ISO, and other styles

31

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.

Full text

Abstract:

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 prot

APA, Harvard, Vancouver, ISO, and other styles

32

Sitzia, Clementina, Andrea Farini, Federica Colleoni, 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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

33

Yu, Lu, Xiaoli Zhang, Yexin Yang, et al. "Small-molecule activation of lysosomal TRP channels ameliorates Duchenne muscular dystrophy in mouse models." Science Advances 6, no. 6 (2020): eaaz2736. http://dx.doi.org/10.1126/sciadv.aaz2736.

Full text

Abstract:

Duchenne muscular dystrophy (DMD) is a devastating disease caused by mutations in dystrophin that compromise sarcolemma integrity. Currently, there is no treatment for DMD. Mutations in transient receptor potential mucolipin 1 (ML1), a lysosomal Ca2+ channel required for lysosomal exocytosis, produce a DMD-like phenotype. Here, we show that transgenic overexpression or pharmacological activation of ML1 in vivo facilitates sarcolemma repair and alleviates the dystrophic phenotypes in both skeletal and cardiac muscles of mdx mice (a mouse model of DMD). Hallmark dystrophic features of DMD, inclu

APA, Harvard, Vancouver, ISO, and other styles

34

Schertzer, Jonathan D., James G. Ryall, and Gordon S. Lynch. "Systemic administration of IGF-I enhances oxidative status and reduces contraction-induced injury in skeletal muscles of mdx dystrophic mice." American Journal of Physiology-Endocrinology and Metabolism 291, no. 3 (2006): E499—E505. http://dx.doi.org/10.1152/ajpendo.00101.2006.

Full text

Abstract:

The absence of dystrophin and resultant disruption of the dystrophin glycoprotein complex renders skeletal muscles of dystrophic patients and dystrophic mdx mice susceptible to contraction-induced injury. Strategies to reduce contraction-induced injury are of critical importance, because this mode of damage contributes to the etiology of myofiber breakdown in the dystrophic pathology. Transgenic overexpression of insulin-like growth factor-I (IGF-I) causes myofiber hypertrophy, increases force production, and can improve the dystrophic pathology in mdx mice. In contrast, the predominant effect

APA, Harvard, Vancouver, ISO, and other styles

35

Srivastava, U. S., E. A. Sugden, P. K. Majumdar, M. L. Thakur, and G. M. Bhatnagar. "Biochemical changes in progressive muscular dystrophy. XIV. Skeletal muscle myosin mRNA translatability in dystrophic mice." Biochemistry and Cell Biology 65, no. 9 (1987): 833–41. http://dx.doi.org/10.1139/o87-108.

Full text

Abstract:

Variations in the content and translatability of the poly(A)+ RNA and mRNA molecules coding for myosin (M) were studied in the hind leg muscles of genetically dystrophic mice. The poly(A)+ RNA content of total skeletal muscle failed to increase normally during progression of the disease. M mRNA, isolated from dystrophic murine muscle poly(A)+ RNA, was mostly found to be associated with the 26S RNA species. The translation of M mRNA in an in vitro heterologous wheat germ system was lower at 8 and 16 weeks in the dystrophic group as compared with the controls. Analysis of the translation product

APA, Harvard, Vancouver, ISO, and other styles

36

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

37

Jakubiec-Puka, Anna, Donatella Biral, Kazimierz Krawczyk, and Romeo Betto. "Ultrastructure of diaphragm from dystrophic alpha-sarcoglycan-null mice." Acta Biochimica Polonica 52, no. 2 (2005): 453–60. http://dx.doi.org/10.18388/abp.2005_3459.

Full text

Abstract:

alpha-Sarcoglycan is a 50 kDa single-pass transmembrane glycoprotein exclusively expressed in striated muscle that, together with beta-, gamma-, and delta-sarcoglycan, forms a sub-complex at the muscle fibre cell membrane. The sarcoglycans are components of the dystrophin-associated glycoprotein (DAG) complex which forms a mechanical link between the intracellular cytoskeleton and extracellular matrix. The DAG complex function is to protect the muscle membrane from the stress of contractile activity and as a structure for the docking of signalling proteins. Genetic defects of DAG components ca

APA, Harvard, Vancouver, ISO, and other styles

38

Pákozdy, Á., M. Leschnik, B. Nell, et al. "Myotonic dystrophy in two European grey wolves ( Canis lupus )." Acta Veterinaria Hungarica 55, no. 1 (2007): 87–95. http://dx.doi.org/10.1556/avet.55.2007.1.9.

Full text

Abstract:

Two related European Grey wolves ( Canis lupus ) with the history of muscle stiffness beginning at 2 weeks of age were examined in this study. Muscle tone and muscle mass were increased in both animals. Muscle stiffness was worsened by stress so that the animals fell into lateral recumbency. Blood chemistry revealed mildly increased serum creatine kinase activity. Abnormal potentials typical of myotonic discharges were recorded by electromyography. Cataract, first-degree atrioventricular (AV) block and inhomogeneous myocardial texture by ultrasound suggested extramuscular involvement. Myopatho

APA, Harvard, Vancouver, ISO, and other styles

39

Kiriaev, Leonit, Sindy Kueh, John W. Morley, Kathryn N. North, Peter J. Houweling, and Stewart I. Head. "Branched fibers from old fast-twitch dystrophic muscles are the sites of terminal damage in muscular dystrophy." American Journal of Physiology-Cell Physiology 314, no. 6 (2018): C662—C674. http://dx.doi.org/10.1152/ajpcell.00161.2017.

Full text

Abstract:

A striking pathological feature of dystrophinopathies is the presence of morphologically abnormal branched skeletal muscle fibers. The deterioration of muscle contractile function in Duchenne muscular dystrophy is accompanied by both an increase in number and complexity of these branched fibers. We propose that when number and complexity of branched fibers reaches a critical threshold, or “tipping point,” the branches in and of themselves are the site of contraction-induced rupture. In the present study, we use the dystrophic mdx mouse and littermate controls to study the prediseased dystrophi

APA, Harvard, Vancouver, ISO, and other styles

40

Hayes, Alan, and David A. Williams. "Contractile properties of clenbuterol-treatedmdx muscle are enhanced by low-intensity swimming." Journal of Applied Physiology 82, no. 2 (1997): 435–39. http://dx.doi.org/10.1152/jappl.1997.82.2.435.

Full text

Abstract:

Hayes, Alan, and David A. Williams. Contractile properties of clenbuterol-treated mdxmuscle are enhanced by low-intensity swimming. J. Appl. Physiol. 82(2): 435–439, 1997.—The β2-agonist clenbuterol has potent anabolic properties in normal and denervated muscle and, as such, may be of use in muscle wasting diseases such as muscular dystrophy. However, potential side effects such as the transformation of the fiber type pool toward increased proportions of fast-twitch fibers must be balanced with the beneficial anabolic properties. In the present report, we clearly show that extensor digitorum l

APA, Harvard, Vancouver, ISO, and other styles

41

Matsumura, Cíntia Yuri, Ana Paula Tiemi Taniguti, Adriana Pertille, Humberto Santo Neto, and Maria Julia Marques. "Stretch-activated calcium channel protein TRPC1 is correlated with the different degrees of the dystrophic phenotype in mdx mice." American Journal of Physiology-Cell Physiology 301, no. 6 (2011): C1344—C1350. http://dx.doi.org/10.1152/ajpcell.00056.2011.

Full text

Abstract:

In Duchenne muscular dystrophy (DMD) and in the mdx mouse model of DMD, the lack of dystrophin is related to enhanced calcium influx and muscle degeneration. Stretch-activated channels (SACs) might be directly involved in the pathology of DMD, and transient receptor potential cation channels have been proposed as likely candidates of SACs. We investigated the levels of transient receptor potential canonical channel 1 (TRPC1) and the effects of streptomycin, a SAC blocker, in muscles showing different degrees of the dystrophic phenotype. Mdx mice (18 days old, n = 16) received daily intraperito

APA, Harvard, Vancouver, ISO, and other styles

42

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

43

Wieneke, Sascha, Peter Heimann, Sigalit Leibovitz, Uri Nudel, and Harald Jockusch. "Acute pathophysiological effects of muscle-expressed Dp71 transgene on normal and dystrophic mouse muscle." Journal of Applied Physiology 95, no. 5 (2003): 1861–66. http://dx.doi.org/10.1152/japplphysiol.00326.2003.

Full text

Abstract:

products of the dystrophin gene range from the 427-kDa full-length dystrophin to the 70.8-kDa Dp71. Dp427 is expressed in skeletal muscle, where it links the actin cytoskeleton with the extracellular matrix via a complex of dystrophin-associated proteins (DAPs). Dystrophin deficiency disrupts the DAP complex and causes muscular dystrophy in humans and the mdx mouse. Dp71, the major nonmuscle product, consists of the COOH-terminal part of dystrophin, including the binding site for the DAP complex but lacks binding sites for microfilaments. Dp71 transgene (Dp71tg) expressed in mdx muscle restore

APA, Harvard, Vancouver, ISO, and other styles

44

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

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

45

Raimondo, Theresa M., and David J. Mooney. "Anti-inflammatory nanoparticles significantly improve muscle function in a murine model of advanced muscular dystrophy." Science Advances 7, no. 26 (2021): eabh3693. http://dx.doi.org/10.1126/sciadv.abh3693.

Full text

Abstract:

Chronic inflammation contributes to the pathogenesis of all muscular dystrophies. Inflammatory T cells damage muscle, while regulatory T cells (Tregs) promote regeneration. We hypothesized that providing anti-inflammatory cytokines in dystrophic muscle would promote proregenerative immune phenotypes and improve function. Primary T cells from dystrophic (mdx) mice responded appropriately to inflammatory or suppressive cytokines. Subsequently, interleukin-4 (IL-4)– or IL-10–conjugated gold nanoparticles (PA4, PA10) were injected into chronically injured, aged, mdx muscle. PA4 and PA10 increased

APA, Harvard, Vancouver, ISO, and other styles

46

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

47

Niranjan, Nandita, Satvik Mareedu, Yimin Tian, et al. "Sarcolipin overexpression impairs myogenic differentiation in Duchenne muscular dystrophy." American Journal of Physiology-Cell Physiology 317, no. 4 (2019): C813—C824. http://dx.doi.org/10.1152/ajpcell.00146.2019.

Full text

Abstract:

Reduction in the expression of sarcolipin (SLN), an inhibitor of sarco(endo)plasmic reticulum (SR) Ca2+-ATPase (SERCA), ameliorates severe muscular dystrophy in mice. However, the mechanism by which SLN inhibition improves muscle structure remains unclear. Here, we describe the previously unknown function of SLN in muscle differentiation in Duchenne muscular dystrophy (DMD). Overexpression of SLN in C2C12 resulted in decreased SERCA pump activity, reduced SR Ca2+ load, and increased intracellular Ca2+ ([Formula: see text]) concentration. In addition, SLN overexpression resulted in altered expr

APA, Harvard, Vancouver, ISO, and other styles

48

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

49

Vandebrouck, Clarisse, Dominique Martin, Monique Colson-Van Schoor, Huguette Debaix, and Philippe Gailly. "Involvement of TRPC in the abnormal calcium influx observed in dystrophic (mdx) mouse skeletal muscle fibers." Journal of Cell Biology 158, no. 6 (2002): 1089–96. http://dx.doi.org/10.1083/jcb.200203091.

Full text

Abstract:

Duchenne muscular dystrophy results from the lack of dystrophin, a cytoskeletal protein associated with the inner surface membrane, in skeletal muscle. The absence of dystrophin induces an abnormal increase of sarcolemmal calcium influx through cationic channels in adult skeletal muscle fibers from dystrophic (mdx) mice. We observed that the activity of these channels was increased after depletion of the stores of calcium with thapsigargin or caffeine. By analogy with the situation observed in nonexcitable cells, we therefore hypothesized that these store-operated channels could belong to the

APA, Harvard, Vancouver, ISO, and other styles

50

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!