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Journal articles on the topic 'Β-sarcoglycan'

Author: Grafiati

Published: 9 March 2023

Last updated: 10 March 2023

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1

Chan, Yiu-mo, Carsten G. Bönnemann, Hart G. W. Lidov, and Louis M. Kunkel. "Molecular Organization of Sarcoglycan Complex in Mouse Myotubes in Culture." Journal of Cell Biology 143, no. 7 (December 28, 1998): 2033–44. http://dx.doi.org/10.1083/jcb.143.7.2033.

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The sarcoglycans are a complex of four transmembrane proteins (α, β, γ, and δ) which are primarily expressed in skeletal muscle and are closely associated with dystrophin and the dystroglycans in the muscle membrane. Mutations in the sarcoglycans are responsible for four autosomal recessive forms of muscular dystrophy. The function and the organization of the sarcoglycan complex are unknown. We have used coimmunoprecipitation and in vivo cross-linking techniques to analyze the sarcoglycan complex in cultured mouse myotubes. We demonstrate that the interaction between β- and δ-sarcoglycan is resistant to high concentrations of SDS and α-sarcoglycan is less tightly associated with other members of the complex. Cross-linking experiments show that β-, γ-, and δ-sarcoglycan are in close proximity to one another and that δ-sarcoglycan can be cross-linked to the dystroglycan complex. In addition, three of the sarcoglycans (β, γ, and δ) are shown to form intramolecular disulfide bonds. These studies further our knowledge of the structure of the sarcoglycan complex. Our proposed model of their interactions helps to explain some of the emerging data on the consequences of mutations in the individual sarcoglycans, their effect on the complex, and potentially the clinical course of muscular dystrophies.

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2

Anastasi, Giuseppe, Giuseppina Cutroneo, Antonina Sidoti, Carmen Rinaldi, Daniele Bruschetta, Giuseppina Rizzo, Rosalia D'Angelo, Guido Tarone, Aldo Amato, and Angelo Favaloro. "Sarcoglycan Subcomplex Expression in Normal Human Smooth Muscle." Journal of Histochemistry & Cytochemistry 55, no. 8 (April 4, 2007): 831–43. http://dx.doi.org/10.1369/jhc.6a7145.2007.

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The sarcoglycan complex (SGC) is a multimember transmembrane complex interacting with other members of the dystrophin–glycoprotein complex (DGC) to provide a mechanosignaling connection from the cytoskeleton to the extracellular matrix. The SGC consists of four proteins (α, β, γ, and δ). A fifth sarcoglycan subunit, ∊-sarcoglycan, shows a wider tissue distribution. Recently, a novel sarcoglycan, the ζ-sarcoglycan, has been identified. All reports about the structure of SGC showed a common assumption of a tetrameric arrangement of sarcoglycans. Addressing this issue, our immunofluorescence and molecular results showed, for the first time, that all sarcoglycans are always detectable in all observed samples. Therefore, one intriguing possibility is the existence of a pentameric or hexameric complex considering ζ-sarcoglycan of SGC, which could present a higher or lower expression of a single sarcoglycan in conformity with muscle type—skeletal, cardiac, or smooth—or also in conformity with the origin of smooth muscle. (J Histochem Cytochem 55:831–843, 2007)

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3

Hack, Andrew A., Chantal T. Ly, Fang Jiang, Cynthia J. Clendenin, Kirsten S. Sigrist, Robert L. Wollmann, and Elizabeth M. McNally. "γ-Sarcoglycan Deficiency Leads to Muscle Membrane Defects and Apoptosis Independent of Dystrophin." Journal of Cell Biology 142, no. 5 (September 7, 1998): 1279–87. http://dx.doi.org/10.1083/jcb.142.5.1279.

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γ-Sarcoglycan is a transmembrane, dystrophin-associated protein expressed in skeletal and cardiac muscle. The murine γ-sarcoglycan gene was disrupted using homologous recombination. Mice lacking γ-sarcoglycan showed pronounced dystrophic muscle changes in early life. By 20 wk of age, these mice developed cardiomyopathy and died prematurely. The loss of γ-sarcoglycan produced secondary reduction of β- and δ-sarcoglycan with partial retention of α- and ε-sarcoglycan, suggesting that β-, γ-, and δ-sarcoglycan function as a unit. Importantly, mice lacking γ-sarco- glycan showed normal dystrophin content and local- ization, demonstrating that myofiber degeneration occurred independently of dystrophin alteration. Furthermore, β-dystroglycan and laminin were left intact, implying that the dystrophin–dystroglycan–laminin mechanical link was unaffected by sarcoglycan deficiency. Apoptotic myonuclei were abundant in skeletal muscle lacking γ-sarcoglycan, suggesting that programmed cell death contributes to myofiber degeneration. Vital staining with Evans blue dye revealed that muscle lacking γ-sarcoglycan developed membrane disruptions like those seen in dystrophin-deficient muscle. Our data demonstrate that sarcoglycan loss was sufficient, and that dystrophin loss was not necessary to cause membrane defects and apoptosis. As a common molecular feature in a variety of muscular dystrophies, sarcoglycan loss is a likely mediator of pathology.

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4

Bönnemann, Carsten G., Raju Modi, Satoru Noguchi, Yuji Mizuno, Mikiharu Yoshida, Emanuela Gussoni, Elizabeth M. McNally, et al. "β–sarcoglycan (A3b) mutations cause autosomal recessive muscular dystrophy with loss of the sarcoglycan complex." Nature Genetics 11, no. 3 (November 1, 1995): 266–73. http://dx.doi.org/10.1038/ng1195-266.

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5

Bouillon, Juliette, Suzanne M. Taylor, Cheryl Vargo, Michelle Lange, Lesley A. Zwicker, Sally L. Sukut, Ling T. Guo, and G. Diane Shelton. "Beta-sarcoglycan-deficient muscular dystrophy presenting as chronic bronchopneumonia in a young cat." Journal of Feline Medicine and Surgery Open Reports 5, no. 2 (July 2019): 205511691985645. http://dx.doi.org/10.1177/2055116919856457.

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Case summaryA 5-month-old cat was evaluated for a 3 week history of cough, nasal discharge, decreased appetite and weight loss. Musculoskeletal examination was normal and serum creatine kinase (CK) activity was within the reference interval. The cat was treated during the next 10 months for chronic, persistent pneumonia. Weakness then became apparent, the cat developed dysphagia and was euthanized. Post-mortem evaluation revealed chronic aspiration pneumonia and muscular dystrophy associated with beta (β)-sarcoglycan deficiency.Relevance and novel informationThis is the first report of a cat with muscular dystrophy presenting for chronic pneumonia without obvious megaesophagus, dysphagia or prominent neuromuscular signs until late in the course of the disease. The absence of gait abnormalities, marked muscle atrophy or hypertrophy and normal serum CK activity delayed the diagnosis in this cat with β-sarcoglycan deficiency.

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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 (August 1, 2002): 407–17. http://dx.doi.org/10.1152/japplphysiol.01242.2001.

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Muscular dystrophies are a clinically and genetically heterogeneous group of disorders that show myofiber degeneration and regeneration. Identification of animal models of muscular dystrophy has been instrumental in research on the pathogenesis, pathophysiology, and treatment of these disorders. We review our understanding of the functional status of dystrophic skeletal muscle from selected animal models with a focus on 1) the mdx mouse model of Duchenne muscular dystrophy, 2) the Bio 14.6 δ-sarcoglycan-deficient hamster model of limb-girdle muscular dystrophy, and 3) transgenic null mutant murine lines of sarcoglycan (α, β, δ, and γ) deficiencies. Although biochemical data from these models suggest that the dystrophin-sarcoglycan-dystroglycan-laminin network is critical for structural integrity of the myofiber plasma membrane, emerging studies of muscle physiology suggest a more complex picture, with specific functional deficits varying considerably from muscle to muscle and model to model. It is likely that changes in muscle structure and function, downstream of the specific, primary biochemical deficiency, may alter muscle contractile properties.

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7

Salvadori, C., G. Vattemi, R. Lombardo, M. Marini, C. Cantile, and G. D. Shelton. "Muscular Dystrophy with Reduced β-Sarcoglycan in a Cat." Journal of Comparative Pathology 140, no. 4 (May 2009): 278–82. http://dx.doi.org/10.1016/j.jcpa.2008.12.003.

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8

Wang, Ruibo, Maria L. Urso, Edward J. Zambraski, Erik P. Rader, Kevin P. Campbell, and Bruce T. Liang. "Adenosine A3 receptor stimulation induces protection of skeletal muscle from eccentric exercise-mediated injury." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 299, no. 1 (July 2010): R259—R267. http://dx.doi.org/10.1152/ajpregu.00060.2010.

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Effective therapy to reduce skeletal muscle injury associated with severe or eccentric exercise is needed. The purpose of this study was to determine whether adenosine receptor stimulation can mediate protection from eccentric exercise-induced muscle injury. Downhill treadmill exercise (−15°) was used to induce eccentric exercise-mediated skeletal muscle injury. Experiments were conducted in both normal wild-type (WT) mice and also in β-sarcoglycan knockout dystrophic mice, animals that show an exaggerated muscle damage with the stress of exercise. In the vehicle-treated WT animals, eccentric exercise increased serum creatine kinase (CK) greater than 3-fold to 358.9 ± 62.7 U/l (SE). This increase was totally abolished by stimulation of the A3 receptor. In the dystrophic β-sarcoglycan-null mice, eccentric exercise caused CK levels to reach 55,124 ± 5,558 U/l. A3 receptor stimulation in these animals reduced the CK response by nearly 50%. In the dystrophic mice at rest, 10% of the fibers were found to be damaged, as indicated by Evans blue dye staining. While this percentage was doubled after exercise, A3 receptor stimulation eliminated this increase. Neither the A1 receptor agonist 2-chloro- N6-cyclopentyladenosine (0.05 mg/kg) nor the A2A receptor agonist 2- p-(2-carboxyethyl)phenethylamino-5′- N-ethylcarboxamidoadenosine (0.07 mg/kg) protected skeletal muscle from eccentric exercise injury in WT or dystrophic mice. The protective effect of adenosine A3 receptor stimulation was absent in mice, in which genes for phospholipase C β2/β3 (PLCβ2/β3) and β-sarcoglycan were deleted. The present study elucidates a new protective role of the A3 receptor and PLCβ2/β3 and points to a potentially effective therapeutic strategy for eccentric exercise-induced skeletal muscle injury.

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9

Hashimoto, Reina, and Masamitsu Yamaguchi. "Genetic link between β-sarcoglycan and the Egfr signaling pathway." Biochemical and Biophysical Research Communications 348, no. 1 (September 2006): 212–21. http://dx.doi.org/10.1016/j.bbrc.2006.07.045.

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10

Fanin, M., and C. Angelini. "Defective assembly of sarcoglycan complex in patients with β-sarcoglycan gene mutations. Study of aneural and innervated cultured myotubes." Neuropathology and Applied Neurobiology 28, no. 3 (June 2002): 190–99. http://dx.doi.org/10.1046/j.1365-2990.2002.00389.x.

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11

Camps, Jordi, Hanne Grosemans, Rik Gijsbers, Christa Maes, and Maurilio Sampaolesi. "Growth Factor Screening in Dystrophic Muscles Reveals PDGFB/PDGFRB-Mediated Migration of Interstitial Stem Cells." International Journal of Molecular Sciences 20, no. 5 (March 5, 2019): 1118. http://dx.doi.org/10.3390/ijms20051118.

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Progressive muscle degeneration followed by dilated cardiomyopathy is a hallmark of muscular dystrophy. Stem cell therapy is suggested to replace diseased myofibers by healthy myofibers, although so far, we are faced by low efficiencies of migration and engraftment of stem cells. Chemokines are signalling proteins guiding cell migration and have been shown to tightly regulate muscle tissue repair. We sought to determine which chemokines are expressed in dystrophic muscles undergoing tissue remodelling. Therefore, we analysed the expression of chemokines and chemokine receptors in skeletal and cardiac muscles from Sarcoglycan-α null, Sarcoglycan-β null and immunodeficient Sgcβ-null mice. We found that several chemokines are dysregulated in dystrophic muscles. We further show that one of these, platelet-derived growth factor-B, promotes interstitial stem cell migration. This finding provides perspective to an approachable mechanism for improving stem cell homing towards dystrophic muscles.

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12

Barresi, Rita, Valeria Confalonieri, Massimo Lanfossi, Claudia Di Blasi, Elena Torchiana, Renato Mantegazza, Laura Jarre, et al. "Concomitant deficiency of β- and γ-sarcoglycans in 20 α-sarcoglycan (adhalin)-deficient patients: immunohistochemical analysis and clinical aspects." Acta Neuropathologica 94, no. 1 (July 12, 1997): 28–35. http://dx.doi.org/10.1007/s004010050668.

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13

Diniz, G., H. Tekgul, F. Hazan, K. Yararbas, and A. Tukun. "Sarcolemmal deficiency of sarcoglycan complex in an 18-month-old Turkish boy with a large deletion in the beta sarcoglycan gene." Balkan Journal of Medical Genetics 18, no. 2 (December 1, 2015): 71–76. http://dx.doi.org/10.1515/bjmg-2015-0088.

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Abstract Limb-girdle muscular dystrophy type 2E (LGMD-2E) is caused by autosomal recessive defects in the beta sarcoglycan (SGCB) gene located on chromosome 4q12. In this case report, the clinical findings, histopathological features and molecular genetic data in a boy with β sarcoglycanopathy are presented. An 18-month-old boy had a very high serum creatinine phosphokinase (CPK) level that was accidentally determined. The results of molecular analyses for the dystrophin gene was found to be normal. He underwent a muscle biopsy which showed dystrophic features. Immunohistochemistry showed that there was a total loss of sarcolemmal sarcoglycan complex. DNA analysis revealed a large homozygous deletion in the SCGB gene. During 4 years of follow-up, there was no evidence to predict a severe clinical course except the muscle enzyme elevation and myopathic electromyography (EMG) finding. The presented milder phenotype of LGMD-2E with a large deletion in the SGCB gene provided additional support for the clinical heterogeneity and pathogenic complexity of the disease.

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14

Murugesan, Vignesh, Eva Degerman, Ann-Kristin Holmen-Pålbrink, Pontus Duner, Anki Knutsson, Anna Hultgårdh-Nilsson, and Uwe Rauch. "β-Sarcoglycan Deficiency Reduces Atherosclerotic Plaque Development in ApoE-Null Mice." Journal of Vascular Research 54, no. 4 (2017): 235–45. http://dx.doi.org/10.1159/000478014.

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15

Pegoraro, Elena, Marina Fanin, Corrado Angelini, and Eric P. Hoffman. "Prenatal diagnosis in a family affected with β-sarcoglycan muscular dystrophy." Neuromuscular Disorders 9, no. 5 (July 1999): 323–25. http://dx.doi.org/10.1016/s0960-8966(99)00020-6.

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16

Pozsgai, E. R., D. A. Griffin, K. N. Heller, J. R. Mendell, and L. R. Rodino-Klapac. "β-Sarcoglycan gene transfer decreases fibrosis and restores force in LGMD2E mice." Gene Therapy 23, no. 1 (August 20, 2015): 57–66. http://dx.doi.org/10.1038/gt.2015.80.

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17

Lim, Leland E., Franck Duclos, Odile Broux, Nathalie Bourg, Yoshihide Sunada, Valérie Allamand, Jon Meyer, et al. "β–sarcoglycan: characterization and role in limb–girdle muscular dystrophy linked to 4q12." Nature Genetics 11, no. 3 (November 1995): 257–65. http://dx.doi.org/10.1038/ng1195-257.

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18

Broux, O., F. Duclos, L. E. Lim, N. Bourg, Y. Sunada, V. Allamand, J. Meyer, et al. "β-sarcoglycan : Characterization and role in limb-girdle muscular dystrophy linked to 4q12." Neuromuscular Disorders 6, no. 2 (March 1996): S9. http://dx.doi.org/10.1016/0960-8966(96)88965-6.

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19

Perez-Ortiz, Andric C., Martha J. Peralta-Ildefonso, Esmeralda Lira-Romero, Ernesto Moya-Albor, Jorge Brieva, Israel Ramirez-Sanchez, Carmen Clapp, et al. "Lack of Delta-Sarcoglycan (Sgcd) Results in Retinal Degeneration." International Journal of Molecular Sciences 20, no. 21 (November 4, 2019): 5480. http://dx.doi.org/10.3390/ijms20215480.

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Age-related macular degeneration (AMD) is the leading cause of central vision loss and severe blindness among the elderly population. Recently, we reported on the association of the SGCD gene (encoding for δ-sarcoglycan) polymorphisms with AMD. However, the functional consequence of Sgcd alterations in retinal degeneration is not known. Herein, we characterized changes in the retina of the Sgcd knocked-out mouse (KO, Sgcd−/−). At baseline, we analyzed the retina structure of three-month-old wild-type (WT, Sgcd+/+) and Sgcd−/− mice by hematoxylin and eosin (H&E) staining, assessed the Sgcd–protein complex (α-, β-, γ-, and ε-sarcoglycan, and sarcospan) by immunofluorescence (IF) and Western blot (WB), and performed electroretinography. Compared to the WT, Sgcd−/− mice are five times more likely to have retinal ruptures. Additionally, all the retinal layers are significantly thinner, more so in the inner plexiform layer (IPL). In addition, the number of nuclei in the KO versus the WT is ever so slightly increased. WT mice express Sgcd-protein partners in specific retinal layers, and as expected, KO mice have decreased or no protein expression, with a significant increase in the α subunit. At three months of age, there were no significant differences in the scotopic electroretinographic responses, regarding both a- and b-waves. According to our data, Sgcd−/− has a phenotype that is compatible with retinal degeneration.

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20

Gastaldello, Stefano, Simona D'Angelo, Susanna Franzoso, Marina Fanin, Corrado Angelini, Romeo Betto, and Dorianna Sandonà. "Inhibition of Proteasome Activity Promotes the Correct Localization of Disease-Causing α-Sarcoglycan Mutants in HEK-293 Cells Constitutively Expressing β-, γ-, and δ-Sarcoglycan." American Journal of Pathology 173, no. 1 (July 2008): 170–81. http://dx.doi.org/10.2353/ajpath.2008.071146.

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21

Hashimoto, Reina, and Masamitsu Yamaguchi. "Dynamic Changes in the Subcellular Localization of Drosophila β-Sarcoglycan during the Cell Cycle." Cell Structure and Function 31, no. 2 (2006): 173–80. http://dx.doi.org/10.1247/csf.06025.

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22

Sewry, C. A., J. Taylor, L. V. B. Anderson, E. Ozawa, R. Pogue, F. Piccolo, K. Bushby, V. Dubowitz, and F. Muntoni. "Abnormalities in α-, β- and γ-sarcoglycan in patients with limb-girdle muscular dystrophy." Neuromuscular Disorders 6, no. 6 (December 1996): 467–74. http://dx.doi.org/10.1016/s0960-8966(96)00389-6.

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23

Bönnemann, C., J. Wong, C. Ben Hamida, M. Ben Hamida, F. Hentati, and L. Kunkel. "LGMD 2E in Tunisia is caused by a missense mutation Arg91Leu in β-sarcoglycan." Neuromuscular Disorders 7, no. 6-7 (September 1997): 460. http://dx.doi.org/10.1016/s0960-8966(97)87298-7.

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24

Draviam, Romesh A., Stuart H. Shand, and Simon C. Watkins. "The β-δ-core of sarcoglycan is essential for deposition at the plasma membrane." Muscle & Nerve 34, no. 6 (December 2006): 691–701. http://dx.doi.org/10.1002/mus.20640.

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25

Sharma, Pawan, Aruni Jha, Gerald L. Stelmack, Karen Detillieux, Sujata Basu, Thomas Klonisch, Helmut Unruh, and Andrew J. Halayko. "Characterization of the dystrophin–glycoprotein complex in airway smooth muscle: role of δ-sarcoglycan in airway responsiveness." Canadian Journal of Physiology and Pharmacology 93, no. 3 (March 2015): 195–202. http://dx.doi.org/10.1139/cjpp-2014-0389.

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The dystrophin–glycoprotein complex (DGC) is an integral part of caveolae microdomains, and its interaction with caveolin-1 is essential for the phenotype and functional properties of airway smooth muscle (ASM). The sarcoglycan complex provides stability to the dystroglycan complex, but its role in ASM contraction and lung physiology in not understood. We tested whether δ-sarcoglycan (δ-SG), through its interaction with the DGC, is a determinant of ASM contraction ex vivo and airway mechanics in vivo. We measured methacholine (MCh)-induced isometric contraction and airway mechanics in δ-SG KO and wild-type mice. Last, we performed immunoblotting and transmission electron microscopy to assess DGC protein expression and the ultrastructural features of tracheal smooth muscle. Our results reveal an age-dependent reduction in the MCh-induced tracheal isometric force and significant reduction in airway resistance at high concentrations of MCh (50.0 mg/mL) in δ-SG KO mice. The changes in contraction and lung function correlated with decreased caveolin-1 and β-dystroglycan abundance, as well as an age-dependent loss of caveolae in the cell membrane of tracheal smooth muscle in δ-SG KO mice. Collectively, these results confirm and extend understanding of a functional role for the DGC in the contractile properties of ASM and demonstrate that this results in altered lung function in vivo.

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26

Bauer, Ralf, Alison Blain, Elizabeth Greally, Kate Bushby, Hanns Lochmüller, Steve Laval, Volker Straub, and Guy A. MacGowan. "Intolerance to β-blockade in a mouse model of δ-sarcoglycan-deficient muscular dystrophy cardiomyopathy." European Journal of Heart Failure 12, no. 11 (November 2010): 1163–70. http://dx.doi.org/10.1093/eurjhf/hfq129.

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27

Beckmann, J. S., I. Richard, O. Broux, F. Fougerousse, V. Allamand, N. Chiannilkulchai, L. E. Lim, F. Duclos, N. Bourg, and L. Brenguier. "Identification of muscle-specific calpain and β-sarcoglycan genes in progressive autosomal recessive muscular dystrophies." Neuromuscular Disorders 6, no. 6 (December 1996): 455–62. http://dx.doi.org/10.1016/s0960-8966(96)00386-0.

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28

Beckmann, J. S., I. Richard, O. Broux, F. Fougerousse, N. Bourg, L. Brenguier, V. Allamand, et al. "Identification of muscle-specific calpain and β-sarcoglycan genes in progressive autosomal recessive muscular dystrophies." Neuromuscular Disorders 6, no. 2 (March 1996): S7. http://dx.doi.org/10.1016/0960-8966(96)88956-5.

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29

Andersson, Daniel C., Albano C. Meli, Steven Reiken, Matthew J. Betzenhauser, Alisa Umanskaya, Takayuki Shiomi, Jeanine D’Armiento, and Andrew R. Marks. "Leaky ryanodine receptors in β-sarcoglycan deficient mice: a potential common defect in muscular dystrophy." Skeletal Muscle 2, no. 1 (2012): 9. http://dx.doi.org/10.1186/2044-5040-2-9.

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30

Chockalingam, Priya Sethu, Rushina Cholera, Shilpa A. Oak, Yi Zheng, Harry W. Jarrett, and Donald B. Thomason. "Dystrophin-glycoprotein complex and Ras and Rho GTPase signaling are altered in muscle atrophy." American Journal of Physiology-Cell Physiology 283, no. 2 (August 1, 2002): C500—C511. http://dx.doi.org/10.1152/ajpcell.00529.2001.

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The dystrophin-glycoprotein complex (DGC) is a sarcolemmal complex whose defects cause muscular dystrophies. The normal function of this complex is not clear. We have proposed that this is a signal transduction complex, signaling normal interactions with matrix laminin, and that the response is normal growth and homeostasis. If so, the complex and its signaling should be altered in other physiological states such as atrophy. The amount of some of the DGC proteins, including dystrophin, β-dystroglycan, and α-sarcoglycan, is reduced significantly in rat skeletal muscle atrophy induced by tenotomy. Furthermore, H-Ras, RhoA, and Cdc42 decrease in expression levels and activities in muscle atrophy. When the small GTPases were assayed after laminin or β-dystroglycan depletion, H-Ras, Rac1, and Cdc42 activities were reduced, suggesting a physical linkage between the DGC and the GTPases. Dominant-negative Cdc42, introduced with a retroviral vector, resulted in fibers that appeared atrophic. These data support a putative role for the DGC in transduction of mechanical signals in muscle.

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31

Duclos, F., O. Broux, N. Bourg, V. Straub, G. L. Feldman, Y. Sunada, L. E. Lim, et al. "β-Sarcoglycan: genomic analysis and identification of a novel missense mutation in the LGMD2E Amish isolate." Neuromuscular Disorders 8, no. 1 (February 1998): 30–38. http://dx.doi.org/10.1016/s0960-8966(97)00135-1.

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32

Bönnemann, C. G., J. Wong, Ch Ben Hamida, M. Ben Hamida, F. Hentati, and L. M. Kunkel. "LGMD 2E in Tunisia is caused by a homozygous missense mutation in β-sarcoglycan exon 3." Neuromuscular Disorders 8, no. 3-4 (May 1998): 193–97. http://dx.doi.org/10.1016/s0960-8966(98)00014-5.

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33

Durbeej, Madeleine, Ronald D. Cohn, Ronald F. Hrstka, Steven A. Moore, Valérie Allamand, Beverly L. Davidson, Roger A. Williamson, and Kevin P. Campbell. "Disruption of the β-Sarcoglycan Gene Reveals Pathogenetic Complexity of Limb-Girdle Muscular Dystrophy Type 2E." Molecular Cell 5, no. 1 (January 2000): 141–51. http://dx.doi.org/10.1016/s1097-2765(00)80410-4.

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34

Pozsgai, Eric, Danielle Griffin, Kristin Heller, Jerry Mendell, and Louise Rodino-Klapac. "622. Systemic β-Sarcoglycan Gene Therapy for Treatment of Cardiac and Skeletal Muscle Deficits in LGMD2E." Molecular Therapy 24 (May 2016): S246—S247. http://dx.doi.org/10.1016/s1525-0016(16)33430-x.

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35

Pozsgai, Eric R., Danielle A. Griffin, Kristin N. Heller, Jerry R. Mendell, and Louise R. Rodino-Klapac. "506. β-Sarcoglycan Gene Transfer Prevents Muscle Fibrosis and Inflammation in an Aged LGMD2E Mouse Model." Molecular Therapy 23 (May 2015): S202—S203. http://dx.doi.org/10.1016/s1525-0016(16)34115-6.

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36

Gawlik, Kinga I., Johan Holmberg, and Madeleine Durbeej. "Loss of Dystrophin and β-Sarcoglycan Significantly Exacerbates the Phenotype of Laminin α2 Chain–Deficient Animals." American Journal of Pathology 184, no. 3 (March 2014): 740–52. http://dx.doi.org/10.1016/j.ajpath.2013.11.017.

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37

Fukai, Yuta, Yutaka Ohsawa, Hideaki Ohtsubo, Shin-ichiro Nishimatsu, Hiroki Hagiwara, Makoto Noda, Toshikuni Sasaoka, Tatsufumi Murakami, and Yoshihide Sunada. "Cleavage of β-dystroglycan occurs in sarcoglycan-deficient skeletal muscle without MMP-2 and MMP-9." Biochemical and Biophysical Research Communications 492, no. 2 (October 2017): 199–205. http://dx.doi.org/10.1016/j.bbrc.2017.08.048.

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Wakayama, Y., Masahiko Inoue, Hiroko Kojima, Makoto Murahashi, Seiji Shibuya, Takahiro Jimi, Hajime Hara, and Hiroaki Oniki. "Ultrastructural localization of α-, β- and γ-sarcoglycan and their mutual relation, and their relation to dystrophin, β-dystroglycan and β-spectrin in normal skeletal myofiber." Acta Neuropathologica 97, no. 3 (March 8, 1999): 288–96. http://dx.doi.org/10.1007/s004010050987.

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ter Laak, H. J., Q. H. Leyten, F. J. M. Gabreëls, H. Kuppen, W. O. Renier, and R. C. A. Sengers. "Laminin-α2 (merosin), β-dystroglycan, α-sarcoglycan (adhalin), and dystrophin expression in congenital muscular dystrophies: An immunohistochemical study." Clinical Neurology and Neurosurgery 100, no. 1 (March 1998): 5–10. http://dx.doi.org/10.1016/s0303-8467(97)00109-1.

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Hoshino, Sachiko, Norio Ohkoshi, Akiko Ishii, and Shin'ichi Shoji. "The expression of dystrophin, α-sarcoglycan, and β-dystroglycan during skeletal muscle regeneration: immunohistochemical and western blot studies." Acta Histochemica 104, no. 2 (January 2002): 139–47. http://dx.doi.org/10.1078/0065-1281-00620.

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O’Rourke, Erin, Louise Rodino-Klapac, Eric Pozsgai, Sarah Lewis, Danielle Griffin, Aaron Meadows, Kelly Lehman, et al. "eP212: Safety, β-Sarcoglycan expression, and functional outcomes from systemic gene transfer of rAAVrh74.MHCK7.hSGCB in LGMD2E/R4." Genetics in Medicine 24, no. 3 (March 2022): S132—S133. http://dx.doi.org/10.1016/j.gim.2022.01.248.

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Pozsgai, Eric R., Danielle A. Griffin, Kristin N. Heller, Jerry R. Mendell, and Louise R. Rodino-Klapac. "Systemic AAV-Mediated β-Sarcoglycan Delivery Targeting Cardiac and Skeletal Muscle Ameliorates Histological and Functional Deficits in LGMD2E Mice." Molecular Therapy 25, no. 4 (April 2017): 855–69. http://dx.doi.org/10.1016/j.ymthe.2017.02.013.

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Lovering, Richard M., and Patrick G. De Deyne. "Contractile function, sarcolemma integrity, and the loss of dystrophin after skeletal muscle eccentric contraction-induced injury." American Journal of Physiology-Cell Physiology 286, no. 2 (February 2004): C230—C238. http://dx.doi.org/10.1152/ajpcell.00199.2003.

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The purpose of this study was to evaluate the integrity of the muscle membrane and its associated cytoskeleton after a contraction-induced injury. A single eccentric contraction was performed in vivo on the tibialis anterior (TA) of male Sprague-Dawley rats at 900°/s throughout a 90°-arc of motion. Maximal tetanic tension (Po) of the TAs was assessed immediately and at 3, 7, and 21 days after the injury. To evaluate sarcolemmal integrity, we used an Evans blue dye (EBD) assay, and to assess structural changes, we used immunofluorescent labeling with antibodies against contractile (myosin, actin), cytoskeletal (α-actinin, desmin, dystrophin, β-spectrin), integral membrane (α- and β-dystroglycan, sarcoglycan), and extracellular (laminin, fibronectin) proteins. Immediately after injury, P0 was significantly reduced to 4.23 ± 0.22 N, compared with 8.24 ± 1.34 N in noninjured controls, and EBD was detected intracellularly in 54 ± 22% of fibers from the injured TA, compared with 0% in noninjured controls. We found a significant association between EBD-positive fibers and the loss of complete dystrophin labeling. The loss of dystrophin was notable because organization of other components of the subsarcolemmal cytoskeleton was affected minimally (β-spectrin) or not at all (α- and β-dystroglycan). Labeling with specific antibodies indicated that dystrophin's COOH terminus was selectively more affected than its rod domain. Twenty-one days after injury, contractile properties were normal, fibers did not contain EBD, and dystrophin organization and protein level returned to normal. These data indicate the selective vulnerability of dystrophin after a single eccentric contraction-induced injury and suggest a critical role of dystrophin in force transduction.

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Assereto, Stefania, Silvia Stringara, Federica Sotgia, Gloria Bonuccelli, Aldobrando Broccolini, Marina Pedemonte, Monica Traverso, et al. "Pharmacological rescue of the dystrophin-glycoprotein complex in Duchenne and Becker skeletal muscle explants by proteasome inhibitor treatment." American Journal of Physiology-Cell Physiology 290, no. 2 (February 2006): C577—C582. http://dx.doi.org/10.1152/ajpcell.00434.2005.

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In this report, we have developed a novel method to identify compounds that rescue the dystrophin-glycoprotein complex (DGC) in patients with Duchenne or Becker muscular dystrophy. Briefly, freshly isolated skeletal muscle biopsies (termed skeletal muscle explants) from patients with Duchenne or Becker muscular dystrophy were maintained under defined cell culture conditions for a 24-h period in the absence or presence of a specific candidate compound. Using this approach, we have demonstrated that treatment with a well-characterized proteasome inhibitor, MG-132, is sufficient to rescue the expression of dystrophin, β-dystroglycan, and α-sarcoglycan in skeletal muscle explants from patients with Duchenne or Becker muscular dystrophy. These data are consistent with our previous findings regarding systemic treatment with MG-132 in a dystrophin-deficient mdx mouse model (Bonuccelli G, Sotgia F, Schubert W, Park D, Frank PG, Woodman SE, Insabato L, Cammer M, Minetti C, and Lisanti MP. Am J Pathol 163: 1663–1675, 2003). Our present results may have important new implications for the possible pharmacological treatment of Duchenne or Becker muscular dystrophy in humans.

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Crippa, Stefania, Marco Cassano, Graziella Messina, Daniela Galli, Beatriz G. Galvez, Tomaz Curk, Claudia Altomare, et al. "miR669a and miR669q prevent skeletal muscle differentiation in postnatal cardiac progenitors." Journal of Cell Biology 193, no. 7 (June 27, 2011): 1197–212. http://dx.doi.org/10.1083/jcb.201011099.

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Postnatal heart stem and progenitor cells are a potential therapeutic tool for cardiomyopathies, but little is known about the mechanisms that control cardiac differentiation. Recent work has highlighted an important role for microribonucleic acids (miRNAs) as regulators of cardiac and skeletal myogenesis. In this paper, we isolated cardiac progenitors from neonatal β-sarcoglycan (Sgcb)–null mouse hearts affected by dilated cardiomyopathy. Unexpectedly, Sgcb-null cardiac progenitors spontaneously differentiated into skeletal muscle fibers both in vitro and when transplanted into regenerating muscles or infarcted hearts. Differentiation potential correlated with the absence of expression of a novel miRNA, miR669q, and with down-regulation of miR669a. Other miRNAs are known to promote myogenesis, but only miR669a and miR669q act upstream of myogenic regulatory factors to prevent myogenesis by directly targeting the MyoD 3′ untranslated region. This finding reveals an added level of complexity in the mechanism of the fate choice of mesoderm progenitors and suggests that using endogenous cardiac stem cells therapeutically will require specially tailored procedures for certain genetic diseases.

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Sharma, Pawan, Thai Tran, Gerald L. Stelmack, Karol McNeill, Reinoud Gosens, Mark M. Mutawe, Helmut Unruh, William T. Gerthoffer, and Andrew J. Halayko. "Expression of the dystrophin-glycoprotein complex is a marker for human airway smooth muscle phenotype maturation." American Journal of Physiology-Lung Cellular and Molecular Physiology 294, no. 1 (January 2008): L57—L68. http://dx.doi.org/10.1152/ajplung.00378.2007.

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Airway smooth muscle (ASM) cells may contribute to asthma pathogenesis through their capacity to switch between a synthetic/proliferative and a contractile phenotype. The multimeric dystrophin-glycoprotein complex (DGC) spans the sarcolemma, linking the actin cytoskeleton and extracellular matrix. The DGC is expressed in smooth muscle tissue, but its functional role is not fully established. We tested whether contractile phenotype maturation of human ASM is associated with accumulation of DGC proteins. We compared subconfluent, serum-fed cultures and confluent cultures subjected to serum deprivation, which express a contractile phenotype. Western blotting confirmed that β-dystroglycan, β-, δ-, and ε-sarcoglycan, and dystrophin abundance increased six- to eightfold in association with smooth muscle myosin heavy chain (smMHC) and calponin accumulation during 4-day serum deprivation. Immunocytochemistry showed that the accumulation of DGC subunits was specifically localized to a subset of cells that exhibit robust staining for smMHC. Laminin competing peptide (YIGSR, 1 μM) and phosphatidylinositol 3-kinase (PI3K) inhibitors (20 μM LY-294002 or 100 nM wortmannin) abrogated the accumulation of smMHC, calponin, and DGC proteins. These studies demonstrate that the accumulation of DGC is an integral feature for phenotype maturation of human ASM cells. This provides a strong rationale for future studies investigating the role of the DGC in ASM smooth muscle physiology in health and disease.

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Ikeda, Yasuhiro, Maryann Martone, Yusu Gu, Masahiko Hoshijima, Andrea Thor, Sam S. Oh, Kirk L. Peterson, and John Ross. "Altered membrane proteins and permeability correlate with cardiac dysfunction in cardiomyopathic hamsters." American Journal of Physiology-Heart and Circulatory Physiology 278, no. 4 (April 1, 2000): H1362—H1370. http://dx.doi.org/10.1152/ajpheart.2000.278.4.h1362.

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A mutation in the δ-sarcoglycan (SG) gene with absence of δ-SG protein in the heart has been identified in the BIO14.6 cardiomyopathic (CM) hamster, but how the defective gene leads to myocardial degeneration and dysfunction is unknown. We correlated left ventricular (LV) function with increased sarcolemmal membrane permeability and investigated the LV distribution of the dystrophin-dystroglycan complex in BIO14.6 CM hamsters. On echocardiography at 5 wk of age, the CM hamsters showed a mildly enlarged diastolic dimension (LVDD) with decreased LV percent fractional shortening (%FS), and at 9 wk further enlargement of LVDD with reduction of %FS was observed. The percent area of myocardium exhibiting increased membrane permeability or membrane rupture, assessed by Evans blue dye (EBD) staining and wheat germ agglutinin, was greater at 9 than at 5 wk. In areas not stained by EBD, immunostaining of dystrophin was detected in CM hamsters at sarcolemma and T tubules, as expected, but it was also abnormally expressed at the intercalated discs; in addition, the expression of β-dystroglycan was significantly reduced compared with control hearts. As previously described, α-SG was completely deficient in CM hearts compared with control hearts. In myocardial areas showing increased sarcolemmal permeability, neither dystrophin nor β-dystroglycan could be identified by immunolabeling. Thus, together with the known loss of δ-SG and other SGs, abnormal distribution of dystrophin and reduction of β-dystroglycan are associated with increased sarcolemmal permeability followed by cell rupture, which correlates with early progressive cardiac dysfunction in the BIO14.6 CM hamster.

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Sylvius, Nicolas, Laetitia Duboscq-Bidot, Christiane Bouchier, Philippe Charron, Abdelaziz Benaiche, Pascale Sébillon, Michel Komajda, and Eric Villard. "Mutational analysis of the β- and δ-sarcoglycan genes in a large number of patients with familial and sporadic dilated cardiomyopathy." American Journal of Medical Genetics Part A 120A, no. 1 (January 16, 2003): 8–12. http://dx.doi.org/10.1002/ajmg.a.20003.

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Fernández-Eulate, Gorka, France Leturcq, Pascal Laforêt, Isabelle Richard, and Tanya Stojkovic. "Les sarcoglycanopathies." médecine/sciences 36 (December 2020): 22–27. http://dx.doi.org/10.1051/medsci/2020243.

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Les sarcoglycanopathies font partie des dystrophies musculaires des ceintures (LGMD) autosomiques récessives et représentent la troisième cause la plus fréquente d’entre elles. Elles sont consécutives à un déficit d’un des sarcoglycanes α, β, γ, ou δ. La présentation clinique habituelle est celle d’une atteinte symétrique des muscles des ceintures pelvienne et scapulaire ainsi que du tronc, associée à une atteinte cardiorespiratoire plus ou moins sévère et une élévation franche des créatine-phospho-kinases (CPK). Les premiers symptômes apparaissent au cours de la première décennie, la perte de la marche survenant souvent au cours de la deuxième décennie. Les lésions sont de type dystrophique sur la biopsie musculaire. Il s’y associe une diminution ou une absence d’immunomarquage du sarcoglycane correspondant au gène muté, et dans une moindre mesure des trois autres sarcoglycanes associés. De nombreuses mutations ont été rapportées dans les quatre gènes impliqués et quelques-unes d’entre elles sont prépondérantes dans certaines populations. à ce jour, il n’existe pas de traitement curatif ce qui n’empêche pas de voir se développer de nombreux essais cliniques, notamment en thérapie génique.

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Rodino-Klapac, L., E. Pozsgai, S. Lewis, D. Griffin, A. Meadows, K. Lehman, K. Church, et al. "P.170 Safety, β-sarcoglycan expression, and functional outcomes from systemic gene transfer of bidridistrogene xeboparvovec in limb-girdle muscular dystrophy type 2E/R4." Neuromuscular Disorders 32 (October 2022): S116. http://dx.doi.org/10.1016/j.nmd.2022.07.308.

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