Adenovirus-mediated expression of myogenic differentiation factor 1 (MyoD) in equine and human dermal fibroblasts enables their conversion to caffeine-sensitive myotubes

Neuromuscular Disorders

Volumn 24, Issue 3, 2014, Pages 250-258

  Fernandez Fuente, Marta ^a   Martin Duque, Pilar ^b   Vassaux, Georges ^c   Brown, Susan C ^a   Muntoni, Francesco ^d   Terracciano, Cesare M ^e   Piercy, Richard J ^a  

^a ROYAL VETERINARY COLLEGE   (United Kingdom)

^b UNIVERSIDAD FRANCISCO DE VITORIA   (Spain)

^c Laboratoire TIRO   (France)

^d UNIVERSITY COLLEGE LONDON   (United Kingdom)

^e HAREFIELD HOSPITAL   (United Kingdom)

Author keywords

Adenovirus; Calcium; Equine; Exertional rhabdomyolysis; Malignant hyperthermia; MyoD

Indexed keywords

ADENOVIRUS; CALCIUM; EQUINE; EXERTIONAL RHABDOMYOLYSIS; MALIGNANT HYPERTHERMIA; MYOD;

ADENOVIRIDAE; ANIMALS; CAFFEINE; CELLS, CULTURED; DERMIS; FIBROBLASTS; HORSES; HUMANS; MALE; MUSCLE FIBERS, SKELETAL; MYOD PROTEIN;

EID: 84894272501     PISSN: 09608966     EISSN: 18732364     Source Type: Journal    
DOI: 10.1016/j.nmd.2013.11.009     Document Type: Article

References (44)

1. Cole F.L., Mellor D.J., Hodgson D.R., Reid S.W. Prevalence and demographic characteristics of exertional rhabdomyolysis in horses in Australia. Vet Rec 2004, 155:625-630.
2. MacLeay J.M., Sorum S.A., Valberg S.J., Marsh W.E., Sorum M.D. Epidemiologic analysis of factors influencing exertional rhabdomyolysis in Thoroughbreds. Am J Vet Res 1999, 60:1562-1566.
3. Upjohn M.M., Archer R.M., Christley R.M., McGowan C.M. Incidence and risk factors associated with exertional rhabdomyolysis syndrome in National Hunt racehorses in Great Britain. Vet Rec 2005, 156:763-766.
4. Herszberg B., McCue M.E., Larcher T., et al. A GYS1 gene mutation is highly associated with polysaccharide storage myopathy in Cob Normand draught horses. Anim Genet 2009, 40:94-96.
5. McCue M.E., Anderson S.M., Valberg S.J., et al. Estimated prevalence of the type 1 polysaccharide storage myopathy mutation in selected North American and European breeds. Anim Genet 2010, 41(Suppl. 2):145-149.
6. McCue M.E., Valberg S.J., Lucio M., Mickelson J.R. Glycogen synthase 1 (GYS1) mutation in diverse breeds with polysaccharide storage myopathy. J Vet Intern Med 2008, 22:1228-1233.
7. Stanley R.L., McCue M.E., Valberg S.J., et al. A glycogen synthase 1 mutation associated with equine polysaccharide storage myopathy and exertional rhabdomyolysis occurs in a variety of UK breeds. Equine Vet J 2009, 41:597-601.
8. McCue M.E., Valberg S.J., Miller M.B., et al. Glycogen synthase (GYS1) mutation causes a novel skeletal muscle glycogenosis. Genomics 2008, 91:458-466.
9. Lentz L.R., Valberg S.J., Balog E.M., Mickelson J.R., Gallant E.M. Abnormal regulation of muscle contraction in horses with recurrent exertional rhabdomyolysis. Am J Vet Res 1999, 60:992-999.
10. Beech J., Lindborg S., Fletcher J.E., Lizzo F., Tripolitis L., Braund K. Caffeine contractures, twitch characteristics and the threshold for Ca(2+)-induced Ca2+ release in skeletal muscle from horses with chronic intermittent rhabdomyolysis. Res Vet Sci 1993, 54:110-117.
11. Larach M.G. Standardization of the caffeine halothane muscle contracture test. North American Malignant Hyperthermia Group. Anesth Analg 1989, 69:511-515.
12. Temh G. A protocol for the investigation of malignant hyperpyrexia (MH) susceptibility. The European Malignant Hyperpyrexia Group. Br J Anaesth 1984, 56:1267-1269.
13. Isgren C.M., Upjohn M.M., Fernandez-Fuente M., et al. Epidemiology of exertional rhabdomyolysis susceptibility in standardbred horses reveals associated risk factors and underlying enhanced performance. PLoS One 2010, 5:e11594.
14. Aleman M., Nieto J.E., Magdesian K.G. Malignant hyperthermia associated with ryanodine receptor 1 (C7360G) mutation in Quarter Horses. J Vet Intern Med 2009, 23:329-334.
15. Censier K., Urwyler A., Zorzato F., Treves S. Intracellular calcium homeostasis in human primary muscle cells from malignant hyperthermia-susceptible and normal individuals. Effect of overexpression of recombinant wild-type and Arg163Cys mutated ryanodine receptors. J Clin Invest 1998, 101:1233-1242.
16. Ducreux S., Zorzato F., Muller C., et al. Effect of ryanodine receptor mutations on interleukin-6 release and intracellular calcium homeostasis in human myotubes from malignant hyperthermia-susceptible individuals and patients affected by central core disease. J Biol Chem 2004, 279:43838-43846.
17. Girard T., Treves S., Censier K., Mueller C.R., Zorzato F., Urwyler A. Phenotyping malignant hyperthermia susceptibility by measuring halothane-induced changes in myoplasmic calcium concentration in cultured human skeletal muscle cells. Br J Anaesth 2002, 89:571-579.
18. Wehner M., Rueffert H., Koenig F., Olthoff D. Functional characterization of malignant hyperthermia-associated RyR1 mutations in exon 44, using the human myotube model. Neuromuscul Disord 2004, 14:429-437.
19. Zacharias J.M., Anderson J.E. Muscle regeneration after imposed injury is better in younger than older mdx dystrophic mice. J Neurol Sci 1991, 104:190-196.
20. Zammit P., Beauchamp J. The skeletal muscle satellite cell: stem cell or son of stem cell?. Differentiation 2001, 68:193-204.
21. Choi J., Costa M.L., Mermelstein C.S., Chagas C., Holtzer S., Holtzer H. MyoD converts primary dermal fibroblasts, chondroblasts, smooth muscle, and retinal pigmented epithelial cells into striated mononucleated myoblasts and multinucleated myotubes. Proc Natl Acad Sci USA 1990, 87:7988-7992.
22. Fernandez-Fuente M., Ames E.G., Wagner M.L., et al. Assessment of the transformation of equine skin-derived fibroblasts to multinucleated skeletal myotubes following lentiviral-induced expression of equine myogenic differentiation 1. Am J Vet Res 2008, 69:1637-1645.
23. Lattanzi L., Salvatori G., Coletta M., et al. High efficiency myogenic conversion of human fibroblasts by adenoviral vector-mediated MyoD gene transfer. An alternative strategy for ex vivo gene therapy of primary myopathies. J Clin Invest 1998, 101:2119-2128.
24. Weintraub H., Tapscott S.J., Davis R.L., et al. Activation of muscle-specific genes in pigment, nerve, fat, liver, and fibroblast cell lines by forced expression of MyoD. Proc Natl Acad Sci USA 1989, 86:5434-5438.
25. Piercy R.J., Zhou H., Feng L., Pombo A., Muntoni F., Brown S.C. Desmin immunolocalisation in autosomal dominant Emery-Dreifuss muscular dystrophy. Neuromuscul Disord 2007, 17:297-305.
26. Niessen S.J., Fernandez-Fuente M., Mahmoud A., et al. Novel diabetes mellitus treatment: mature canine insulin production by canine striated muscle through gene therapy. Domest Anim Endocrinol 2012, 43:16-25.
27. Zhou H., Yamaguchi N., Xu L., et al. Characterization of recessive RYR1 mutations in core myopathies. Hum Mol Genet 2006, 15:2791-2803.
28. Mancheno-Corvo P., Martin-Duque P. Viral gene therapy. Clin Transl Oncol 2006, 8:858-867.
29. Walther W.S.U. Viral vectors for gene transfer: a review of their use in the treatment of human diseases. Drugs 2000, 60:249-271.
30. Asakura A., Hirai H., Kablar B., et al. Increased survival of muscle stem cells lacking the MyoD gene after transplantation into regenerating skeletal muscle. Proc Natl Acad Sci USA 2007, 104:16552-16557.
31. Kuang S., Kuroda K., Le Grand F., Rudnicki M.A. Asymmetric self-renewal and commitment of satellite stem cells in muscle. Cell 2007, 129:999-1010.
32. Montarras D., Morgan J., Collins C., et al. Direct isolation of satellite cells for skeletal muscle regeneration. Science 2005, 309:2064-2067.
33. He T.C., Zhou S., da Costa L.T., Yu J., Kinzler K.W., Vogelstein B. A simplified system for generating recombinant adenoviruses. Proc Natl Acad Sci USA 1998, 95:2509-2514.
34. Martín-Duque P.Q., McNeish M., Lopes I., et al. Caspase-1 as a radio- and chemo-sensitiser in vitro and in vivo. Int J Mol Med 2007, 17:841-847.
35. Tapscott S.J. The circuitry of a master switch: Myod and the regulation of skeletal muscle gene transcription. Development 2005, 132:2685-2695.
36. Tilgen N., Zorzato F., Halliger-Keller B., et al. Identification of four novel mutations in the C-terminal membrane spanning domain of the ryanodine receptor 1: association with central core disease and alteration of calcium homeostasis. Hum Mol Genet 2001, 10:2879-2887.
37. Xu L.W.Y., Yamaguchi N., Pasek D.A., Meissner G. Single channel properties of heterotetrameric mutant RyR1 ion channels linked to core myopathies. J Biol Chem 2008, 7:6321-6329.
38. Guis S., Figarella-Branger D., Monnier N., et al. Multiminicore disease in a family susceptible to malignant hyperthermia: histology, in vitro contracture tests, and genetic characterization. Arch Neurol 2004, 61:106-113.
39. Lyfenko A.D., Ducreux S., Wang Y., et al. Two central core disease (CCD) deletions in the C-terminal region of RYR1 alter muscle excitation-contraction (EC) coupling by distinct mechanisms. Hum Mutat 2007, 28:61-68.
40. Treves S., Anderson A.A., Ducreux S., et al. Ryanodine receptor 1 mutations, dysregulation of calcium homeostasis and neuromuscular disorders. Neuromuscul Disord 2005, 15:577-587.
41. Treves S., Vukcevic M., Jeannet P.Y., et al. Enhanced excitation-coupled Ca(2+) entry induces nuclear translocation of NFAT and contributes to IL-6 release from myotubes from patients with central core disease. Hum Mol Genet 2011, 20:589-600.
42. Bendahan D., Guis S., Monnier N., et al. Comparative analysis of in vitro contracture tests with ryanodine and a combination of ryanodine with either halothane or caffeine: a comparative investigation in malignant hyperthermia. Acta Anaesthesiol Scand 2004, 48:1019-1027.
43. Dlamini N., Voermans N.C., Lillis S., et al. Mutations in RYR1 are a common cause of exertional myalgia and rhabdomyolysis. Neuromuscul Disord 2013, 23:540-548.
44. Roelvink P.W., Lizonova A., Lee J.G., et al. The coxsackievirus-adenovirus receptor protein can function as a cellular attachment protein for adenovirus serotypes from subgroups A, C, D, E, and F. J Virol 1998, 72:7909-7915.