Characterization of excitation-contraction coupling components in human extraocular muscles

Biochemical Journal

Volumn 466, Issue , 2015, Pages 29-36

  Sekulic Jablanovic, Marijana ^a   Palmowski Wolfe, Anja ^a   Zorzato, Francesco ^b   Treves, Susan ^b  

^a UNIVERSITY HOSPITAL BASEL   (Switzerland)

^b UNIVERSITY OF FERRARA   (Italy)

Author keywords

Calcium homoeostasis; Excitation contraction coupling; Gene expression

Indexed keywords

1,4 DIHYDROPYRIDINE RECEPTOR; CALCIUM; CALSEQUESTRIN; RYANODINE RECEPTOR 1; RYANODINE RECEPTOR 2; CALCIUM CHANNEL L TYPE; CASQ2 PROTEIN, HUMAN; PROTEIN SUBUNIT; RYANODINE RECEPTOR;

ARTICLE; CALCIUM HOMEOSTASIS; CELL MEMBRANE; CELLULAR DISTRIBUTION; CENTRAL CORE DISEASE; CENTRONUCLEAR MYOPATHY; EXCITATION CONTRACTION COUPLING; EXTRAOCULAR MUSCLE; GENE EXPRESSION; GENE MUTATION; HUMAN; HUMAN CELL; MULTIMINICORE DISEASE; MUSCLE BIOPSY; MYOPATHY; OPHTHALMOPLEGIA; PRIORITY JOURNAL; PROTEIN EXPRESSION; UPREGULATION; CALCIUM SIGNALING; CELL DIFFERENTIATION; CYTOLOGY; GENE EXPRESSION PROFILING; GENE EXPRESSION REGULATION; GENETIC TRANSCRIPTION; GENETICS; METABOLISM; MUSCLE CELL; MUTATION; ORBIT; PHYSIOLOGY; PRIMARY CELL CULTURE; PROTEIN SUBUNIT; SKELETAL MUSCLE;

CALCIUM; CALCIUM CHANNELS, L-TYPE; CALCIUM SIGNALING; CALSEQUESTRIN; CELL DIFFERENTIATION; EXCITATION CONTRACTION COUPLING; GENE EXPRESSION PROFILING; GENE EXPRESSION REGULATION; HUMANS; MUSCLE CELLS; MUSCLE, SKELETAL; MUTATION; ORBIT; PRIMARY CELL CULTURE; PROTEIN SUBUNITS; RYANODINE RECEPTOR CALCIUM RELEASE CHANNEL; TRANSCRIPTION, GENETIC;

EID: 84922331130     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20140970     Document Type: Article

References (44)

1. Porter, J.D., Baker, R.S., Ragusa, R.J. and Brueckner, J.K. (1995) Extraocular muscles: basic and clinical aspects of structure and function. Surv. Ophthalmol. 39, 451-484
2. Hoh, J.F.Y., Hughes, S., Hugh, G. and Pozgaj, I. (1989) Three hierarchies in skeletal muscle fibre classification: allotype, isotype and phenotype. In UCLA Symposia on Molecular and Cellular Biology (Stockdale, F. and Kedes, L., eds), pp. 15-26, Alan R. Liss, New York
3. Hauschka, S.D. (1994) The embryonic origin of muscle. In Myology (Engel, A.G. and Franzini-Armstrong, C., eds), pp. 3-73, McGraw Hill, New York
4. Spencer, R.F. and Porter, J.D. (2006) Structural organization of the extraocular muscles. In Neuroanatomy of the Oculomotor System (Reviews in Oculomotor Research Vol. 2) (Buttner-Ennever, J.A., ed.), pp. 33-73, Elsevier, New York
5. Ketterer, C., Zeiger, U., Budak, M.T., Rubinstein, N.A. and Khurana, T.S. (2010) Identification of the neuromuscular junction transcriptome of extraocular muscle by laser capture microdissection. Invest. Ophthalmol. Vis. Sci. 51, 4589-4599
6. Fischer, M.D., Budak, M.T., Bakay, M., Gorospe, J.R., Kjellgren, D., Pedrosa-Domellof, F., Hoffman, E.P. and Khurana, T.S. (2005) Definition of the unique human extraocular muscle allotype by expression profiling. Physiol. Genomics 22, 283-291
7. Fleischer, S. and Inui, M. (1989) Biochemistry and biophysics of excitation-contraction coupling. Annu. Rev. Biophys. Biophys. Chem. 18, 333-364
8. Van Petegem, F. (2011) Ryanodine receptors: structure and function. J. Biol. Chem. 287, 31624-31632
9. Robinson, R., Carpenter, D., Shaw, M.A., Halsall, J. and Hopkins, P. (2006) Mutations in RYR1 in malignant hyperthermia and central core disease. Hum. Mutat. 27, 977-989
10. Hwang, J.H., Zorzato, F., Clarke, N.F. and Treves, S. (2012) Mapping domains and mutations on the skeletal muscle ryanodine receptor channel. Trends Mol. Med. 18, 644-657
11. Jungbluth, H. (2007) Multi-minicore disease. Orphanet J. Rare Dis. 2, 31
12. Jungbluth, H., Zhou, H., Hartley, L., Halliger-Keller, B., Messina, S., Longman, C., Brockington, M., Robb, S.A., Straub, V., Voit, T. et al. (2005) Minicore myopathy with ophthalmoplegia caused by mutations in the ryanodine receptor type 1 gene. Neurology 65, 1930-1935
13. Clarke, N.F., Waddell, L.B., Cooper, S.T., Perry, M., Smith, R.L., Kornberg, A.J., Muntoni, F., Lillis, S., Straub, V., Bushby, K. et al. (2010) Recessive mutations in RYR1 are a common cause of congenital fiber type disproportion. Hum. Mutat. 31, E1544-E1550
14. Wilmshurst, J.M., Lillis, S., Zhou, H., Pillay, K., Henderson, H., Kress, W., M?uller, C.R., Ndondo, A., Cloke, V., Cullup, T. et al. (2010) RYR1 mutations are a common cause of congenital myopathies with central nuclei. Ann. Neurol. 68, 717-726
15. Treves, S., Jungbluth, H., Muntoni, F. and Zorzato, F. (2008) Congenital muscle disorders with cores: the ryanodine receptor calcium channel paradigm. Curr. Opin. Pharmacol. 8, 319-326
16. Shaaban, S., Ramos-Platt, L., Gilles, F.H., Chan, W.M., Andrews, C., De Girolami, U., Derner, J. and Engle, E.C. (2013) RYR1 mutations as a cause of ophthalmoplegia, facial weakness, and malignant hyperthermia. JAMA Ophthalmol. 131, 1532-1540
17. Kaminski, H.J. and Ruff, R.L. (1997) Ocular muscle involvement by myasthenia gravis. Ann. Neurol. 41, 419-420
18. Kaminski, H.J., Al-Hakim, M., Leigh, R.J., Katirji, M.B. and Ruff, R.L. (1992) Extraocular muscles are spared in advanced Duchenne dystrophy. Ann. Neurol. 32, 586-588
19. Khurana, T.S., Prendergast, R.A., Alameddine, H.S., Tome, F.M., Fardeau, M., Arahata, K., Sugita, H. and Kunkel, L.M. (1995) Absence of extraocular muscle pathology in Duchenne's muscular dystrophy: role for calcium homeostasis in extraocular muscle sparing. J. Exp. Med. 182, 467-475
20. Kallestad, K.M., Hebert, S.L., McDonald, A.A., Daniel, M.L., Cu, S.R. and McLoon, L. K. (2011) Sparing of extraocular muscle in aging and muscular distrophies: a myogenig precursor cell hypothesis. Exp. Cell Res. 317, 873-885
21. Censier, K., Urwyler, A., Zorzato, F. and Treves, S. (1998) 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. 101, 1233-1242
22. Ducreux, S., Zorzato, F., Müller, C., Sewry, C., Muntoni, F., Quinlivan, R., Restagno, G., Girard, T. and Treves, S. (2004) Effect of ryanodine receptor mutations on IL-6 release and intracellular calcium homeostasis in human myotubes from malignant hyperthermia susceptible individuals and patients affected by central core disease. J. Biol. Chem. 279, 43838-43846
23. Vukcevic, M., Zorzato, F., Keck, S., Tsakiris, D.A., Keiser, J., Maizels, R.M. and Treves, S. (2013) Gain of function in the immune system caused by a ryanodine receptor 1 mutation. J. Cell Sci. 126, 3485-3492
24. 2 + entry induces nuclear translocation of NFAT and contributes to IL-6 release from myotubes from patients with central core disease. Hum. Mol. Genet. 20, 589-600
25. Rokach, O., Ullrich, N.D., Rausch, M., Mouly, V., Zhou, H., Muntoni, F., Zorzato, F. and Treves, S. (2013) Establishment of a human skeletal muscle-derived cell line: biochemical, cellular and electrophysiological characterization. Biochem. J. 455, 169-177
26. Anderson, A.A., Treves, S., Biral, D., Betto, R., Sandon'a, D., Ronjat, M. and Zorzato, F. (2003) The novel skeletal muscle sarcoplasmic reticulum JP-45 protein: molecular cloning, tissue distribution, developmental expression, and interaction with α 1.1 subunit of the voltage-gated calcium channel. J. Biol. Chem. 278, 39987-39992
27. Cherednichenko, G., Hurne, A.M., Fessenden, J.D., Lee, E.H., Allen, P.D., Beam, K.G. and Pessah, I.N. (2004) Conformational activation of calcium entry by depolarisation of skeletal muscle myotubes. Proc. Natl. Acad. Sci. U.S.A. 101, 15793-15798
28. 2 + entry. J. Gen. Physiol. 133, 79-91
29. Porter, J.D., Khanna, S., Kaminski, H.J., Rao, J.S., Merriam, A.P., Richmonds, C.R., Leahy, P., Li, J. and Andrade, P.H. (2001) Extraocular muscle is defined by a fundamentally distinct gene expression profile. Proc. Natl. Acad. Sci. U.S.A. 98, 12062-12067
30. Altick, A.L., Feng, C.Y., Schlauch, K., Johnson, L.A. and von Barthold, C.S. (2012) Differences in gene expression between expression between strabismic and normal human extraocular muscles. Invest. Ophthalmol. Vis. 53, 5168-5177
31. Kjellgren, D., Ryan, M., Ohlendieck, K., Thornell, L.E. and Pedrosa-Domell öf, F. (2003) Sarco(endo)plasmic reticulum Ca2 + ATPases (SERCA1 and-2) in human extraocular muscles. Invest. Ophthalmol. Vis. Sci. 44, 5057-5062
32. Wescombe, L., Lahooti, H., Gopinath, B. and Wall, J.R. (2010) The cardiac calsequestrin gene (CASQ2) is up-regulated in the thyroid in patients with Grave's ophthalmopathy: support for a role of autoimmunity against calsequestrin as the triggering event. Clin. Endocrinol. 73, 522-528
33. Slupsky, J.R., Ohnishi, M., Carpenter, M.R. and Reithemier, R.A. (1987) Characterization of cardiac calsequestrin. Biochemistry 26, 6539-6544
34. Cala, S.E. and Jones, L.R. (1991) Phosphorylation of cardiac and skeletal muscle calsequestrin isoforms by casein kinase II. J. Biol. Chem. 266, 391-398 PubMed
35. Sanchez, E.J., Muske, G.R., Criswell, A., Milting, H., Dunker, A.K. and Kang, C. (2011) Phosphorylation of human calsequestin: implications for calcium regulation. Mol. Cell. Biochem. 353, 195-204
36. Nabauer, M., Callewaert, G., Cleemann, L. and Morad, M. (1989) Regulation of calcium release is gated by calcium current, not gating charge, in cardiac myocytes. Science 244, 800-803
37. Berridge, M.J. (2008) Smooth muscle cell activation mechanisms. J. Physiol. 586, 5047-5061
38. Zeiger, U., Mitchell, C.H. and Khurana, T.S. (2010) Superior calcium homeostasis of extraocular muscles. Exp. Eye Res. 91, 613-622
39. Heizmann, C.W., Berchtold, M.W. and Rowlerson, A.M. (1982) Correlation of parvalbumin concentration with relaxation speed in mammalian muscles. Proc. Natl. Acad. Sci. U.S.A. 79, 7243-7247
40. Stuhlfauth, I., Reininghaus, J., Jockusch, H. and Heizmann, C.W. (1984) Calcium-binding protein, parvalbumin, is reduced in mutant mammalian muscle with abnormal contractile properties. Proc. Natl. Acad. Sci. U.S.A. 81, 4814-4818
41. Yoshida, M., Minamisawa, S., Shimura, M., Komazaki, S., Kume, H., Zhang, M., Matsumura, K., Nishi, M., Saito, M., Saeki, Y. et al. (2005) Impaired Ca2 + store functions in skeletal and cardiac muscle cells from sarcalumenin-deficient mice. J. Biol. Chem. 280, 3500-3506
42. Cherednichenko, G., Hurne, A.M., Fessenden, J., Lee, E.H., Allen, P.D., Beam, K.G. and Pessah, I.N. (2004) Conformational activation of Ca2 + entry by depolarization of skeletal myotubes. Proc. Natl. Acad. Sci. U.S.A. 101, 15793-15798
43. Mosca, B., Delbono, O., Messi, M.L., Bergamelli, L., Wang, Z.M., Vukcevic, M., Lopez, R., Treves, S., Nishi, M., Takeshima, H. et al. (2103) Enhanced dihydropyridine receptor channel activity restores muscle strength in JP45/CASQ1 double knockout mice. Nat. Commun. 4, 1541
44. Kalhovde, J.M., Jerkovic, R., Sefland, I., Cordonnier, C., Calantibodiesria, E., Schiaffino, S. and Lømo, T. (2005) "Fast" and "slow" muscle fibres in hindlimb muscles of adult rats regenerate from intrinsically different satellite cells. J. Physiol. 562, 847-857