Altered stored calcium release in skeletal myotubes deficient of triadin and junctin

Cell Calcium

Volumn 45, Issue 1, 2009, Pages 29-37

  Wang, Ying ^a,b   Li, Xinghai ^a,b   Duan, Hongzhe ^a   Fulton, Timothy R ^a,b   Eu, Jerry P ^c   Meissner, Gerhard ^a,b  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF NORTH CAROLINA   (United States)

^c DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

C2C12 myotubes; Calcium release; Junctin; Ryanodine receptor; Sarcoplasmic reticulum; Triadin

Indexed keywords

CAFFEINE; CALCIUM ION; CALSEQUESTRIN; CHLOROCRESOL; JUNCTIN; MEMBRANE PROTEIN; MESSENGER RNA; POTASSIUM CHLORIDE; RYANODINE RECEPTOR 1; SMALL INTERFERING RNA; THAPSIGARGIN; TRIADIN; UNCLASSIFIED DRUG; URIDINE TRIPHOSPHATE;

ANIMAL CELL; ARTICLE; CALCIUM SIGNALING; CALCIUM TRANSPORT; CONTROLLED STUDY; DEPOLARIZATION; DOWN REGULATION; GENE EXPRESSION; MOUSE; MYOTUBE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; SARCOPLASMIC RETICULUM; SKELETAL MUSCLE;

EID: 58149110941     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceca.2008.05.006     Document Type: Article

References (40)

1. Franzini-Armstrong C., and Protasi F. Ryanodine receptors of striated muscles: a complex channel capable of multiple interactions. Physiol. Rev. 77 (1997) 699-729
2. Guo W., and Campbell K.P. Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum. J. Biol. Chem. 270 (1995) 9027-9030
3. Beard N.A., Laver D.R., and Dulhunty A.F. Calsequestrin and the calcium release channel of skeletal and cardiac muscle. Prog. Biophys. Mol. Biol. 85 (2004) 33-69
4. Goonasekera S.A., Beard N.A., Groom L., et al. Triadin binding to the C-terminal luminal loop of the ryanodine receptor is important for skeletal muscle excitation contraction coupling. J. Gen. Physiol. 130 (2007) 365-378
5. Lee J.M., Rho S.H., Shin D.W., et al. Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin. J. Biol. Chem. 279 (2004) 6994-7000
6. Knudson C.M., Stang K.K., Moomaw C.R., Slaughter C.A., and Campbell K.P. Primary structure and topological analysis of a skeletal muscle-specific junctional sarcoplasmic reticulum glycoprotein (triadin). J. Biol. Chem. 268 (1993) 12646-12654
7. Taske N.L., Eyre H.J., RO O.B., Sutherland G.R., Denborough M.A., and Foster P.S. Molecular cloning of the cDNA encoding human skeletal muscle triadin and its localisation to chromosome 6q22-6q23. Eur. J. Biochem. 233 (1995) 258-265
8. Guo W., Jorgensen A.O., and Campbell K.P. Triadin, a linker for calsequestrin and the ryanodine receptor. Soc. Gene. Physiol. Ser. 51 (1996) 19-28
9. Kobayashi Y.M., and Jones J.R. Identification of triadin 1 as the predominant triadin isoform expressed in mammalian myocardium. J. Biol. Chem. 274 (1999) 28660-28668
10. Marty I., Thevenon D., Scotto C., et al. Cloning and characterization of a new isoform of skeletal muscle triadin. J. Biol. Chem. 275 (2000) 8206-8212
11. Hong C.S., Ji J.H., Kim J.P., Jung D.H., and Kim D.H. Molecular cloning and characterization of mouse cardiac triadin isoforms. Gene 278 (2001) 193-199
12. Brandt N.R., Caswell A.H., Wen S.R., and Talvenheimo J.A. Molecular interactions of the junctional foot protein and dihydropyridine receptor in skeletal muscle triads. J. Membr. Biol. 113 (1990) 237-251
13. Kim K.C., Caswell A.H., Talvenheimo J.A., and Brandt N.R. Isolation of a terminal cisterna protein which may link the dihydropyridine receptor to the junctional foot protein in skeletal muscle. Biochemistry 29 (1990) 9281-9289
14. Kobayashi Y.M., Alseikhan B.A., and Jones L.R. Localization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction. J. Biol. Chem. 275 (2000) 17639-17646
15. 2+ transients in triadin-binding deficient-RYR1 mutants. Biochem. Biophys. Res. Commun. 351 (2006) 909-914
16. Ohkura M., Furukawa K., Fujimori H., et al. Dual regulation of the skeletal muscle ryanodine receptor by triadin and calsequestrin. Biochemistry 37 (1998) 12987-12993
17. Groh S., Marty I., Ottolia M., et al. Functional interaction of the cytoplasmic domain of triadin with the skeletal ryanodine receptor. J. Biol. Chem. 274 (1999) 12278-12283
18. Rezgui S.S., Vassilopoulos S., Brocard J., et al. Triadin (Trisk 95) overexpression blocks excitation-contraction coupling in rat skeletal myotubes. J. Biol. Chem. 280 (2005) 39302-39308
19. 2+ homeostasis but are not essential for excitation-contraction coupling in skeletal muscle. J. Biol. Chem. 282 (2007) 37864-37874
20. Jones L.R., Zhang L., Sanborn K., Jorgensen A.O., and Kelley J. Purification, primary structure, and immunological characterization of the 26-kDa calsequestrin binding protein (junctin) from cardiac junctional sarcoplasmic reticulum. J. Biol. Chem. 270 (1995) 30787-30796
21. Lim K.Y., Hong C.S., and Kim D.H. cDNA cloning and characterization of human cardiac junction. Gene 255 (2000) 35-42
22. Yuan Q., Fan G.C., Dong M., et al. Sarcoplasmic reticulum calcium overloading in junctin deficiency enhances cardiac contractility but increases ventricular automaticity. Circulation 115 (2007) 300-309
23. 12 skeletal muscle myotubes. J. Biol. Chem. 281 (2006) 15572-15581
24. Y. Wang, X. Li, H. Duan, T.R. Fulton, G. Meissner, Knockdown of sarcoplasmic reticulum triadin and junctin in C2C12 cells, Biophysical Society Meeting, Baltimore, MD (Abstract), 2007.
25. Du W., McMahon T.J., Zhang Z.S., Stiber J.A., Meissner G., and Eu J.P. Excitation-contraction coupling in airway smooth muscle. J. Biol. Chem. 281 (2006) 30143-30151
26. Xiao X., Li J., and Samulski R.J. Production of high-titer recombinant adeno-associated virus vector in the absence of helper adenovirus. J. Virol. 72 (1998) 2224-2232
27. Li J., Samulski R.J., and Xiao X. Role for highly regulated rep gene expression in adeno-associated virus vector production. J. Virol. 71 (1997) 5236-5243
28. Kim H.S., Lee G., John S.W.M., Maeda N., and Smithies O. Molecular phenotyping for analyzing subtle genetic effects in mice: application to an angiotensinogen gene titration. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 4602-4607
29. 2+ by sarcoplasmic reticulum fragments. J. Biol. Chem. 239 (1964) 648-658
30. 2+ release channels (ryanodine receptors) by multiple mechanisms. J. Biol. Chem. 274 (1999) 32680-32691
31. Schoenmakers T.J., Visser G.J., Flik G., and Theuvenet A.P. CHELATOR: an improved method for computing metal ion concentrations in physiological solutions. BioTechniques 12 (1992) 870-879
32. Fessenden J.D., Wang Y., Moore R.A., Chen S.R., Allen P.D., and Pessah I.N. Divergent functional properties of ryanodine receptor types 1 and 3 expressed in a myogenic cell line. Biophys. J. 79 (2000) 2509-2525
33. Meissner G. Regulation of mammalian ryanodine receptors. Front Biosci. 7 (2002) d2072-d2080
34. Carozzi A.J., Ikonen E., Lindsay M.R., and Parton R.G. Role of cholesterol in developing T-tubules: analogous mechanisms for T-tubule and caveolae biogenesis. Traffic 1 (2000) 326-341
35. Parton R.G., Way M., Zorzi N., and Stang E. Caveolin-3 associates with developing T-tubules during muscle differentiation. J. Cell Biol. 136 (1997) 137-154
36. Nori A., Valle G., Bortoloso E., Turcato F., and Volpe P. Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers. Am. J. Physiol. Cell. 291 (2006) C245-C253
37. Hong C.S., Cho M.C., Kwak Y.G., et al. Cardiac remodeling and atrial fibrillation in transgenic mice overexpressing junctin. FASEB J. 16 (2002) 1310-1312
38. 2+ signaling. Cell Calcium 39 (2006) 131-142
39. Kirchhefer U., Neumann J., Bers D.M., et al. Impaired relaxation in transgenic mice overexpressing junctin. Cardiovasc. Res. 59 (2003) 369-379
40. 2+ handling, contractility, and heart failure. Am. J. Physiol. 293 (2007) H728-H734