Dissection of the inhibition of cardiac ryanodine receptors by human glutathione transferase GSTM2-2

Biochemical Pharmacology

Volumn 77, Issue 7, 2009, Pages 1181-1193

  Liu, Dan ^a   Hewawasam, Ruwani ^a   Pace, Suzy M ^a   Gallant, Esther M ^a   Casarotto, Marco G ^a   Dulhunty, Angela F ^a   Board, Philip G ^a  

^a Biology and Environment   (Australia)

Author keywords

Calcium release from cardiac sarcoplasmic reticulum; Calcium release from skeletal sarcoplasmic reticulum; Cardiac RyR2 channels; Glutathione transferase GSTM2 2; Lipid bilayer single channel experiments; Skeletal RyR1 channels

Indexed keywords

CALCIUM CHANNEL; GLUTATHIONE TRANSFERASE M2; RYANODINE RECEPTOR 1; RYANODINE RECEPTOR 2;

ARTICLE; BINDING AFFINITY; BINDING SITE; CALCIUM TRANSPORT; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CROSS LINKING; GENE CONSTRUCT; INHIBITION KINETICS; NONHUMAN; PRIORITY JOURNAL; SARCOPLASMIC RETICULUM; SEQUENCE ANALYSIS;

ANIMALS; CALCIUM; GLUTATHIONE TRANSFERASE; HUMANS; MYOCARDIUM; RABBITS; RYANODINE RECEPTOR CALCIUM RELEASE CHANNEL; SARCOPLASMIC RETICULUM; SHEEP;

EID: 61449224434     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2008.12.024     Document Type: Article

References (25)

1. Dulhunty A., Gage P., Curtis S., Chelvanayagam G., and Board P. The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator. J Biol Chem 276 (2001) 3319-3323
2. 2+ release channels. Int J Biochem Cell Biol 36 (2004) 1599-1612
3. 2+ and ATP. Biochem J 390 (2005) 333-343
4. Abdellatif Y., Liu D., Gallant E.M., Gage P.W., Board P.G., and Dulhunty A.F. The Mu class glutathione transferase is abundant in striated muscle and is an isoform-specific regulator of ryanodine receptor calcium channels. Cell Calcium 41 (2007) 429-440
5. Jalilian C., Gallant E.M., Board P.G., and Dulhunty A.F. Redox potential and the response of cardiac ryanodine receptors to CLIC-2, a member of the glutathione S-transferase structural family. Antioxid Redox Signal 10 (2008) 1675-1686
6. Sambrook J., Fritsch E.F., and Maniatis T. Molecular cloning: a laboratory manual (1989), Cold Spring Harbor Laboratory, NY
7. Ross V.L., and Board P.G. Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript. Biochem J 294 Pt 2 (1993) 373-380
8. Catanzariti A.M., Soboleva T.A., Jans D.A., Board P.G., and Baker R.T. An efficient system for high-level expression and easy purification of authentic recombinant proteins. Protein Sci 13 (2004) 1331-1339
9. Baker R.T., Catanzariti A.M., Karunasekara Y., Soboleva T.A., Sharwood R., Whitney S., et al. Using deubiquitylating enzymes as research tools. Methods Enzymol 398 (2005) 540-554
10. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
11. Wei L., Abdellatif Y.A., Liu D., Kimura T., Coggan M., Gallant E.M., et al. Muscle-specific GSTM2-2 on the luminal side of the sarcoplasmic reticulum modifies RyR ion channel activity. Int J Biochem Cell Biol 40 (2008) 1616-1628
12. Dulhunty A.F., Cengia L., Young J., Pace S.M., Harvey P.J., Lamb G.D., et al. Functional implications of modifying RyR-activating peptides for membrane permeability. Br J Pharmacol 144 (2005) 743-754
13. Minium E.W., King B.M., and Bear G. Statistical reasoning in psychology and education (1993), John Wiley and Sons, New York
14. Raghunathan S., Chandross R.J., Kretsinger R.H., Allison T.J., Penington C.J., and Rule G.S. Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity. J Mol Biol 238 (1994) 815-832
15. McCallum S.A., Hitchens T.K., and Rule G.S. Solution structure of the carboxyl terminus of a human class Mu glutathione S-transferase: NMR assignment strategies in large proteins. J Mol Biol 285 (1999) 2119-2132
16. Lu X., Xu L., and Meissner G. Activation of the skeletal muscle calcium release channel by a cytoplasmic loop of the dihydropyridine receptor. J Biol Chem 269 (1994) 6511-6516
17. Dulhunty A.F., Laver D.R., Gallant E.M., Casarotto M.G., Pace S.M., and Curtis S. Activation and inhibition of skeletal RyR channels by a part of the skeletal DHPR II-III loop: effects of DHPR Ser687 and FKBP12. Biophys J 77 (1999) 189-203
18. Dulhunty A.F., Laver D., Curtis S.M., Pace S., Haarmann C., and Gallant E.M. Characteristics of irreversible ATP activation suggest that native skeletal ryanodine receptors can be phosphorylated via an endogenous CaMKII. Biophys J 81 (2001) 3240-3252
19. Murray B.E., and Ohlendieck K. Cross-linking analysis of the ryanodine receptor and alpha1-dihydropyridine receptor in rabbit skeletal muscle triads. Biochem J 324 Pt 2 (1997) 689-696
20. 2+ release channel from skeletal muscle. Biochim Biophys Acta 1237 (1995) 151-161
21. Penington C.J., and Rule G.S. Mapping the substrate-binding site of a human class mu glutathione transferase using nuclear magnetic resonance spectroscopy. Biochemistry 31 (1992) 2912-2920
22. Van Den Bosch L., Verhoeven K., De Smedt H., Wuytack F., Missiaen L., and Robberecht W. Calcium handling proteins in isolated spinal motoneurons. Life Sci 65 (1999) 1597-1606
23. 2+ handling in vascular smooth muscle cells is affected by proliferation. Arterioscler Thromb Vasc Biol 20 (2000) 1225-1235
24. Wehrens X.H., Lehnart S.E., and Marks A.R. Ryanodine receptor-targeted anti-arrhythmic therapy. Ann N Y Acad Sci 1047 (2005) 366-375
25. Laver D.R., Baynes T.M., and Dulhunty A.F. Magnesium inhibition of ryanodine-receptor calcium channels: evidence for two independent mechanisms. J Membr Biol 156 (1997) 213-229