Non-thiol reagents regulate ryanodine receptor function by redox interactions that modify reactive thiols

Antioxidants and Redox Signaling

Volumn 9, Issue 5, 2007, Pages 609-621

  Marinov, Benjamin S ^a   Olojo, Rotimi O ^a   Xia, Ruohong ^b   Abramson, Jonathan J ^a  

^a PORTLAND STATE UNIVERSITY   (United States)

^b EAST CHINA NORMAL UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CAFFEINE; DISULFIDE; LIGAND; REAGENT; RYANODINE RECEPTOR; TETRACAINE; THIOL; THIOL DERIVATIVE;

ANIMAL TISSUE; ARTICLE; CALCIUM TRANSPORT; CHEMICAL REACTION; CONTROLLED STUDY; ELECTRON TRANSPORT; MOLECULAR INTERACTION; NONHUMAN; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; SARCOPLASMIC RETICULUM;

ANIMALS; CAFFEINE; CALCIUM CHANNEL AGONISTS; CALCIUM CHANNEL BLOCKERS; CALCIUM CHANNELS; ELECTRONS; OXIDATION-REDUCTION; RABBITS; RYANODINE RECEPTOR CALCIUM RELEASE CHANNEL; SULFHYDRYL COMPOUNDS; SULFHYDRYL REAGENTS; TETRACAINE;

EID: 34247168526     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2006.1426     Document Type: Article

References (43)

1. Abramson JJ, Buck E, Salama G, Casida JE, and Pessah IN. Mechanism of anthraquinone-induced calcium release from skeletal muscle sarcoplasmic reticulum. J Biol Chem 263: 18750-18758, 1988.
2. Abramson JJ, Milne S, Buck E, and Pessah IN. Porphyrin induced calcium release from skeletal muscle sarcoplasmic reticulum. Arch Biochem Biophys 301: 396-403, 1993.
3. Castleman AW Jr, Zhong Q, and Hurley SM. Femtochemistry uncovers the nature of electron transfer reactions. Proc Natl Acad Sci USA 96: 4219-4220, 1999.
4. Cheong E, Tumbev V, Abramson J, Salama G, and Stoyanovsky DA. Nitroxyl triggers Ca2+ release from skeletal and cardiac sarcoplasmic reticulum by oxidizing ryanodine receptors. Cell Calcium 37: 87-96, 2005.
5. Dulhunty A, Haarmann C, Green D, and Hart J. How many cysteine residues regulate ryanodine receptor channel activity? Antioxid Redox Signal 2: 27-34, 2000.
6. Eu JP, Sun J, Xu L, Stamler JS, and Meissner G. The skeletal muscle calcium release channel: coupled O2 sensor and NO signaling functions. Cell 102: 499-509, 2000.
7. Fabiato A. Calcium-induced release of calcium from the cardiac sarcoplasmic reticulum Am J Physiol 245: C1-14; 1983.
8. Favero TG, Webb J, Papiez M, Fisher E, Trippichio RJ, Broide M, and Abramson JJ. Hypochlorous acid modifies calcium release channel function from skeletal muscle sarcoplasmic reticulum. J Appl Physiol 94: 1387-1394; 2003.
9. Favero TG, Zable AC, and Abramson J J. Hydrogen peroxide stimulates the Ca2+ release channel from skeletal muscle sarcoplasmic reticulum. J Biol Chem 270: 25557-25563; 1995.
10. Favero TG, Zable AC, Colter D, and Abramson JJ. Lactate inhibits Ca(2+) -activated Ca(2+)-channel activity from skeletal muscle sarcoplasmic reticulum. J Appl Physiol 82: 447-452; 1997.
11. Feng W, Liu G, Xia R, Abramson JJ, and Pessah IN. Site-selective modification of hyperreactive cysteines of ryanodine receptor complex by quinones. Mol Pharmacol 55: 821-831; 1999.
12. Hess P, Lansman JB, and Tsien RW. Different modes of Ca channel gating behaviour favoured by dihydropyridine Ca agonists and antagonists. Nature 311: 538-544; 1984.
13. Honen BN, Saint DA, and Laver DR. Suppression of calcium sparks in rat ventricular myocytes and direct inhibition of sheep cardiac RyR channels by EPA, DHA and oleic acid. J Membr Biol 196: 95-103; 2003.
14. Jayaraman T, Brillantes AM, Timerman AP, Fleischer S, Erdjument-Bromage H, Tempst P, and Marks AR. FK506 binding protein associated with the calcium release channel (ryanodine receptor) J Biol Chem 267: 9474-9477; 1992.
15. Liu G, Abramson JJ, Zable AC, and Pessah IN. Direct evidence for the existence and functional role of hyperreactive sulfhydryls on the ryanodine receptor-triadin complex selectively labeled by the coumarin maleimide 7-diethylamino-3-(4′-maleimidylphenyl)-4-methylcoumarin. Mol Pharmacol 45: 189-200; 1994.
16. MacLennan DH. Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum. J Biol Chem 245: 4508-4518; 1970.
17. Marinov BS. Na+ channel antagonists act as electron donors while agonists act as electron acceptors with free radicals. FEBS Lett 191: 159-162; 1985.
18. Marinov BS, Bend EG, and Abramson JJ. Reactions with dye free radicals reveal weak redox properties of drugs Photochem Photobiol 2006.
19. Marinov BS and Evtodienko JV Estimation of redox properties of chemical compounds by their reactions with free radicals. Anal Biochem 220: 154-159; 1994.
20. Marinov BS and Saxon ME. Dihydropyridine Ca2+ agonists and channel blockers interact in the opposite manner with photogenerated unpaired electrons. FEBS Lett 186: 251-254; 1985.
21. Menshikova EV and Salama G. Reactive disulfides elevate cytosolic free Ca2+ in cardiomyocytes by oxidizing regulatory thiols on ryanodine receptors (RyRs). Circulation 98: 805; 1998.
22. Olojo RO, Xia RH, and Abramson JJ. Spectrophotometric and fluorometric assay of superoxide ion using 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole. Anal Biochem 339: 338-344; 2005.
23. Pessah IN, Stambuk RA, and Casida JE. Ca2+-activated ryanodine binding: mechanisms of sensitivity and intensity modulation by Mg2+, caffeine, and adenine nucleotides. Mol Pharmacol 31: 232-238; 1987.
24. Rousseau E, Ladine J, Liu QY, and Meissner G. Activation of the Ca2+ release channel of skeletal muscle sarcoplasmic reticulum by caffeine and related compounds. Arch Biochem Biophys 267: 75-86; 1988.
25. Salama G and Abramson J. Silver ions trigger Ca2+ release by acting at the apparent physiological release site in sarcoplasmic reticulum. J Biol Chem 259: 13363-13369; 1984.
26. Samso M, Trujillo R, Gurrola GB, Valdivia HH, and Wagenknecht T. Three-dimensional location of the imperatoxin A binding site on the ryanodine receptor. J Cell Biol 146: 493-499; 1999.
27. Schafer FQ and Buettner GR. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med'30: 1191-1212; 2001.
28. Schaffner W and Weissmann C. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal Biochem 56: 502-514; 1973.
29. Schneider MF and Chandler WK. Voltage dependent charge movement of skeletal muscle: a possible step in excitation-contraction coupling. Nature 242: 244-246; 1973.
30. Sharma MR, Jeyakumar LH, Fleischer S, and Wagenknecht T. Three-dimensional visualization of FKBP12.6 binding to an open conformation of cardiac ryanodine receptor. Biophys J 90: 164-172; 2006.
31. Stoyanovsky D, Murphy T, Anno PR, Kim YM, and Salama G. Nitric oxide activates skeletal and cardiac ryanodine receptors. Cell Calcium 21: 19-29; 1997.
32. Sun J, Xin C, Eu JP, Stamler JS, and Meissner G. Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO. Proc Natl Acad Sci USA 98: 11158-11162; 2001.
33. Sutherland MW and Learmonth BA. The tetrazolium dyes MTS and XTT provide new quantitative assays for superoxide and superoxide dismutase. Free Radic Res 27: 283-289; 1997.
34. Takeshima H, Nishimura S, Matsumoto T, Ishida H, Kangawa K, Minamino N, Matsuo H, Ueda M, Hanaoka M, and Hirose T. Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor. Nature 339: 439-445; 1989.
35. Tezcan FA, Crane BR, Winkler JR, and Gray HB. Electron tunneling in protein crystals. Proc Natl Acad Sci USA 98: 5002-5006; 2001.
36. Trimm JL, Salama G, and Abramson JJ. Sulfhydryl oxidation induces rapid calcium release from sarcoplasmic reticulum vesicles. J Biol Chem 261: 16092-16098; 1986.
37. Voss AA, Lango J, Ernst-Russell M, Morin D, and Pessah IN. Identification of hyperreactive cysteines within ryanodine receptor type 1 by mass spectrometry. J Biol Chem 279: 34514-34520; 2004.
38. Weber A. The mechanism of the action of caffeine on sarcoplasmic reticulum. J Gen Physiol 52: 760-772; 1968.
39. West DJ, Smith EC, and Williams AJ. A novel and rapid approach to isolating functional ryanodine receptors 1. Biochem Biophys Res Commun 294: 402-407; 2002.
40. Xia R, Stangler T, and Abramson JJ. Skeletal muscle ryanodine receptor is a redox sensor with a well defined redox potential that is sensitive to channel modulators. J Biol Chem 275: 36556-36561; 2000.
41. Xia R, Webb JA, Gnall LL, Cutler K, and Abramson JJ. Skeletal muscle sarcoplasmic reticulum contains a NADH-dependent oxidase that generates superoxide. Am J Physiol Cell Physiol 285: C215-C221; 2003.
42. Xu L, Jones R, and Meissner G. Effects of local anesthetics on single channel behavior of skeletal muscle calcium release channel. J Gen Physiol 101: 207-233; 1993.
43. Zable AC, Favero TG, and Abramson JJ. Glutathione modulates ryanodine receptor from skeletal muscle sarcoplasmic reticulum. Evidence for redox regulation of the Ca2+ release mechanism. J Biol Chem 272: 7069-7077; 1997.