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Journal of Biomedicine and Biotechnology
Volume 2011, Article ID 386384, 10 pages
http://dx.doi.org/10.1155/2011/386384
Research Article

Both Basic and Acidic Amino Acid Residues of Are Involved in Triggering Substate of RyR1

1Systems Biology Research Center, Gwangju Institute of Science and Technology (GIST), Gwangju 500-712, Republic of Korea
2School of Life Sciences, Gwangju Institute of Science and Technology (GIST), 1 Oryong-dong, Buk-gu, Gwangju 500-712, Republic of Korea

Received 1 June 2011; Revised 5 August 2011; Accepted 10 August 2011

Academic Editor: Aikaterini Kontrogianni-Konstantopoulos

Copyright © 2011 In Ra Seo et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. A. Tsugorka, E. Rios, and L. A. Blatter, “Imaging elementary events of calcium release in skeletal muscle cells,” Science, vol. 269, no. 5231, pp. 1723–1726, 1995. View at Google Scholar · View at Scopus
  2. E. Rios, J. Ma, and A. Gonzalez, “The mechanical hypothesis of excitation-contraction (EC) coupling in skeletal muscle,” Journal of Muscle Research and Cell Motility, vol. 12, no. 2, pp. 127–135, 1991. View at Google Scholar · View at Scopus
  3. W. Cheng, X. Altafaj, M. Ronjat, and R. Coronado, “Interaction between the dihydropyridine receptor Ca2+ channel β-subunit and ryanodine receptor type 1 strengthens excitation-contraction coupling,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 52, pp. 19225–19230, 2005. View at Publisher · View at Google Scholar · View at Scopus
  4. M. D. Stern and E. G. Lakatta, “Excitation-contraction coupling in the heart: the state of the question,” FASEB Journal, vol. 6, no. 12, pp. 3092–3100, 1992. View at Google Scholar
  5. W. G. Wier, T. M. Egan, J. R. López-López, and C. W. Balke, “Local control of excitation-contraction coupling in rat heart cells,” Journal of Physiology, vol. 474, no. 3, pp. 463–471, 1994. View at Google Scholar · View at Scopus
  6. D. M. Bers, “Macromolecular complexes regulating cardiac ryanodine receptor function,” Journal of Molecular and Cellular Cardiology, vol. 37, no. 2, pp. 417–429, 2004. View at Publisher · View at Google Scholar · View at Scopus
  7. J. J. Mackrill, “Ryanodine receptor calcium channels and their partners as drug targets,” Biochemical Pharmacology, vol. 79, no. 11, pp. 1535–1543, 2010. View at Publisher · View at Google Scholar · View at Scopus
  8. D. W. Song, J. G. Lee, H. S. Youn, S. H. Eom, and D. H. Kim, “Ryanodine receptor assembly: a novel systems biology approach to 3D mapping,” Progress in Biophysics and Molecular Biology, vol. 105, no. 3, pp. 145–161, 2011. View at Publisher · View at Google Scholar · View at Scopus
  9. R. El-Hayek, B. Antoniu, J. Wang, S. L. Hamilton, and N. Ikemoto, “Identification of calcium release-triggering and blocking regions of the II-III loop of the skeletal muscle dihydropyridine receptor,” The Journal of Biological Chemistry, vol. 270, no. 38, pp. 22116–22118, 1995. View at Publisher · View at Google Scholar · View at Scopus
  10. Z. Fajloun, R. Kharrat, L. Chen et al., “Chemical synthesis and characterization of maurocalcine, a scorpion toxin that activates Ca2+ release channel/ryanodine receptors,” FEBS Letters, vol. 469, no. 2-3, pp. 179–185, 2000. View at Publisher · View at Google Scholar · View at Scopus
  11. H. H. Valdivia, M. S. Kirby, W. J. Lederer, and R. Coronado, “Scorpion toxins targeted against the sarcoplasmic reticulum Ca2+- release channel of skeletal and cardiac muscle,” Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no. 24, pp. 12185–12189, 1992. View at Publisher · View at Google Scholar · View at Scopus
  12. R. El-Hayek, A. J. Lokuta, C. Arevalo, and H. H. Valdivia, “Peptide probe of ryanodine receptor function: imperatoxin A, a peptide from the venom of the scorpion Pandinus imperator, selectively activates skeletal-type ryanodine receptor isoforms,” The Journal of Biological Chemistry, vol. 270, no. 48, pp. 28696–28704, 1995. View at Publisher · View at Google Scholar · View at Scopus
  13. A. Tripathy, W. Resch, L. E. Xu, H. H. Valdivia, and G. Meissner, “Imperatoxin A induces subconductance states in Ca2+ release channels (ryanodine receptors) of cardiac and skeletal muscle,” Journal of General Physiology, vol. 111, no. 5, pp. 679–690, 1998. View at Publisher · View at Google Scholar · View at Scopus
  14. A. Shtifman, C. W. Ward, J. Wang, H. H. Valdivia, and M. F. Schneider, “Effects of imperatoxin A on local sarcoplasmic reticulum Ca2+ release in frog skeletal muscle,” Biophysical Journal, vol. 79, no. 2, pp. 814–827, 2000. View at Google Scholar · View at Scopus
  15. G. B. Gurrola, C. Arévalo, R. Sreekumar, A. J. Lokuta, J. W. Walker, and H. H. Valdivia, “Activation of ryanodine receptors by imperatoxin A and a peptide segment of the II-III loop of the dihydropyridine receptor,” The Journal of Biological Chemistry, vol. 274, no. 12, pp. 7879–7886, 1999. View at Publisher · View at Google Scholar · View at Scopus
  16. L. Chen, E. Estève, J. M. Sabatier et al., “Maurocalcine and peptide A stabilize distinct subconductance states of ryanodine receptor type 1, revealing a proportional gating mechanism,” The Journal of Biological Chemistry, vol. 278, no. 18, pp. 16095–16106, 2003. View at Publisher · View at Google Scholar · View at Scopus
  17. A. F. Dulhunty, S. M. Curtis, S. Watson, L. Cengia, and M. G. Casarotto, “Multiple actions of imperatoxin A on ryanodine receptors: interactions with the II-III loop “A” fragment,” The Journal of Biological Chemistry, vol. 279, no. 12, pp. 11853–11862, 2004. View at Publisher · View at Google Scholar · View at Scopus
  18. B. Lukacs, M. Sztretye, J. Almassy et al., “Charged surface area of maurocalcine determines its interaction with the skeletal ryanodine receptor,” Biophysical Journal, vol. 95, no. 7, pp. 3497–3509, 2008. View at Publisher · View at Google Scholar
  19. M. G. Casarotto, D. Green, S. M. Pace, S. M. Curtis, and A. F. Dulhunty, “Structural determinants for activation or inhibition of ryanodine receptors by basic residues in the dihydropyridine receptor II-III loop,” Biophysical Journal, vol. 80, no. 6, pp. 2715–2726, 2001. View at Google Scholar · View at Scopus
  20. R. El-Hayek and N. Ikemoto, “Identification of the minimum essential region in the II-III loop of the dihydropyridine receptor α1 subunit required for activation of skeletal muscle-type excitation-contraction coupling,” Biochemistry, vol. 37, no. 19, pp. 7015–7020, 1998. View at Publisher · View at Google Scholar · View at Scopus
  21. C. W. Lee, E. H. Lee, K. Takeuchi et al., “Molecular basis of the high-affinity activation of type 1 ryanodine receptors by imperatoxin A,” Biochemical Journal, vol. 377, no. 2, pp. 385–394, 2004. View at Publisher · View at Google Scholar · View at Scopus
  22. I. R. Seo, M. R. Choi, C. S. Park, and D. H. Kim, “Effects of recombinant imperatoxin A (IpTxa) mutants on the rabbit ryanodine receptor,” Molecules and Cells, vol. 22, no. 3, pp. 328–335, 2006. View at Google Scholar · View at Scopus
  23. D. Green, S. Pace, S. M. Curtis et al., “The three-dimensional structural surface of two β-sheet scorpion toxins mimics that of an α-helical dihydropyridine receptor segment,” Biochemical Journal, vol. 370, no. 2, pp. 517–527, 2003. View at Publisher · View at Google Scholar · View at Scopus
  24. D. H. Kim, S. T. Ohnishi, and N. Ikemoto, “Kinetic studies of calcium release from sarcoplasmic reticulum in vitro,” The Journal of Biological Chemistry, vol. 258, no. 16, pp. 9662–9668, 1983. View at Google Scholar · View at Scopus
  25. C. Miller and E. Racker, “Ca2+ induced fusion of fragmented sarcoplasmic reticulum with artificial planar bilayers,” Journal of Membrane Biology, vol. 30, no. 1, pp. 283–300, 1976. View at Google Scholar · View at Scopus
  26. J. S. Smith, R. Coronado, and G. Meissner, “Single channel measurements of the calcium release channel from skeletal muscle sarcoplasmic reticulum: activation by Ca2+ and ATP and modulation by Mg2+,” Journal of General Physiology, vol. 88, no. 5, pp. 573–588, 1986. View at Google Scholar · View at Scopus
  27. E. H. Lee, G. Meissner, and D. H. Kim, “Effects of quercetin on single Ca2+ release channel behavior of skeletal muscle,” Biophysical Journal, vol. 82, no. 3, pp. 1266–1277, 2002. View at Google Scholar · View at Scopus
  28. F. A. Lai, H. P. Erickson, E. Rousseau, Q. Y. Liu, and G. Meissner, “Purification and reconstitution of the calcium release channel from skeletal muscle,” Nature, vol. 331, no. 6154, pp. 315–319, 1988. View at Google Scholar · View at Scopus
  29. E. Estève, S. Smida-Rezgui, S. Sarkozi et al., “Critical amino acid residues determine the binding affinity and the Ca 2+ release efficacy of maurocalcine in skeletal muscle cells,” The Journal of Biological Chemistry, vol. 278, no. 39, pp. 37822–37831, 2003. View at Publisher · View at Google Scholar · View at Scopus
  30. A. Mosbah, R. Kharrat, Z. Fajloun et al., “A new fold in the scorpion toxin family, associated with an activity on a ryanodine-sensitive calcium channel,” Proteins, vol. 40, no. 3, pp. 436–442, 2000. View at Publisher · View at Google Scholar · View at Scopus