Table of Contents
Journal of Signal Transduction
Volume 2012, Article ID 754964, 9 pages
http://dx.doi.org/10.1155/2012/754964
Research Article

Redox Regulation of Nonmuscle Myosin Heavy Chain during Integrin Engagement

Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134 Florence, Italy

Received 21 July 2011; Accepted 20 September 2011

Academic Editor: Lorenza Trabalzini

Copyright © 2012 Tania Fiaschi 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. T. Finkel and N. J. Holbrook, “Oxidants, oxidative stress and the biology of ageing,” Nature, vol. 408, no. 6809, pp. 239–247, 2000. View at Publisher · View at Google Scholar · View at Scopus
  2. R. Schreck, P. Rieber, and P. A. Baeuerle, “Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1,” EMBO Journal, vol. 10, no. 8, pp. 2247–2258, 1991. View at Google Scholar · View at Scopus
  3. H. Okuno, A. Akahori, H. Sato, S. Xanthoudakis, T. Curran, and H. Iba, “Escape from redox regulation enhances the transforming activity of Fos,” Oncogene, vol. 8, no. 3, pp. 695–701, 1993. View at Google Scholar · View at Scopus
  4. G. L. Wang, B. H. Jiang, and G. L. Semenza, “Effect of protein kinase and phosphatase inhibitors on expression of hypoxia-inducible factor 1,” Biochemical and Biophysical Research Communications, vol. 216, no. 2, pp. 669–675, 1995. View at Publisher · View at Google Scholar · View at Scopus
  5. R. Rainwater, D. Parks, M. E. Anderson, P. Tegtmeyer, and K. Mann, “Role of cysteine residues in regulation of p53 function,” Molecular and Cellular Biology, vol. 15, no. 7, pp. 3892–3903, 1995. View at Google Scholar · View at Scopus
  6. H. M. Lander, J. S. Ogiste, K. K. Teng, and A. Novogrodsky, “p21(ras) as a common signaling target of reactive free radicals and cellular redox stress,” Journal of Biological Chemistry, vol. 270, no. 36, pp. 21195–21198, 1995. View at Publisher · View at Google Scholar · View at Scopus
  7. P. Chiarugi and P. Cirri, “Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction,” Trends in Biochemical Sciences, vol. 28, no. 9, pp. 509–514, 2003. View at Publisher · View at Google Scholar · View at Scopus
  8. E. Giannoni, F. Buricchi, G. Raugei, G. Ramponi, and P. Chiarugi, “Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth,” Molecular and Cellular Biology, vol. 25, no. 15, pp. 6391–6403, 2005. View at Publisher · View at Google Scholar · View at Scopus
  9. P. Chiarugi, G. Pani, E. Giannoni et al., “Reactive oxygen species as essential mediators of cell adhesion: the oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion,” Journal of Cell Biology, vol. 161, no. 5, pp. 933–944, 2003. View at Publisher · View at Google Scholar · View at Scopus
  10. P. Chiarugi, P. Cirri, L. Taddei et al., “The low M(r) protein-tyrosine phosphatase is involved in Rho-mediated cytoskeleton rearrangement after integrin and platelet-derived growth factor stimulation,” Journal of Biological Chemistry, vol. 275, no. 7, pp. 4640–4646, 2000. View at Publisher · View at Google Scholar · View at Scopus
  11. W. Dröge, “Free radicals in the physiological control of cell function,” Physiological Reviews, vol. 82, no. 1, pp. 47–95, 2002. View at Google Scholar · View at Scopus
  12. A. S. Nimnual, L. J. Taylor, and D. Bar-Sagi, “Redox-dependent downregulation of Rho by Rac,” Nature Cell Biology, vol. 5, no. 3, pp. 236–241, 2003. View at Publisher · View at Google Scholar · View at Scopus
  13. M. L. Taddei, M. Parri, T. Mello et al., “Integrin-mediated cell adhesion and spreading engage different sources of reactive oxygen species,” Antioxidants and Redox Signaling, vol. 9, no. 4, pp. 469–481, 2007. View at Publisher · View at Google Scholar · View at Scopus
  14. P. Chiarugi and T. Fiaschi, “Redox signalling in anchorage-dependent cell growth,” Cellular Signalling, vol. 19, no. 4, pp. 672–682, 2007. View at Publisher · View at Google Scholar · View at Scopus
  15. T. Fiaschi, G. Cozzi, G. Raugei, L. Formigli, G. Ramponi, and P. Chiarugi, “Redox regulation of β-actin during integrin-mediated cell adhesion,” Journal of Biological Chemistry, vol. 281, no. 32, pp. 22983–22991, 2006. View at Publisher · View at Google Scholar · View at Scopus
  16. E. Giannoni, F. Bianchini, L. Masieri et al., “Reciprocal activation of prostate cancer cells and cancer-associated fibroblasts stimulates epithelial-mesenchymal transition and cancer stemness,” Cancer Research, vol. 70, no. 17, pp. 6945–6956, 2010. View at Publisher · View at Google Scholar · View at Scopus
  17. E. Giannoni, F. Bianchini, L. Calorini, and P. Chiarugi, “Cancer associated fibroblasts exploit reactive oxygen species through a proinflammatory signature leading to epithelial mesenchymal transition and stemness,” Antioxidants & Redox Signaling, vol. 14, pp. 2361–2371, 2011. View at Google Scholar
  18. J. R. Kim, H. W. Yoon, K. S. Kwon, S. R. Lee, and S. G. Rhee, “Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH,” Analytical Biochemistry, vol. 283, no. 2, pp. 214–221, 2000. View at Publisher · View at Google Scholar · View at Scopus
  19. T. Wakatsuki, R. B. Wysolmerski, and E. L. Elson, “Mechanics of cell spreading: role of myosin II,” Journal of Cell Science, vol. 116, no. 8, pp. 1617–1625, 2003. View at Publisher · View at Google Scholar · View at Scopus
  20. I. Lassing, F. Schmitzberger, M. Björnstedt et al., “Molecular and structural basis for redox regulation of β-actin,” Journal of Molecular Biology, vol. 370, no. 2, pp. 331–348, 2007. View at Publisher · View at Google Scholar · View at Scopus
  21. F. Klamt, S. Zdanov, R. L. Levine et al., “Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin,” Nature Cell Biology, vol. 11, no. 11, pp. 1241–1246, 2009. View at Publisher · View at Google Scholar · View at Scopus
  22. T. Fiaschi, P. Chiarugi, F. Buricchi et al., “Low molecular weight protein-tyrosine phosphatase is involved in growth inhibition during cell differentiation,” Journal of Biological Chemistry, vol. 276, no. 52, pp. 49156–49163, 2001. View at Publisher · View at Google Scholar · View at Scopus
  23. H. Westerblad and D. G. Allen, “Emerging roles of ROS/RNS in muscle function and fatigue,” Antioxidants & Redox Signaling, vol. 15, no. 9, pp. 2487–2499, 2011. View at Google Scholar
  24. J. G. Tidball and M. Wehling-Henricks, “The role of free radicals in the pathophysiology of muscular dystrophy,” Journal of Applied Physiology, vol. 102, no. 4, pp. 1677–1686, 2007. View at Publisher · View at Google Scholar · View at Scopus
  25. T. R. Moopanar and D. G. Allen, “The activity-induced reduction of myofibrillar Ca2+ sensitivity in mouse skeletal muscle is reversed by dithiothreitol,” Journal of Physiology, vol. 571, no. 1, pp. 191–200, 2006. View at Publisher · View at Google Scholar · View at Scopus
  26. S. K. Powers and M. J. Jackson, “Exercise-induced oxidative stress: cellular mechanisms and impact on muscle force production,” Physiological Reviews, vol. 88, no. 4, pp. 1243–1276, 2008. View at Publisher · View at Google Scholar · View at Scopus
  27. C. Passarelli, A. Di Venere, N. Piroddi et al., “Susceptibility of isolated myofibrils to in vitro glutathionylation: potential relevance to muscle functions,” Cytoskeleton, vol. 67, no. 2, pp. 81–89, 2010. View at Publisher · View at Google Scholar · View at Scopus
  28. E. Prochniewicz, D. A. Lowe, D. J. Spakowicz et al., “Functional, structural, and chemical changes in myosin associated with hydrogen peroxide treatment of skeletal muscle fibers,” American Journal of Physiology, vol. 294, no. 2, pp. C613–C626, 2008. View at Publisher · View at Google Scholar · View at Scopus