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Advances in Pharmacological Sciences
Volume 2012, Article ID 768720, 16 pages
http://dx.doi.org/10.1155/2012/768720
Research Article

Allosteric Modulation of Beta1 Integrin Function Induces Lung Tissue Repair

1Avipero Ltd., 5th Floor, 125 Princes Street, Edinburgh EH2 4AD, UK
2School of Biomedical Sciences, The University of Edinburgh, Hugh Robson Building, George Square, Edinburgh EH8 9XD, UK
3Division of Pathology, Institute of Genetics and Molecular Medicine, The University of Edinburgh, Western General Hospital, Edinburgh EH4 2XU, UK
4MRC Centre for Inflammation Research, The Queen's Medical Research Institute, The University of Edinburgh, 47 Little France Crescent, Edinburgh EH16 4TJ, UK

Received 16 August 2011; Revised 21 October 2011; Accepted 31 October 2011

Academic Editor: Chi Hin Cho

Copyright © 2012 Rehab AlJamal-Naylor 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. R. Al-Jamal and D. J. Harrison, “Beta1 integrin in tissue remodelling and repair: from phenomena to concepts,” Pharmacology and Therapeutics, vol. 120, no. 2, pp. 81–101, 2008. View at Publisher · View at Google Scholar · View at Scopus
  2. T. Fujimura, Y. Shibuya, S. Moriwaki et al., “Fucoidan is the active component of Fucus vesiculosus that promotes contraction of fibroblast-populated collagen gels,” Biological and Pharmaceutical Bulletin, vol. 23, no. 10, pp. 1180–1184, 2000. View at Google Scholar · View at Scopus
  3. T. Fujimura, K. Tsukahara, S. Moriwaki, T. Kitahara, and Y. Takema, “Effects of natural product extracts on contraction and mechanical properties of fibroblast populated collagen gel,” Biological and Pharmaceutical Bulletin, vol. 23, no. 3, pp. 291–297, 2000. View at Google Scholar · View at Scopus
  4. T. Fujimura, S. Moriwaki, G. Imokawa, and Y. Takema, “Crucial role of fibroblast integrins α2 and β1 in maintaining the structural and mechanical properties of the skin,” Journal of Dermatological Science, vol. 45, no. 1, pp. 45–53, 2007. View at Publisher · View at Google Scholar
  5. M. Shimaoka and T. A. Springer, “Therapeutic antagonists and conformational regulation of integrin function,” Nature Reviews Drug Discovery, vol. 2, no. 9, pp. 703–716, 2003. View at Google Scholar · View at Scopus
  6. J. C. Friedland, M. H. Lee, and D. Boettiger, “Mechanically activated integrin switch controls α5β1 function,” Science, vol. 323, no. 5914, pp. 642–644, 2009. View at Publisher · View at Google Scholar · View at Scopus
  7. M. Kato and M. Mrksich, “Using model substrates to study the dependence of focal adhesion formation on the affinity of integrin-ligand complexes,” Biochemistry, vol. 43, no. 10, pp. 2699–2707, 2004. View at Publisher · View at Google Scholar · View at Scopus
  8. B. H. Luo, K. Strokovich, T. Walz, T. A. Springer, and J. Takagi, “Allosteric β1 integrin antibodies that stabilize the low affinity state by preventing the swing-out of the hybrid domain,” Journal of Biological Chemistry, vol. 279, no. 26, pp. 27466–27471, 2004. View at Publisher · View at Google Scholar · View at Scopus
  9. M. Shimaoka, J. Takagi, and T. A. Springer, “Conformational regulation of integrin structure and function,” Annual Review of Biophysics and Biomolecular Structure, vol. 31, pp. 485–516, 2002. View at Publisher · View at Google Scholar
  10. J. Takagi, B. M. Petre, T. Walz, and T. A. Springer, “Global conformational earrangements in integrin extracellular domains in outside-in and inside-out signaling,” Cell, vol. 110, no. 5, pp. 599–611, 2002. View at Publisher · View at Google Scholar · View at Scopus
  11. H. Xia, D. Diebold, R. Nho et al., “Pathological integrin signaling enhances proliferation of primary lung fibroblasts from patients with idiopathic pulmonary fibrosis,” Journal of Experimental Medicine, vol. 205, no. 7, pp. 1659–1672, 2008. View at Publisher · View at Google Scholar · View at Scopus
  12. N. Koyama, J. Seki, S. Vergel et al., “Regulation and function of an activation-dependent epitope of the β1 integrins in vascular cells after balloon injury in baboon arteries and in vitro,” American Journal of Pathology, vol. 148, no. 3, pp. 749–761, 1996. View at Google Scholar · View at Scopus
  13. M. W. Johansson, S. R. Barthel, C. A. Swenson et al., “Eosinophil β1 integrin activation state correlates with asthma activity in a blind study of inhaled corticosteroid withdrawal,” Journal of Allergy and Clinical Immunology, vol. 117, no. 6, pp. 1502–1504, 2006. View at Publisher · View at Google Scholar · View at Scopus
  14. S. Wright, N. L. Malinin, K. A. Powell, T. Yednock, R. E. Rydel, and I. Griswold-Prenner, “α2β1 and αVβ1 integrin signaling pathways mediate amyloid-β-induced neurotoxicity,” Neurobiology of Aging, vol. 28, no. 2, pp. 226–237, 2007. View at Publisher · View at Google Scholar · View at Scopus
  15. H. Ni and J. A. Wilkins, “Localisation of a novel adhesion blocking epitope on the human β1 integrin chain,” Cell Adhesion and Communication, vol. 5, no. 4, pp. 257–271, 1998. View at Google Scholar · View at Scopus
  16. D. L. Brown, D. R. Phillips, C. H. Damsky, and I. F. Charo, “Synthesis and expression of the fibroblast fibronectin receptor in human monocytes,” Journal of Clinical Investigation, vol. 84, no. 1, pp. 366–370, 1989. View at Google Scholar · View at Scopus
  17. M. Ticchioni, C. Aussel, J. P. Breittmayer, S. Manie, C. Pelassy, and A. Bernard, “Suppressive effect of T cell proliferation via the CD29 molecule: the CD29 mAb 1 “K20” decreases diacylglycerol and phosphatidic acid levels in activated T cells,” Journal of Immunology, vol. 151, no. 1, pp. 119–127, 1993. View at Google Scholar · View at Scopus
  18. A. A. Porollo, R. Adamczak, and J. Meller, “POLYVIEW: a flexible visualization tool for structural and functional annotations of proteins,” Bioinformatics, vol. 20, no. 15, pp. 2460–2462, 2004. View at Publisher · View at Google Scholar · View at Scopus
  19. A. Chigaev, A. Waller, O. Amit, L. Halip, C. G. Bologa, and L. A. Sklar, “Real-time analysis of conformation-sensitive antibody binding provides new insights into integrin conformational regulation,” Journal of Biological Chemistry, vol. 284, no. 21, pp. 14337–14346, 2009. View at Publisher · View at Google Scholar · View at Scopus
  20. A. Chigaev, T. Buranda, D. C. Dwyer, E. R. Prossnitz, and L. A. Sklar, “FRET detection of cellular α4-integrin conformational activation,” Biophysical Journal, vol. 85, no. 6, pp. 3951–3962, 2003. View at Google Scholar · View at Scopus
  21. X. Trepat, L. Deng, S. S. An et al., “Universal physical responses to stretch in the living cell,” Nature, vol. 447, no. 7144, pp. 592–595, 2007. View at Publisher · View at Google Scholar · View at Scopus
  22. U. Cavallaro, J. Niedermeyer, M. Fuxa, and G. Christofori, “N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signalling,” Nature Cell Biology, vol. 3, no. 7, pp. 650–657, 2001. View at Publisher · View at Google Scholar · View at Scopus
  23. G. E. Hannigan, C. Leung-Hagesteijn, L. Fitz-Gibbon et al., “Regulation of cell adhesion and anchorage-dependent growth by a new β1-integrin-linked protein kinase,” Nature, vol. 379, no. 6560, pp. 91–96, 1996. View at Publisher · View at Google Scholar · View at Scopus
  24. M. D'Amico, J. Hulit, D. F. Amanatullah et al., “The integrated-linked kinase regulates the cyclin D1 gene through glycogen synthase kinase 3β and cAMP-responsive element-binding protein-dependent pathways,” Journal of Biological Chemistry, vol. 275, no. 42, pp. 32649–32657, 2000. View at Google Scholar
  25. M. Delcommenne, C. Tan, V. Gray, L. Rue, J. Woodgett, and S. Dedhar, “Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 19, pp. 11211–11216, 1998. View at Publisher · View at Google Scholar · View at Scopus
  26. Y. Shikata, K. Shikata, M. Matsuda et al., “Integrins mediate the inhibitory effect of focal adhesion on angiotensin II-induced p44/42 mitogen-activated protein (MAP) kinase activity in human mesangial cells,” Biochemical and Biophysical Research Communications, vol. 261, no. 3, pp. 820–823, 1999. View at Publisher · View at Google Scholar · View at Scopus
  27. A. Chigaev, A. M. Blenc, J. V. Braaten et al., “Real time analysis of the affinity regulation of α 4-integrin: the physiologically activated receptor is intermediate in affinity between resting and Mn2+ or antibody activation,” Journal of Biological Chemistry, vol. 276, no. 52, pp. 48670–48678, 2001. View at Publisher · View at Google Scholar · View at Scopus
  28. R. Barsacchi, C. Perrotta, P. Sestili, O. Cantoni, S. Moncada, and E. Clementi, “Cyclic GMP-dependent inhibition of acid sphingomyelinase by nitric oxide: an early step in protection against apoptosis,” Cell Death and Differentiation, vol. 9, no. 11, pp. 1248–1255, 2002. View at Publisher · View at Google Scholar · View at Scopus
  29. D. K. Sharma, J. C. Brown, Z. Cheng, E. L. Holicky, D. L. Marks, and R. E. Pagano, “The glycosphingolipid, lactosylceramide, regulates β1- integrin clustering and endocytosis,” Cancer Research, vol. 65, no. 18, pp. 8233–8241, 2005. View at Publisher · View at Google Scholar · View at Scopus
  30. S. Filosto, S. Castillo, A. Danielson et al., “Neutral sphingomyelinase 2: a novel target in cigarette smoke-induced apoptosis and lung injury,” American Journal of Respiratory Cell and Molecular Biology, vol. 44, no. 3, pp. 350–360, 2011. View at Publisher · View at Google Scholar
  31. M. A. Fernàndez, C. Albor, M. Ingelmo-Torres et al., “Caveolin-1 is essential for liver regeneration,” Science, vol. 313, no. 5793, pp. 1628–1632, 2006. View at Publisher · View at Google Scholar · View at Scopus
  32. M. A. del Pozo, N. Balasubramanian, N. B. Alderson et al., “Phospho-caveolin-1 mediates integrin-regulated membrane domain internalization,” Nature Cell Biology, vol. 7, no. 9, pp. 901–908, 2005. View at Publisher · View at Google Scholar · View at Scopus
  33. R. D. Singh, E. L. Holicky, Z. J. Cheng et al., “Inhibition of caveolar uptake, SV40 infection, and β1-integrin signaling by a nonnatural glycosphingolipid stereoisomer,” Journal of Cell Biology, vol. 176, no. 7, pp. 895–901, 2007. View at Publisher · View at Google Scholar · View at Scopus
  34. A. M. Houghton, P. A. Quintero, D. L. Perkins et al., “Elastin fragments drive disease progression in a murine model of emphysema,” Journal of Clinical Investigation, vol. 116, no. 3, pp. 753–759, 2006. View at Publisher · View at Google Scholar · View at Scopus
  35. S. Wright, C. Parham, B. Lee et al., “Perlecan domain V inhibits α2 integrin-mediated amyloid-β neurotoxicity,” Neurobiology of Aging. In press.
  36. R. Al-Jamal and D. G. Harrison, “Tissue repair,” WO2005037313, 2003, http://v3.espacenet.com/publicationDetails/biblio?DB=EPODOC&adjacent=true&locale=en_GB&FT=D&date=20050428&CC=WO&NR=2005037313A2&KC=A2.
  37. R. O. Hynes, “Integrins: bidirectional, allosteric signaling machines,” Cell, vol. 110, no. 6, pp. 673–687, 2002. View at Publisher · View at Google Scholar · View at Scopus
  38. S. J. Shattil, C. Kim, and M. H. Ginsberg, “The final steps of integrin activation: the end game,” Nature Reviews Molecular Cell Biology, vol. 11, no. 4, pp. 288–300, 2010. View at Publisher · View at Google Scholar · View at Scopus
  39. R. Pankov, T. Markovska, R. Hazarosova, P. Antonov, L. Ivanova, and A. Momchilova, “Cholesterol distribution in plasma membranes of β1 integrin-expressing and β1 integrin-deficient fibroblasts,” Archives of Biochemistry and Biophysics, vol. 442, no. 2, pp. 160–168, 2005. View at Publisher · View at Google Scholar
  40. G. Pande, “The role of membrane lipids in regulation of integrin functions,” Current Opinion in Cell Biology, vol. 12, no. 5, pp. 569–574, 2000. View at Publisher · View at Google Scholar · View at Scopus
  41. I. Petrache, V. Natarajan, L. Zhen et al., “Ceramide upregulation causes pulmonary cell apoptosis and emphysema-like disease in mice,” Nature Medicine, vol. 11, no. 5, pp. 491–498, 2005. View at Publisher · View at Google Scholar · View at Scopus
  42. B. Butler, C. Gao, A. T. Mersich, and S. D. Blystone, “Purified integrin adhesion complexes exhibit actin-polymerization activity,” Current Biology, vol. 16, no. 3, pp. 242–251, 2006. View at Publisher · View at Google Scholar · View at Scopus
  43. J. D. Whittard and S. K. Akiyama, “Activation of β1 integrins induces cell-cell adhesion,” Experimental Cell Research, vol. 263, no. 1, pp. 65–76, 2001. View at Publisher · View at Google Scholar · View at Scopus
  44. N. Minematsu, A. Blumental-Perry, and S. D. Shapiro, “Cigarette smoke inhibits engulfment of apoptotic cells by macrophages through inhibition of actin rearrangement,” American Journal of Respiratory Cell and Molecular Biology, vol. 44, no. 4, pp. 474–482, 2011. View at Publisher · View at Google Scholar
  45. J. L. Daniel, I. R. Molish, L. Robkin, and H. Holmsen, “Nucleotide exchange between cytosolic ATP and F-actin-bound ADP may be a major energy-utilizing process in unstimulated platelets,” European Journal of Biochemistry, vol. 156, no. 3, pp. 677–684, 1986. View at Google Scholar · View at Scopus
  46. I. Bock-Marquette, A. Saxena, M. D. White, J. M. DiMaio, and D. Srivastava, “Thymosin β4 activates integrin-linked kinase and promotes cardiac cell migration, survival and cardiac repair,” Nature, vol. 432, no. 7016, pp. 466–472, 2004. View at Publisher · View at Google Scholar · View at Scopus
  47. M. W. Johansson, S. R. Barthel, C. A. Swenson et al., “Eosinophil β1 integrin activation state correlates with asthma activity in a blind study of inhaled corticosteroid withdrawal,” Journal of Allergy and Clinical Immunology, vol. 117, no. 6, pp. 1502–1504, 2006. View at Publisher · View at Google Scholar · View at Scopus
  48. R. Al-Jamal and D. J. Harrison, “Compounds and methods for the modulation of integrin function to mediate tissue repair,” WO2008104808, 2007, http://v3.espacenet.com/publicationDetails/biblio?DB=EPODOC&adjacent=true&locale=en_GB&FT=D&date=20080904&CC=WO&NR=2008104808A2&KC=A2.
  49. E. C. Lucey, R. H. Goldstein, R. Breuer, B. N. Rexer, D. E. Ong, and G. L. Snider, “Retinoic acid does not affect alveolar septation in adult FVB mice with elastase-induced emphysema,” Respiration, vol. 70, no. 2, pp. 200–205, 2003. View at Publisher · View at Google Scholar · View at Scopus
  50. D. H. Miller, O. A. Khan, W. A. Sheremata et al., “A controlled trial of natalizumab for relapsing multiple sclerosis,” New England Journal of Medicine, vol. 348, no. 1, pp. 15–23, 2003. View at Publisher · View at Google Scholar · View at Scopus