Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2014, Article ID 676493, 10 pages
http://dx.doi.org/10.1155/2014/676493
Research Article

Towards Scarless Wound Healing: A Comparison of Protein Expression between Human, Adult and Foetal Fibroblasts

Bio/Polymer Research Group, School of Biotechnology & Biomolecular Sciences, University of New South Wales, Sydney, NSW 2052, Australia

Received 31 October 2013; Revised 4 December 2013; Accepted 4 December 2013; Published 30 January 2014

Academic Editor: Tadamichi Shimizu

Copyright © 2014 Sonia Ho 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. B. Sund, New Developments in Wound Care, PJB Publications, London, UK, 2000.
  2. S. Reichert-Penetrat, A. Barbaud, S. Martin, L. Omhover, M. Weber, and J.-L. Schmutz, “Pemphigus vulgaris on an old surgical scar: Koebner's phenomenon?” European Journal of Dermatology, vol. 8, no. 1, pp. 60–62, 1998. View at Google Scholar · View at Scopus
  3. M. Mockenhaupt, C. Viboud, A. Dunant et al., “Stevens-Johnson syndrome and toxic epidermal necrolysis: assessment of medication risks with emphasis on recently marketed drugs. The EuroSCAR-study,” Journal of Investigative Dermatology, vol. 128, no. 1, pp. 35–44, 2008. View at Publisher · View at Google Scholar · View at Scopus
  4. T. Kaneki, A. Kawashima, T. Hayano et al., “Churg-Strauss syndrome (allergic granulomatous angitis) presenting with ileus caused by ischemic ileal ulcer,” Journal of Gastroenterology, vol. 33, no. 1, pp. 112–116, 1998. View at Publisher · View at Google Scholar · View at Scopus
  5. R. Lad, “Biotechnology in skin care (I): overview,” in Biotechnology in Personal Care, chapter 5, pp. 117–138, Taylor & Francis, New York, NY, USA, 1st edition, 2006. View at Google Scholar
  6. P. Martin, “Wound healing—aiming for perfect skin regeneration,” Science, vol. 276, no. 5309, pp. 75–81, 1997. View at Publisher · View at Google Scholar · View at Scopus
  7. G. C. Gurtner, S. Werner, Y. Barrandon, and M. T. Longaker, “Wound repair and regeneration,” Nature, vol. 453, no. 7193, pp. 314–321, 2008. View at Publisher · View at Google Scholar · View at Scopus
  8. B. D. Cumming, D. L. S. McElwain, and Z. Upton, “A mathematical model of wound healing and subsequent scarring,” Journal of the Royal Society Interface, vol. 7, no. 42, pp. 19–34, 2009. View at Publisher · View at Google Scholar · View at Scopus
  9. T. Rovee and H. Press, “Natural course of wound repair versus impaired healing in chronic skin ulcers,” in Wound Healing and Ulcers of the Skin, A. Shai and H. I. Maibach, Eds., pp. 7–17, Springer, Berlin, Germany, 2005. View at Publisher · View at Google Scholar
  10. M. W. J. Ferguson, D. J. Whitby, M. Shah, J. Armstrong, J. W. Siebert, and M. T. Longaker, “Scar formation: the spectral nature of fetal and adult wound repair,” Plastic and Reconstructive Surgery, vol. 97, no. 4, pp. 854–860, 1996. View at Publisher · View at Google Scholar · View at Scopus
  11. A. S. Colwell, M. T. Longaker, and H. P. Lorenz, “Fetal wound healing,” Frontiers in Bioscience, vol. 8, pp. s1240–s1248, 2003. View at Publisher · View at Google Scholar · View at Scopus
  12. L. J. Draaijers, F. R. H. Tempelman, Y. A. M. Botman et al., “The patient and observer scar assessment scale: a reliable and feasible tool for scar evaluation,” Plastic and Reconstructive Surgery, vol. 113, no. 7, pp. 1960–1965, 2004. View at Publisher · View at Google Scholar · View at Scopus
  13. H. P. Lorenz, D. J. Whitby, M. T. Longaker, and N. S. Adzick, “Fetal wound healing: the ontogeny of scar formation in the non-human primate,” Annals of Surgery, vol. 217, no. 4, pp. 391–396, 1993. View at Publisher · View at Google Scholar · View at Scopus
  14. R. Clark, “Wound repair: overview and general considerations,” in The Molecular and Cellular Biology of Wound Repair, pp. 3–50, Plenum Press, New York, NY, USA, 1996. View at Google Scholar
  15. National Institute of Health, Surface Plot, 2013.
  16. D. Honardoust and E. E. Tredget, “Adult skin wounds can be induced to regenerate through modulation of cells and extracellular matrix molecules,” in Advances in Wound Care, C. K. Sen, Ed., vol. 2, Mary Ann Liebert, 2011. View at Google Scholar
  17. F. Boraldi, L. Bini, S. Liberatori et al., “Proteome analysis of dermal fibroblasts cultured in vitro from human healthy subjects of different ages,” Proteomics, vol. 3, no. 6, pp. 917–929, 2003. View at Publisher · View at Google Scholar · View at Scopus
  18. S. Benvenuti, R. Cramer, C. C. Quinn et al., “Differential proteome analysis of replicative senescence in rat embryo fibroblasts,” Molecular & Cellular Proteomics, vol. 1, no. 4, pp. 280–292, 2002. View at Publisher · View at Google Scholar · View at Scopus
  19. M. J. Dutt and K. H. Lee, “Proteomic analysis,” Current Opinion in Biotechnology, vol. 11, no. 2, pp. 176–179, 2000. View at Publisher · View at Google Scholar · View at Scopus
  20. B. Honoré, “Genome- and proteome-based technologies: status and applications in the postgenomic era,” Expert Review of Molecular Diagnostics, vol. 1, no. 3, pp. 265–274, 2001. View at Publisher · View at Google Scholar · View at Scopus
  21. M. Mann and O. N. Jensen, “Proteomic analysis of post-translational modifications,” Nature Biotechnology, vol. 21, no. 3, pp. 255–261, 2003. View at Publisher · View at Google Scholar · View at Scopus
  22. S. Thompson, F. Mayerl, O. P. Peoples, S. Masamune, A. J. Sinskey, and C. T. Walsh, “Mechanistic studies on β-ketoacyl thiolase from Zoogloea ramigera: identification of the active-site nucleophile as CyS89, its mutation to Ser89, and kinetic and thermodynamic characterization of wild-type and mutant enzymes,” Biochemistry, vol. 28, no. 14, pp. 5735–5742, 1989. View at Publisher · View at Google Scholar · View at Scopus
  23. W. Cao, N. Liu, S. Tang et al., “Acetyl-coenzyme A acyltransferase 2 attenuates the apoptotic effects of BNIP3 in two human cell lines,” Biochimica et Biophysica Acta, vol. 1780, no. 6, pp. 873–880, 2008. View at Publisher · View at Google Scholar · View at Scopus
  24. R. Donato, “S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles,” The International Journal of Biochemistry and Cell Biology, vol. 33, no. 7, pp. 637–668, 2001. View at Publisher · View at Google Scholar · View at Scopus
  25. M. F. Pelletier, A. Marcil, G. Sevigny et al., “The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo,” Glycobiology, vol. 10, no. 8, pp. 815–827, 2000. View at Publisher · View at Google Scholar · View at Scopus
  26. I. B. Alieva, E. A. Zemskov, I. I. Kireev et al., “Microtubules growth rate alteration in human endothelial cells,” Journal of Biomedicine and Biotechnology, vol. 2010, Article ID 671536, 10 pages, 2010. View at Publisher · View at Google Scholar · View at Scopus
  27. J. G. Kiang and G. C. Tsokos, “Heat shock protein 70 kDa: molecular biology, biochemistry, and physiology,” Pharmacology and Therapeutics, vol. 80, no. 2, pp. 183–201, 1998. View at Publisher · View at Google Scholar · View at Scopus
  28. D. R. Ciocca, S. Green, R. M. Elledge et al., “Heat shock proteins hsp27 and hsp70: lack of correlation with response to tamoxifen and clinical course of disease in estrogen receptor-positive metastatic breast cancer (a southwest oncology group study),” Clinical Cancer Research, vol. 4, no. 5, pp. 1263–1266, 1998. View at Google Scholar · View at Scopus
  29. T. Kusakabe, K. Motoki, and K. Hori, “Mode of interactions of human aldolase isozymes with cytoskeletons,” Archives of Biochemistry and Biophysics, vol. 344, no. 1, pp. 184–193, 1997. View at Publisher · View at Google Scholar · View at Scopus
  30. E. Nishida, S. Maekawa, and H. Sakai, “Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin,” Biochemistry, vol. 23, no. 22, pp. 5307–5313, 1984. View at Publisher · View at Google Scholar · View at Scopus
  31. A. Kümin, M. Schäfer, N. Epp et al., “Peroxiredoxin 6 is required for blood vessel integrity in wounded skin,” Journal of Cell Biology, vol. 179, no. 4, pp. 747–760, 2007. View at Publisher · View at Google Scholar · View at Scopus
  32. D. Legrand, E. Elass, A. Pierce, and J. Mazurier, “Lactoferrin and host defence: an overview of its immuno-modulating and anti-inflammatory properties,” Biometals, vol. 17, no. 3, pp. 225–229, 2004. View at Publisher · View at Google Scholar · View at Scopus
  33. L. I. Gold, M. Rahman, K. M. Blechman et al., “Overview of the role for calreticulin in the enhancement of wound healing through multiple biological effects,” Journal of Investigative Dermatology Symposium Proceedings, vol. 11, no. 1, pp. 57–65, 2006. View at Publisher · View at Google Scholar · View at Scopus
  34. J. Klíma, L. Lacina, B. Dvořánková et al., “Differential regulation of galectin expression/reactivity during wound healing in porcine skin and in cultures of epidermal cells with functional impact on migration,” Physiological Research, vol. 58, no. 6, pp. 873–884, 2009. View at Google Scholar · View at Scopus
  35. W. Witke, “The role of profilin complexes in cell motility and other cellular processes,” Trends in Cell Biology, vol. 14, no. 8, pp. 461–469, 2004. View at Publisher · View at Google Scholar · View at Scopus
  36. B. Alberts, A. Johnson, J. Lewis, M. Raff, K. Roberts, and P. Walter, “The cytoskeleton and cell behavior,” in Molecular Biology of the Cell, Garland Science, New York, NY, USA, 2002. View at Google Scholar
  37. L. Zhu, Y. Zhang, Y. Hu, T. Wen, and Q. Wang, “Dynamic actin gene family evolution in primates,” BioMed Research International, vol. 2013, Article ID 630803, 11 pages, 2013. View at Publisher · View at Google Scholar
  38. R. Dominguez and K. C. Holmes, “Actin structure and function,” Annual Review of Biophysics, vol. 40, no. 1, pp. 169–186, 2011. View at Publisher · View at Google Scholar · View at Scopus
  39. J. Condeelis, “How is actin polymerization nucleated in vivo?” Trends in Cell Biology, vol. 11, no. 7, pp. 288–293, 2001. View at Publisher · View at Google Scholar · View at Scopus
  40. N. Bosselut, C. Housset, P. Marcelo et al., “Distinct proteomic features of two fibrogenic liver cell populations: hepatic stellate cells and portal myofibroblasts,” Proteomics, vol. 10, no. 5, pp. 1017–1028, 2010. View at Publisher · View at Google Scholar · View at Scopus
  41. E. H. J. Danen, J. van Rheenen, W. Franken et al., “Integrins control motile strategy through a Rho-cofilin pathway,” Journal of Cell Biology, vol. 169, no. 3, pp. 515–526, 2005. View at Publisher · View at Google Scholar · View at Scopus
  42. M. M. L. Davidson and R. J. Haslam, “Dephosphorylation of cofilin in stimulated platelets: roles for a GTP-binding protein and Ca2+,” Biochemical Journal, vol. 301, part 1, pp. 41–47, 1994. View at Google Scholar · View at Scopus
  43. P. J. Goldschmidt-Clermont, L. M. Machesky, J. J. Baldassare, and T. D. Pollard, “The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C,” Science, vol. 247, no. 4950, pp. 1575–1578, 1990. View at Publisher · View at Google Scholar · View at Scopus
  44. Z. Ding, A. Lambrechts, M. Parepally, and P. Roy, “Silencing profilin-1 inhibits endothelial cell proliferation, migration and cord morphogenesis,” Journal of Cell Science, vol. 119, no. 19, pp. 4127–4137, 2006. View at Publisher · View at Google Scholar · View at Scopus
  45. C. M. Pickart, “Mechanisms underlying ubiquitination,” Annual Review of Biochemistry, vol. 70, no. 1, pp. 503–533, 2001. View at Publisher · View at Google Scholar · View at Scopus
  46. W. Kim, E. J. Bennett, E. L. Huttlin et al., “Systematic and quantitative assessment of the ubiquitin-modified proteome,” Molecular Cell, vol. 44, no. 2, pp. 325–340, 2011. View at Publisher · View at Google Scholar · View at Scopus
  47. P. Xu, D. M. Duong, N. T. Seyfried et al., “Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation,” Cell, vol. 137, no. 1, pp. 133–145, 2009. View at Publisher · View at Google Scholar · View at Scopus
  48. C. V. Segré and S. Chiocca, “Regulating the regulators: the post-translational code of class I HDAC1 and HDAC2,” Journal of Biomedicine and Biotechnology, vol. 2011, Article ID 690848, 15 pages, 2011. View at Publisher · View at Google Scholar · View at Scopus
  49. Z. A. Wood, E. Schröder, J. R. Harris, and L. B. Poole, “Structure, mechanism and regulation of peroxiredoxins,” Trends in Biochemical Sciences, vol. 28, no. 1, pp. 32–40, 2003. View at Publisher · View at Google Scholar · View at Scopus
  50. T. Kalebic, A. Kinter, G. Poli, M. E. Anderson, A. Meister, and A. S. Fauci, “Suppression of human immunodeficiency virus expression in chronically infected monocytic cells by glutathione, glutathione ester, and N-acetylcysteine,” Proceedings of the National Academy of Sciences of the United States of America, vol. 88, no. 3, pp. 986–990, 1991. View at Publisher · View at Google Scholar · View at Scopus
  51. Y. Wang, Y. Manevich, S. I. Feinstein, and A. B. Fisher, “Adenovirus-mediated transfer of the 1-cys peroxiredoxin gene to mouse lung protects against hyperoxic injury,” The American Journal of Physiology—Lung Cellular and Molecular Physiology, vol. 286, no. 6, pp. L1188–L1193, 2004. View at Publisher · View at Google Scholar · View at Scopus
  52. J.-H. Kim, P. N. Bogner, S.-H. Baek et al., “Up-regulation of peroxiredoxin 1 in lung cancer and its implication as a prognostic and therapeutic target,” Clinical Cancer Research, vol. 14, no. 8, pp. 2326–2333, 2008. View at Publisher · View at Google Scholar · View at Scopus
  53. M. Cumberbatch, R. J. Dearman, S. Uribe-Luna et al., “Regulation of epidermal Langerhans cell migration by lactoferrin,” Immunology, vol. 100, no. 1, pp. 21–28, 2000. View at Publisher · View at Google Scholar · View at Scopus
  54. D. Legrand and J. Mazurier, “A critical review of the roles of host lactoferrin in immunity,” Biometals, vol. 23, no. 3, pp. 365–376, 2010. View at Publisher · View at Google Scholar · View at Scopus
  55. G. de la Rosa, D. Yang, P. Tewary, A. Varadhachary, and J. J. Oppenheim, “Lactoferrin acts as an alarmin to promote the recruitment and activation of APCs and antigen-specific immune responses,” The Journal of Immunology, vol. 180, no. 10, pp. 6868–6876, 2008. View at Google Scholar · View at Scopus
  56. Y. Takayama and K. Mizumachi, “Effects of lactoferrin on collagen gel contractile activity and myosin light chain phosphorylation in human fibroblasts,” FEBS Letters, vol. 508, no. 1, pp. 111–116, 2001. View at Publisher · View at Google Scholar · View at Scopus
  57. A. H. M. Beare, S. O'Kane, S. M. Krane, and M. W. J. Ferguson, “Severely impaired wound healing in the collagenase-resistant mouse,” Journal of Investigative Dermatology, vol. 120, no. 1, pp. 153–163, 2003. View at Publisher · View at Google Scholar · View at Scopus
  58. M. Ferguson and G. Howarth, “Marsupial models of scarless fetal wound healing,” in Fetal Wound Healing, pp. 95–124, 1992. View at Google Scholar
  59. B. Dvořánková, P. Szabo, L. Lacina et al., “Human galectins induce conversion of dermal fibroblasts into myofibroblasts and production of extracellular matrix: potential application in tissue engineering and wound repair,” Cells Tissues Organs, vol. 194, no. 6, pp. 469–480, 2011. View at Publisher · View at Google Scholar · View at Scopus
  60. S. J. Gardai, K. A. McPhillips, S. C. Frasch et al., “Cell-surface calreticulin initiates clearance of viable or apoptotic cells through trans-activation of LRP on the phagocyte,” Cell, vol. 123, no. 2, pp. 321–334, 2005. View at Publisher · View at Google Scholar · View at Scopus
  61. J. A. Coppinger, G. Cagney, S. Toomey et al., “Characterization of the proteins released from activated platelets leads to localization of novel platelet proteins in human atherosclerotic lesions,” Blood, vol. 103, no. 6, pp. 2096–2104, 2004. View at Publisher · View at Google Scholar · View at Scopus
  62. R. Clark, The Molecular and Cellular Biology of Wound Repair, Springer, New York, NY, USA, 1996.
  63. Y. Milev and D. W. Essex, “Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of thrombospondin-1 with thrombin-antithrombin III,” Archives of Biochemistry and Biophysics, vol. 361, no. 1, pp. 120–126, 1999. View at Publisher · View at Google Scholar · View at Scopus
  64. E. M. Huang, T. C. Detwiler, Y. Milev, and D. W. Essex, “Thiol-disulfide isomerization in thrombospondin: effects of conformation and protein disulfide isomerase,” Blood, vol. 89, no. 9, pp. 3205–3212, 1997. View at Google Scholar · View at Scopus
  65. T. C. Detwiler, A. C. Chang, M. V. Speziale, P. C. Browne, J. J. Miller, and K. Chen, “Complexes of thrombin with proteins secreted by activated platelets,” Seminars in Thrombosis and Hemostasis, vol. 18, no. 1, pp. 60–66, 1992. View at Google Scholar · View at Scopus
  66. K. J. Langenbach and J. Sottile, “Identification of protein-disulfide isomerase activity in fibronectin,” The Journal of Biological Chemistry, vol. 274, no. 11, pp. 7032–7038, 1999. View at Publisher · View at Google Scholar · View at Scopus
  67. M. G. Tonnesen, X. Feng, and R. A. F. Clark, “Angiogenesis in wound healing,” Journal of Investigative Dermatology Symposium Proceedings, vol. 5, no. 1, pp. 40–46, 2000. View at Publisher · View at Google Scholar · View at Scopus