Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2014, Article ID 934848, 12 pages
http://dx.doi.org/10.1155/2014/934848
Research Article

Proteomics and Metabolomics for In Situ Monitoring of Wound Healing

1Department of Proteomics, Helmholtz-Centre for Environmental Research-UFZ, Permoserstraße 15, 04318 Leipzig, Germany
2University Center of Orthopedics and Trauma Surgery, University Hospital “Carl Gustav Carus”, TU Dresden, Fetscherstraße 74, 01307 Dresden, Germany
3Department of Oral and Maxillofacial Surgery, University Hospital “Carl Gustav Carus”, TU Dresden, Fetscherstraße 74, 01307 Dresden, Germany
4Department of Metabolomics, Helmholtz-Centre for Environmental Research-UFZ, Permoserstraße 15, 04318 Leipzig, Germany
5Institute of Pharmacy, Faculty of Biosciences, Pharmacy and Psychology, University of Leipzig, 04103 Leipzig, Germany
6Institute of Physiological Chemistry, TU Dresden, Fiedlerstraße 42, 01307 Dresden, Germany
7Department of Biotechnology, Chemistry and Environmental Engineering, Aalborg University, Sohngaardsholmsvej 49, 9000 Aalborg, Denmark

Received 28 February 2014; Revised 3 June 2014; Accepted 4 June 2014; Published 4 August 2014

Academic Editor: Antonio Salgado

Copyright © 2014 Stefan Kalkhof 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. J. Salbach, T. D. Rachner, M. Rauner et al., “Regenerative potential of glycosaminoglycans for skin and bone,” Journal of Molecular Medicine, vol. 90, no. 6, pp. 625–635, 2012. View at Publisher · View at Google Scholar · View at Scopus
  2. D. R. Yager, R. A. Kulina, and L. A. Gilman, “Wound fluids: a window into the wound environment?” The International Journal of Lower Extremity Wounds, vol. 6, no. 4, pp. 262–272, 2007. View at Publisher · View at Google Scholar · View at Scopus
  3. N. J. Trengove, H. Bielefeldt-Ohmann, and M. C. Stacey, “Mitogenic activity and cytokine levels in non-healing and healing chronic leg ulcers,” Wound Repair and Regeneration, vol. 8, no. 1, pp. 13–25, 2000. View at Publisher · View at Google Scholar · View at Scopus
  4. S. K. Beidler, C. D. Douillet, D. F. Berndt et al., “Inflammatory cytokine levels in chronic venous insufficiency ulcer tissue before and after compression therapy,” Journal of Vascular Surgery, vol. 49, no. 4, pp. 1013–1020, 2009. View at Publisher · View at Google Scholar
  5. E. R. Utz, E. A. Elster, D. K. Tadaki et al., “Metalloproteinase expression is associated with traumatic wound failure,” Journal of Surgical Research, vol. 159, no. 2, pp. 633–639, 2010. View at Publisher · View at Google Scholar · View at Scopus
  6. G. P. Ladwig, M. C. Robson, R. A. N. Liu, M. A. Kuhn, D. F. Muir, and G. S. Schultz, “Ratios of activated matrix metalloproteinase-9 to tissue inhibitor of matrix metalloproteinase-1 in wound fluids are inversely correlated with healing of pressure ulcers,” Wound Repair and Regeneration, vol. 10, no. 1, pp. 26–37, 2002. View at Publisher · View at Google Scholar · View at Scopus
  7. A. N. Moor, D. J. Vachon, and L. J. Gould, “Proteolytic activity in wound fluids and tissues derived from chronic venous leg ulcers,” Wound Repair and Regeneration, vol. 17, no. 6, pp. 832–839, 2009. View at Publisher · View at Google Scholar · View at Scopus
  8. R. Moseley, J. R. Hilton, R. J. Waddington, K. G. Harding, P. Stephens, and D. W. Thomas, “Comparison of oxidative stress biomarker profiles between acute and chronic wound environments,” Wound Repair and Regeneration, vol. 12, no. 4, pp. 419–429, 2004. View at Publisher · View at Google Scholar · View at Scopus
  9. J. Broadbent, T. Walsh, and Z. Upton, “Proteomics in chronic wound research: potentials in healing and health,” Proteomics—Clinical Applications, vol. 4, no. 2, pp. 204–214, 2010. View at Publisher · View at Google Scholar · View at Scopus
  10. M. Averbeck, S. Beilharz, M. Bauer et al., “In situ profiling and quantification of cytokines released during ultraviolet B-induced inflammation by combining dermal microdialysis and protein microarrays,” Experimental Dermatology, vol. 15, no. 6, pp. 447–454, 2006. View at Publisher · View at Google Scholar · View at Scopus
  11. M. H. Maurer, C. Berger, M. Wolf et al., “The proteome of human brain microdialysate,” Proteome Science, vol. 1, no. 1, article 7, 2003. View at Publisher · View at Google Scholar · View at Scopus
  12. C. Yang, P. Tsai, W. Chen, L. Liu, and J. Kuo, “Determination of extracellular glutathione in livers of anaesthetized rats by microdialysis with on-line high-performance liquid chromatography,” Journal of Chromatography B: Biomedical Sciences and Applications, vol. 667, no. 1, pp. 41–48, 1995. View at Publisher · View at Google Scholar · View at Scopus
  13. Y. Förster, W. Gao, A. Demmrich, U. Hempel, L. C. Hofbauer, and S. Rammelt, “Monitoring of the first stages of bone healing with microdialysis,” Acta Orthopaedica, vol. 84, no. 1, pp. 76–81, 2013. View at Publisher · View at Google Scholar · View at Scopus
  14. G. Wei, P.-T. Ding, J. Zheng, and W. Lu, “Pharmacokinetics of timolol in aqueous humor sampled by microdialysis after topical administration of thermosetting gels,” Biomedical Chromatography, vol. 20, no. 1, pp. 67–71, 2006. View at Publisher · View at Google Scholar · View at Scopus
  15. C. Gill, E. Parkinson, M. K. Church et al., “A qualitative and quantitative proteomic study of human microdialysate and the cutaneous response to injury,” The AAPS Journal, vol. 13, no. 2, pp. 309–317, 2011. View at Publisher · View at Google Scholar · View at Scopus
  16. L. J. Petersen, M. A. Sørensen, M. C. Codrea, H. D. Zacho, and E. Bendixen, “Large pore dermal microdialysis and liquid chromatography-tandem mass spectroscopy shotgun proteomic analysis: a feasibility study,” Skin Research and Technology, vol. 19, no. 4, pp. 424–431, 2013. View at Publisher · View at Google Scholar · View at Scopus
  17. G. Clough and M. Noble, “Microdialysis—a model for studying chronic wounds,” The International Journal of Lower Extremity Wounds, vol. 2, pp. 233–239, 2003. View at Google Scholar
  18. G. F. Clough, “Microdialysis of large molecules,” The AAPS Journal, vol. 7, no. 3, pp. E686–E692, 2005. View at Google Scholar · View at Scopus
  19. M. Schmohl, S. Beckert, T. O. Joos, A. Königsrainer, N. Schneiderhan-Marra, and M. W. Löffler, “Superficial wound swabbing: a novel method of sampling and processing wound fluid for subsequent immunoassay analysis in diabetic foot ulcerations,” Diabetes Care, vol. 35, no. 11, pp. 2113–2120, 2012. View at Publisher · View at Google Scholar · View at Scopus
  20. J. T. Wyffels, K. M. Fries, J. S. Randall et al., “Analysis of pressure ulcer wound fluid using two-dimensional electrophoresis,” International Wound Journal, vol. 7, no. 4, pp. 236–248, 2010. View at Publisher · View at Google Scholar · View at Scopus
  21. D. M. Cooper, E. Z. Yu, P. Hennessey et al., “Determination of endogenous cytokines in chronic wounds,” Annals of Surgery, vol. 219, no. 6, pp. 688–692, 1994. View at Publisher · View at Google Scholar · View at Scopus
  22. A. B. Wysocki and F. Grinnell, “Fibronectin profiles in normal and chronic wound fluid,” Laboratory Investigation, vol. 63, no. 6, pp. 825–831, 1990. View at Google Scholar · View at Scopus
  23. A. Estreicher, A. Broggiato, P. Duroux, E. Andersen, and G. Cimasoni, “Low molecular-weight proteins in human gingival crevicular fluid,” Archives of Oral Biology, vol. 41, no. 8-9, pp. 733–738, 1996. View at Publisher · View at Google Scholar · View at Scopus
  24. R. Gonzalez, L. L. Jennings, M. Knuth et al., “Screening the mammalian extracellular proteome for regulators of embryonic human stem cell pluripotency,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 8, pp. 3552–3557, 2010. View at Publisher · View at Google Scholar · View at Scopus
  25. S. Kliemt, C. Lange, W. Otto et al., “Sulfated hyaluronan containing collagen matrices enhance cell-matrix-interaction, endocytosis, and osteogenic differentiation of human mesenchymal stromal cells,” Journal of Proteome Research, vol. 12, no. 1, pp. 378–389, 2013. View at Publisher · View at Google Scholar · View at Scopus
  26. C. Goettsch, S. Kliemt, K. Sinningen, M. von Bergen, L. C. Hofbauer, and S. Kalkhof, “Quantitative proteomics reveals novel functions of osteoclast-associated receptor in STAT signaling and cell adhesion in human endothelial cells,” Journal of Molecular and Cellular Cardiology, vol. 53, no. 6, pp. 829–837, 2012. View at Publisher · View at Google Scholar · View at Scopus
  27. D. W. Huang, B. T. Sherman, and R. A. Lempicki, “Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources,” Nature Protocols, vol. 4, no. 1, pp. 44–57, 2009. View at Publisher · View at Google Scholar · View at Scopus
  28. H. Mi, N. Guo, A. Kejariwal, and P. D. Thomas, “PANTHER version 6: protein sequence and function evolution data with expanded representation of biological pathways,” Nucleic Acids Research, vol. 35, no. 1, pp. D247–D252, 2007. View at Publisher · View at Google Scholar · View at Scopus
  29. G. Ouyang, D. Vuckovic, and J. Pawliszyn, “Nondestructive sampling of living systems using in vivo solid-phase microextraction,” Chemical Reviews, vol. 111, no. 4, pp. 2784–2814, 2011. View at Publisher · View at Google Scholar · View at Scopus
  30. S. A. Eming, M. Koch, A. Krieger et al., “Differential proteomic analysis distinguishes tissue repair biomarker signatures in wound exudates obtained from normal healing and chronic wounds,” Journal of Proteome Research, vol. 9, no. 9, pp. 4758–4766, 2010. View at Publisher · View at Google Scholar · View at Scopus
  31. P. Picotti and R. Aebersold, “Selected reaction monitoring-based proteomics: workflows, potential, pitfalls and future directions,” Nature Methods, vol. 9, no. 6, pp. 555–566, 2012. View at Publisher · View at Google Scholar · View at Scopus
  32. T. Takasuka, M. Sakayama, S. Ishibashi, and I. Ide, “tsJT16, a cell-cycle ts mutant defective in a function operating soon after growth stimulation, fails to induce a primarily activated labile nuclear protein,” Cell Structure and Function, vol. 15, no. 1, pp. 47–52, 1990. View at Publisher · View at Google Scholar · View at Scopus
  33. M. Shi, D. Majumdar, Y. Gao et al., “Glia co-culture with neurons in microfluidic platforms promotes the formation and stabilization of synaptic contacts,” Lab on a Chip—Miniaturisation for Chemistry and Biology, vol. 13, no. 15, pp. 3008–3021, 2013. View at Publisher · View at Google Scholar · View at Scopus
  34. M. Ciborowski, J. L. Martin-Ventura, O. Meilhac et al., “Metabolites secreted by human atherothrombotic aneurysms revealed through a metabolomic approach,” Journal of Proteome Research, vol. 10, no. 3, pp. 1374–1382, 2011. View at Publisher · View at Google Scholar · View at Scopus
  35. J. Hadrevi, B. Ghafouri, A. Sjörs et al., “Comparative metabolomics of muscle interstitium fluid in human trapezius myalgia: an in vivo microdialysis study,” European Journal of Applied Physiology, vol. 113, no. 12, pp. 2977–2989, 2013. View at Google Scholar
  36. S. J. M. Yussof, E. Omar, D. R. Pai, and S. Sood, “Cellular events and biomarkers of wound healing,” Indian Journal of Plastic Surgery, vol. 45, no. 2, pp. 220–228, 2012. View at Publisher · View at Google Scholar · View at Scopus
  37. Y. Liu, D. Min, T. Bolton et al., “Increased matrix metalloproteinase-9 predicts poor wound healing in diabetic foot ulcers,” Diabetes Care, vol. 32, no. 1, pp. 117–119, 2009. View at Publisher · View at Google Scholar · View at Scopus
  38. I. S. Thorey, J. Roth, J. Regenbogen et al., “The Ca2+-binding Proteins S100A8 and S100A9 are Encoded by Novel Injury-regulated Genes,” The Journal of Biological Chemistry, vol. 276, no. 38, pp. 35818–35825, 2001. View at Publisher · View at Google Scholar · View at Scopus
  39. S. A. Müller, T. Kohajda, S. Findei et al., “Optimization of parameters for coverage of low molecular weight proteins,” Analytical and Bioanalytical Chemistry, vol. 398, no. 7-8, pp. 2867–2881, 2010. View at Publisher · View at Google Scholar · View at Scopus
  40. G. Cazander, G. N. Jukema, and P. H. Nibbering, “Complement activation and inhibition in wound healing,” Clinical and Developmental Immunology, vol. 2012, Article ID 534291, 14 pages, 2012. View at Publisher · View at Google Scholar · View at Scopus
  41. S. A. Eming, T. Krieg, and J. M. Davidson, “Inflammation in wound repair: Molecular and cellular mechanisms,” Journal of Investigative Dermatology, vol. 127, no. 3, pp. 514–525, 2007. View at Publisher · View at Google Scholar · View at Scopus
  42. N. Buchstein, D. Hoffmann, H. Smola et al., “Alternative proteolytic processing of hepatocyte growth factor during wound repair,” The American Journal of Pathology, vol. 174, no. 6, pp. 2116–2128, 2009. View at Publisher · View at Google Scholar · View at Scopus
  43. Y. Ishida, T. Kondo, A. Kimura, K. Matsushima, and N. Mukaida, “Absence of IL-1 receptor antagonist impaired wound healing along with aberrant NF-κB activation and a reciprocal suppression of TGF-β signal pathway,” Journal of Immunology, vol. 176, no. 9, pp. 5598–5606, 2006. View at Publisher · View at Google Scholar · View at Scopus
  44. A. Gutiérrez-Fernández, M. Inada, and M. Balbín, “Increased inflammation delays wound healing in mice deficient in collagenase-2 (MMP-8),” FASEB Journal, vol. 21, no. 10, pp. 2580–2591, 2007. View at Publisher · View at Google Scholar
  45. M. J. Reiss, Y. Han, E. Garcia, M. Goldberg, H. Yu, and W. L. Garner, “Matrix metalloproteinase-9 delays wound healing in a murine wound model,” Surgery, vol. 147, no. 2, pp. 295–302, 2010. View at Publisher · View at Google Scholar · View at Scopus
  46. G. Leoni, A. Alam, P. Alexander Neumann et al., “Annexin A1, formyl peptide receptor, and NOX1 orchestrate epithelial repair,” Journal of Clinical Investigation, vol. 123, no. 1, pp. 443–454, 2013. View at Publisher · View at Google Scholar · View at Scopus