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Original Papers

The Efficacy of a Polyhydrated Ionogen Impregnated Dressing in the Treatment of Recalcitrant Diabetic Foot Ulcers: a Multi-centre Pilot Study

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Pages 675-681 | Published online: 11 Mar 2016

References

  • Most R. S., Sinnock P. The epidemiology of lower extremity amputations in diabetic individuals. Diabetes Care, 1983, 6: 8791.
  • Centers for Disease Control and Prevention: National Diabetes fact sheet. National estimates on diabetes, 2000–2001. Available from http://www.cdc.gov/diabetes/pubs/estimates.htm. Accessed september 10, 2005.
  • Reiber G. E., Boyko E. J., Smith D. G. Lower extremity foot ulcers and amputations in diabetes. In: Harris M. I., Cowie C., Stern M. P. (eds.). National Diabetes Data Group of the National Institute of Diabetes and Digestive and Kidney Diseases. Bethesda, Maryland, 1995: 409–28. (DHEW publ. no.NIH 951468).
  • Ramsey S. D., Newton K., Blough D. Incidence, outcomes, and cost of foot ulcers in patients with diabetes. Diabetes Care, 1999. 22: 382–7.
  • Eckman M. H., Greenfield S., Mackey W. C. Foot infections in diabetic patients: decision and cost-effectiveness analyses. JAMA, 1995, 273: 712–720.
  • New J. P., McDowell D., Burns E. et al. Problem of amputations in patients with newly diagnosed diabetes mellitus. Diabet Med, 1998, 15: 760–4.
  • Apelqvist J., Bakker K., van Houtum W. H. et al. International consensus and practical guidelines on the management and the prevention of the diabetic foot: International Working Group on the Diabetic Foot. Diabetes Metab Res Rev, 2000, 16: 84S-92S.
  • Armstrong D. G, Lavery L. A. Evidence-based options for off-loading diabetic wounds. Clin Podiatr Med Surg, 1998, 15: 95–104.
  • Veves A., Sheehan P., Pham H. T. A randomized, controlled trial of Promogran (a collagen/oxidized regenerated cellulose dressing) vs. standard treatment in the management of diabetic foot ulcers. Arch Surg, 2002, 137: 822–7.
  • Cullen B., Smith R., McCulloch E. et al. Mechanism of action of PROMOGRAN, a protease modulating matrix, for the treatment of diabetic foot ulcers. Wound Repair Regen, 2002, 10: 1625.
  • Donaghue V. M., Chrzan J. S., Rosenblum B. I. et al. Evaluation of a collagen-alginate topical wound dressing in the management of diabetic foot ulcers. Adv Wound Care, 1998, 11: 114–9.
  • Wieman T. J., Smiell J. M., Su Y. Efficacy and safety of a topical gel formulation of recombinant human platelet-derived growth factor-BB (becaplermin) in patients with chronic neuropathic diabetic ulcers: a phase III randomized placebo-controlled doubleblind study. Diabetes Care, 1998, 21: 822–7.
  • Pollak R. A., Edington H., Jensen J. L. et al. A human dermal replacement for the treatment of diabetic foot ulcers. Wounds, 1997, 9: 175–83.
  • Pham H. T., Rosenblum B. I., Lyons T. E. Evaluation of a human skin equivalent (Apligraf), for the treatment of diabetic foot ulcers in a prospective, randomized, clinical trial. Wounds, 1999, 11: 7986.
  • Tarmuzzer R. W., Schultz G. S. Biochemical analysis of acute and chronic wound environments. Wound Repair Regen, 1996, 4: 321–5.
  • Mast B. A., Schultz G. S. Interactions of cytokines, growth factors and proteasesin acute and chronic wounds. Wound repair Regen, 1996, 4: 414–20.
  • Nwomeh B. C., Yager D. R., Cohen I. K. Physiology of the chronic wound. Clin Plast Surg, 1998, 25: 341–56.
  • Singer A. J., Clark R. A. Cutaneous wound healing. N Engl J Med, 1999, 341: 738–46.
  • Gillitzer R., Goebeler M. Chemokines in cutaneous wound healing. J Leukoc Biol, 2001, 69: 513–21.
  • Yager D. R., Zhang Y., Liang H.-X. et al. Wound fluids from human pressure ulcers contain elevated matrix metalloproteinase levels and activity compaired to surgical wound fluids. J Invest Dermatol, 1996, 107: 743–48.
  • Woessner J. F. Jr. The family of matrix metalloproteinases. Ann N Y Acad Sci, 1994, 732: 11–21.
  • Ravanti L., Kahari V. M. Matrix metalloproteinases in wound repair (review). Int J Mol Med, 2000, 6: 391–407.
  • Lobmann L., Schultz G., Lehnert H. Proteases and the diabetic foot syndrome: mechanisms and therapeutic implecations. Diabetes Care, 2005, 28: 461–71.
  • van den Berg A. J., Halkes S. B., Quarles van Ufford H. C. et al. A novel formulation of metal ions and citric acid reduces reactive oxygen species in vitro. J Wound Care, 2003, 12: 413–8.
  • Monroe S., Sampson E. M., Popp M. P. et al. Effect of poly-hydrated ionogen (PHI) on viability and matrix metalloproteinase levels in cultures of normal and diabetic human dermal fibro-blasts. Poster presented on Wound Healing Society Meeting, May 2005, Chicago, IL, USA.
  • Silhi N. Diabetes and wound healing. J Wound Care, 1998, 7: 47–51.
  • Levy D. M., Terenghi G., Gu X. H. Immunohistochemical measurements of nerves and neuropeptides in diabetic skin: relationship to tests of neurological function. Diabetologia, 1992, 35: 889–97.
  • Gibran N. S., Jang Y. C., Isik F. F. Diminished neuropeptide levels contribute to the impaired cutaneous healing response associated with diabetes mellitus. J Surg Res, 2002, 108: 122–8.
  • Goodson W. H., Hunt T. K. Wound healing and the diabetic patient. Surg Gynecol Obstet, 1979, 149: 600–8.
  • Lee T. S., Saltsman K. A., Ohashi H. et al. Activation of protein kinase C by elevation of glucose concentration: proposal for a mechanism in the development of diabetic vascular complications. Proc Natl Acad Sci USA, 1989, 86: 5141–5.
  • Greene D. A., Lattimer S. A., Sima A. A. Sorbitol phosphoinosi-tides, and sodium-potassium-ATPase in the pathogenesis of diabetic complications. N Engl J Med, 1987, 5: 599–606.
  • Wall S. J., Sampson M. J., Levell N. et al. Elevated matrix metalloproteinase-2 and-3 production from human diabetic dermal fibroblasts. Br J Dermatol, 2003, 149: 13–6.
  • Kjersem H., Hilsted J., Madsbad S. Polymorphonuclear leucocyte dysfunction during short term metabolic changes from normo-to hyperglycaemia in type I (insulin dependent) diabetic patients. Infection, 1988, 16: 215–21.
  • Yue D. K., McLennan S., Marsh M. Effects of experimental diabetes uraemia and malnutrition on wound healing. Diabetes, 1987, 36: 295–9.
  • Kahari V. M., Saarialho-Kere U. K. Matrix metalloproteinases in skin. Exp Dermatol, 1997, 6: 199–213.
  • Parsons S. L., Watson S. A., Brown P. D. et al. Matrix metalloproteinase. Br J Surg, 1997, 84: 160–6.
  • Wang J. F., Olson M. E., Reno C. R. et al. Molecular and cell biology of skin wound healing in a pig model. Connect Tissue Res, 2000, 41: 195–211.
  • Mun-Bryce S., Rosenberg G. A. Gealtinase B modulates selective opening of the blood-brain barrier during inflammation. Am J Physiol, 1998, 274: R1203–11.
  • Zhang H., Li C., Baciu P. C. Expression of integrins and MMPs during alkaline-burn-induced corneal angiogenesis. Invest Ophtalmol Vis Sci, 2002, 43: 955–62.
  • Armstrong D. G., Jude E. B. The role of matrix metalloproteinases in wound healing. J Am Podiatr Med Assoc, 2002, 92: 12–8.
  • Ladwig G. P., Robson M. C., Liu R. et al. Ratios of activated matrix metalloproteinase-9 to tissue inhibitor of matrix metallo-proteinase-1 in wound fluids are inversely correlated with healing of pressure ulcers. Wound Repair Regen, 2002, 101: 26–37.
  • Nwomeh B. C., Liang H.-X., Cohen I. K. et al. MMP-8 is the predominant collagenase in healing wounds and non-healing ulcers. J Surg Res, 2001, 81: 189–95.
  • Stricklin G. P., Li L., Jancic V. et al. Localization of mRNAs representing collagenase and TIMP in sections of healing human burn wounds. Am J Pathol, 1993, 143: 1657–66.
  • Saarialho-Kere U. K., Pentland A. P., Birkedal-Hansen H. et al. Distinct populations of basal keratinocytes express stromelysin-1 and stromelysin-2 in chronic wounds. J Clin Invest, 1994, 94: 7988.
  • Mauviel A. Cytokine regulation of metalloproteinase gene expression. J Cell Biochem, 1993, 53: 288–95.
  • Han Y. P., Tuan T. L., Wu H. et al. TNF-stimulates activation of pro-MMP-2 in human skin through NF-KappaB mediated induction of MT1-MMP. J Cell Sci, 2001, 114: 131–9.
  • Zhang Y., McCluskey K., Fujii K. et al. Differential regulation of monocyte matrix metalloproteinase and TIMP-1 production by TNF-alfa, granulocyte-macrophage CSF, and IL-1b through prostaglandin-dependent and independent mechanism. J Immunol, 1998, 161: 3071–6.
  • McClawley L. J., O’Brien P., Hudson L. G. Epidermal growth factor (EGF)-and scatter factor/hepatocyte growth factor (SF/HGF)-mediated keratinocyte migration is coincident with induction of matrix metalloproteinase. J Cell Physiol, 1998, 176: 255–65.
  • Mauviel A., Chung K. Y., Agarwal A. et al. Cell-specific induction of distinct oncogenes of the Jun family is responsible for differential regulation of collagenase gene expression by transforming growth factor-beta in fibroblasts and keratinocytes. J Biol Chem, 1996, 271: 10917–23.
  • Kim J. H., Hong S. H., Nah H. Y. et al. Influence of transforming growth factor-alpha on expression of matrix metalloproteinase-2, matrix metalloproteinase-9, and epidermal growth factor receptor gene in the mouse blastocysts. J Assist Reprod Genet, 2002, 19: 232–9.
  • Han Y. P., Tuan T. L., Hughes M. et al. Transforming growth factor-beta-and tumor necrosis factor-alpha-mediated induction and proteolytic activation of MMP-9 in human skin. J Biol Chem, 2001, 276: 22341–50.
  • Van Wart H. E., Birkedal-Hensen H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci USA, 1990, 87: 5578–82.
  • Vaalamo M., Weckroth M., Puolakkainen P. et al. Patterns of matrix metalloproteinase and TIMP-1 expression in chronic and normally healing human cutaneous wounds. Br J Dermatol, 1996, 135: 52–9.
  • Wysocki A. B., Staiano-Coico L., Grinnell F. Wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP-9. J Invest Dermatol, 1993, 101: 64–8.

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