Type I collagen particles: stimulates healing with high patient satisfaction and substantial reduction in health care costs. Estimates show that healing with Helisorb Particles is achieved at approximately one third the cost of preceding treatment that has failed to bring about healing.

Helisorb Particles produce excellent outcomes in wounds where standard care has failed or where the clinician assesses that standard care may not bring about desired outcomes.

How long should you wait for signs of healing before considering switching to Type I collagen?
Shehan et al 2003 showed that 4 weeks of observation is a robust predictor of healing at 12 weeks.

4 weeks may serve as a pivotal clinical decision point in the care of diabetic foot ulcers for early identification of patients who may not respond to standard care and may need additional treatment.

Helisorb Particles:

  • Are highly absorbent and create an environment conducive to healing by initiating chemotaxis of granulocytes, macrophages and fibroblasts
  • Reduces wound pH levels
  • intact Type I collagen molecules act as a scaffold for cellualr attachment
  • Remove exudate, reduce inflammation and oedema, and allow for gaseous exchange
  • Act as a natural stimulant for autolytic debridement
  • Transforms wounds from inflammation phase to remodeling phase. Rapid reduction of inflammation.

Indications

  • Chronic / non-healing wounds eg DFU
  • Dehisced surgical wounds
  • Low to high exudating wounds, infected wounds, sloughy (wet or dry) wounds
  • Cavity wounds
  • EB wounds

In chronic/non-healing wounds, Helisorb Particles effectively act as a competitive substrate for excess matrix metalloproteinase-2, matrix metalloproteinase-9, and bacterial collagenase and influences this imbalance positively.

The increased accessible surface of the particles plays a crucial factor in effectiveness.

See References

References

  1. Hampton S, Understanding the pH balance in wound healing, JCN 2008,22:05
    Sheehan P, Jones P, Caselli A, Giurini JM, Veves A. Percent change in wound area of diabetic foot ulcers over a 4-week period is a robust predictor of complete healing in a 12-week prospective trial Diabetes Care. 2003 Jun;26(6):1879-822.
    Elgharably, H.et al . A Modified collagen gel enhances healing outcome in a preclinical swine model of excisional wounds. Wound Repair and Regeneration. March 2013
    Krieg T. Collagen in the Healing Wound. WOUNDS. 1995;7(Suppl A):5A–12A
  2. Karukonda S, Flynn T, Boh E, Russo G, Milikan L. The effects of drugs on wound healing:part 1. International J of Dermatology 2000;39:250-7r
  3. Schultz G, Mast B. Molecular Analysis of the Environment of Healing and Chronic Wounds: Cytokines, Proteases and Growth Factors. Wounds 1998;10:1F-9F.
  4. Bailey A. Perspective article: the fate of collagen implants in tissue defects. Wound Repair Regen 2000;8:5-12.
  5. Montesano R, Orci L, Vasselli F. In vitro rapid organization of endothelial cells into capillary-like networks is promoted by collagen matrices. J Cell Biol 1983;97:1648-52.
  6. Albini A, Dadelmann-Grill BC. Collagenolytic cleavage products of collagen type I as chemoatractants for human dermal fibroblasts, Eur. J Cell Biol 1985;36:104-7.
  7. Doillon CJ, Silver FH, Olson RM, Kamath CY, Berg RA. Fibroblast and Epidermal Cell-Type I Collagen Interactions: Cell Culture and Human Studies. Scanning Microscopy 1988; 2(2):985-992.
  8. Kakagia DD et.al. “Synergistic action of protease modulating matrix and autologous growth factors in healing of diabetic foot ulcers. A prospective randomized trial.” Journal of Diabetic Complications Vol. 21(6) Nov-Dec 2007, p.387-391
  9. Li F, et al “Low Molecular weight peptides derived from extracellular matrix as chemoattractants for primary endothelial cells” Endothelium, Vol. 11(3-4) May-Aug 2004 p.199-206
  10. Palmieri B. Heterologous Collagen in Wound Healing: A Clinical Study. International Journal of Tissue Reaction 1992; 14:21-25.
  11. Jeffrey J. Metalloproteinases and Tissue Turnover. WOUNDS, A Compendium of Clinical Research and Practice. Vol 7, Supplement A, September/October 1995, p13A-22A.
  12. Pilcher, BK, Dumin JA, Sudbeck BD, Krane SM, Welgus HG, Parks WC. The Activity of Collagenase-1 Is Required for Keratinocyte Migration on a Type I Collagen Matrix. The Journal of Cell Biology, Volume 137, Number 6, June 16, 1997 1445–1457.
  13. Saito S et.al. “Role of matrix metalloproteinases 1, 2, and 9 and tissue inhibitor of matrix metalloproteinase-1 in chronic venous insufficiency”, Journal of Vascular Surgery Vol. 34(5), p.930-938 Nov. 2001.
  14. Metzmacher I Ruth P Abel M Friess W . In vitro binding of matrix metalloproteinase-2 (MMP-2), MMP-9, and bacterial collagenase on collagenous wound dressings. >Wound Repair Regen. . 2007 Jul-Aug;15(4):549-55