Products

 

Neuskin-F is a biodegradable Type I collagen film membrane
derived from a Piscean source.

 

• provides an optimal environment and natural substrate for cellular attachment, growth and vascularisation.
• facilitates epithelialisation and provides a matrix for tissue regeneration
• lowers wound pH
• acts as a biodegradable haemostat
• transparent membrane allows wound observation

Indications:

• Donor sites : Intra-operatively or non-healing
• Epithelialisation of granulated wound beds
• Elective loss of epidermis eg epidermal removal from recipient site for autologous melanocyte keratinocyte transfer
• Superficial burns, scalds

Contraindications:   Infected wounds
Precautions:  Patients sensitive to collagen from any source

Ordering Information

 

Code	Description	Units
NSNF1001	Neuskin-F film membrane, 5cm x 5cm	Box of 10
NSNF1002	Neuskin-F film membrane, 10cm x 10cm	Box of 5
NSNF1003	Neuskin-F film membrane, 10cm x 20cm	Box of 2

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Helisorb® Particles

   

Type I collagen particles: facilitates healing in difficult non-healing wounds.

Helisorb Particles produce excellent outcomes in wounds where standard care has failed.

• Are highly absorbent and create an environment conducive to healing
• Reduces wound pH levels
• 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

Indications
 

• Chronic / non-healing wounds
• Low to high exudating wounds, infected wounds, sloughy (wet or dry) wounds
• Dehisced surgical wounds
• Cavity 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.
Exogenous collagen may also involve specific modulation of the cytokine response in bacteria-containing wounds.
The increased accessible surface of the particles plays a crucial factor in effectiveness.
See References

Contraindication:  venous ulcers under compression bandaging.

Ordering Information

Code	Description	Units
HSBP1002	Helisorb® Particles, 5ml vial	Box of 5
HSBP1003	Helisorb® Particles, 10ml vial	Box of 2

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Helisorb® Sheet

An intact Type I lyophilised porous collagen primary dressing

Indications: 

• Wounds up to 0.5cm depth
• non-healing wounds
• As dressing over primary closure
• Delayed primary closure
• Partial thickness burns
• Large donor sites

• Ordering Information
  

  Code	Description	Units
  HSBS1001	Helisorb® Sheet, 5cm x 10cm	Box of 5
  HSBS1002	Helisorb® Sheet, 10cm x 10cm	Box of 5
  HSBS1003	Helisorb® Sheet, 10cm x 15cm	Box of 5
  HSBS1004	Helisorb® Sheet, 10cm x 20cm	Box of 5
  HSBS1005	Helisorb® Sheet, 10cm x 30cm	Box of 5
  HSBS1006	Helisorb® Sheet, 20cm x 30cm	Box of 5

  
  Medira's Type I collagen range consists of Intact Type I fish collagen, are non cross-linked, and are biocompatible as per EN ISO 10093 standards, non-toxic, non-allergenic, non-immunogenic, non-pyrogenic.

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Helisorb® Powder

Helisorb® Powder is an adjunctive hemostat for soft tissue bleeding and oozing.

Helisorb® Powder  is 100% microfibrillar collagen powder of Piscean origin.

No human thrombin, no bovine or porcine collagen, no cellulose, no polysaccharide powder, no chemical constituents.

• Controls bleeding without damaging tissues
• Achieves hemostasis within a few seconds to one minute
• Can be used in both open and laparoscopic surgery
• Adheres perfectly and immediately to all bleeding surfaces
• Reduces risk of adhesion development
• Reduces operating time
• Reduces risk of infection by reducing wound pH

Contraindications: Neurological and Opthalmic surgery

Ordering Information

Code	Description	Units
HSSB1001	Helisorb® Powder, 1g/5ml vial	Box

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References

1.        Hampton S, Understanding the pH balance in wound healing, JCN 2008,22:05

2.        Krieg T. Collagen in the Healing Wound. WOUNDS. 1995;7(Suppl A):5A–12A

3.        Schultz GS, Sibbald RG, Falanga V, et al. Wound bed preparation: a systematic approach to wound management. Wound Repair Regen. 2003;11(Suppl 1):1–28

4.        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

5.        Schultz G, Mast B. Molecular Analysis of the Environment of Healing and Chronic Wounds: Cytokines, Proteases and Growth Factors. Wounds 1998;10:1F-9F.

6.        Bailey A. Perspective article: the fate of collagen implants in tissue defects. Wound Repair Regen 2000;8:5-12.

7.        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.

8.        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.

9.        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.

10.     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

11.     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

12.     Palmieri B. Heterologous Collagen in Wound Healing:  A Clinical Study.  International Journal of Tissue Reaction 1992; 14:21-25.

13.     Jeffrey J.  Metalloproteinases and Tissue Turnover.  WOUNDS, A Compendium of Clinical Research and Practice.  Vol 7, Supplement A, September/October 1995, p13A-22A.

14.     Parks WC.  The Production, Role, and Regulation of Matrix Metalloproteinsases in the Healing Epidermis.  WOUNDS, A Compendium of Clinical Research and Practice.  Vol 7, Supplement A, September/October 1995, p23A-A33).

15.     Clark RAF, ed: In The Molecular and Cellular Biology of Wound Repair, 2nd Edition. NY, Plenum Press, 1996, pp. 443.

16.     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.

17.     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.

18.     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

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