Procedure:

1. Remove from package and separate the clear backing from the product.
2. Soak in sterile saline or water for a minimum of 5 minutes.
3. Make slits with surgical scalpel if needed and/or if exudate is present.
4. Apply to wound bed, remove any air bubbles.
5. Refer to the Helicoll Layering Guide for dressing recommendations.

For surgical settings: Helicoll can be sutured or stapled in place as needed.

Click here to enlarge image

IMPORTANT:

Helicoll is always to remain directly onto the wound and never removed or wiped off during a dressing change.

WHY TYPE-1 COLLAGEN?

Type-1 Collagen that is a full molecule, purified, and uncross-linked provides 3,000 receptor sites per molecule for growth factors such as fibroblasts to attach to making it an excellent matrix for use in wound healing. Type-I Collagen is 97% the same across different species whereas Type-II & III is only 80% similar in the same species.

For instance, Type-I collagen is extremely similar, or the same, in human as it is in a cow or in a bird. Type-I is least immunogenic. The similarity of Type-I Collagen across species is believed to be the reason that you see a dramatic pain reduction with the use of Helicoll™ with the most painful wounds such as donor sites and burns. Type-I Collagen does not cause an immunogenic response due to its lack of sulfur-containing amino acid cysteine. Type-III has more cysteine than Type-I, & Type-II has the highest concentration making Type-II & Type-III highly immunogenic.

What Is Helicoll Made Of?

How Helicoll™ Collagen Differs From Other Collagen Dermal Replacements?
Collagen exposed during wound formation activates the clotting phase and facilitates the migration of the inflammatory cells to the wound bed. If the matrix made of collagen is native, pure and non-immunogenic, it will possess all the natural binding sites to all the cytokines, including epidermal growth factor (EGF), fibronectin, fibrinogen, histamine, platelet derived growth factor (PDGF), serotonin, and von Willebrand factor etc…A cross-linked or contaminated Type III collagen cannot effectively achieve such wound healing characteristics.

Additionally, a native collagen dressing also has cell membrane binding sites that would attract the neutrophil, for debris scavenging, bacteria destruction, and leukocytes along with the macrophages/monocytes, for wound healing via secretion of enzymes and cytokines for tissue reconstruction.

Subsequently, epithelialization, angiogenesis, granulation tissue formation, and collagen deposition are the principal steps in this anabolic portion of wound healing. It is also hypothesized that the native Type-I collagen creates adhesion sites for growth factors and it would trigger a phenomenon called “Cell Signal Transduction” through which the floating stem cells are converted to appropriate cell-lines to regenerate the damaged tissue.

The other collagen preparations, mostly contaminated with type-III collagen, elastin, lipids and other immunogenic proteins, following chemical cross-linking, that is required to minimize their immunogenicity, does not maintain the native chemistry of collagen and thereby loses its bioactivity and also other binding abilities and gets significantly impaired with its wound healing abilities.

The illustration below depicts the behavior of cross-linked collagen vs. non-crosslinked collagen.

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