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.