Collagen. (from greek. kóla, means glue, and gennân, means produce). m

Collagen is the main protein of connective tissue in animals and the most abundant protein in mammals, making up about 25% of the total protein content. It is one of the long, fibrous structural proteins whose functions are quite different from those of globular proteins such as enzymes; tough bundles of collagen called collagen fibers are a major component of the extracellular matrix that supports most tissues and gives cells structure from the outside, but collagen is also found inside certain cells. Collagen has great tensile strength, and is the main component of cartilage, ligaments, tendons, bone and teeth. Along with soft keratin, it is responsible for skin strength and elasticity, and its degradation leads to wrinkles that accompany aging. It strengthens blood vessels and plays a role in tissue development.

Collagen Molecule in Triple Helix form

The tropocollagen or "collagen molecule" subunit is a rod about 300 nm long and 1.5 nm in diameter, made up of three polypeptide strands, each of which is a left-handed helix, not to be confused with the commonly occurring alpha helix, which is right-handed. These three left-handed helices are twisted together into a right-handed coiled coil, a triple helix, a cooperative quaternary structure stabilized by numerous hydrogen bonds. Tropocollagen subunits spontaneously self-assemble, with regularly staggered ends, into even larger arrays in the extracellular spaces of tissues. There is some covalent crosslinking within the triple helices, and a variable amount of covalent crosslinking between tropocollagen helices, to form the different types of collagen found in different mature tissues — similar to the situation found with the α-keratins in hair. Collagen's insolubility was a barrier to study until it was found that tropocollagen from young animals can be extracted because it is not yet fully crosslinked

Information extracted from Wikipedia.org

In 1967 Thiele described a method about how to separate collagen from animal skin. Since then, many experimental and clinical investigations have demonstrated the benefits of the usage of heterologous collagen in membranes, as haemostatic, healing stimulant and filler of deep wounds with tissue loss.

Collagen is a proteic substance contained in all human and animal connective tissue, which can be isolated from those tissues (mainly from the skin and bovine tendons) and it is chemically and structurally the same in humans and in animals. This likeness allows the usage of lyophilised collagen in different medical areas without rejection problems, allergies or any other sign of intolerance.

Collagen Interlaced Structure

The collagen, because of its hydrophilic characteristics, is applied in wounds and forms the skeleton on which new granulation tissue will be developed.

The pores of the collagen membranes are of an optimum size offering no resistance to granulation tissue penetration.

Applied in a wound, this material, similar to a plastic sponge, absorbs the secretions loaded with cells. By the leukocytes disintegration a proteasa is liberated, this proteasa is supposed to be the responsible from the slow collagen lysis.

Collagen is disintegrated in particles which don't produce any antigenic effect. The amino acids and peptides resultants can probably be reused thanks to the diffusion through the granulation tissue. In spite of this lysis, the contact between the collagen membrane and the wound remains unaffected.

Between the wound and the collagen membrane stays constant: pH, ionic levels, protheic composition, cellular elements and oxygen.

Through the collagen membrane capital operation, the absoption from the wound secretions happens. The secretions, because of containing leukocytes, acts as an outpost defense.