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Collagen is also abundant in corneas, blood vessels, the gut, intervertebral discs, and the dentin in teeth. [3] In muscle tissue, it serves as a major component of the endomysium. Collagen constitutes 1% to 2% of muscle tissue and 6% by weight of skeletal muscle. [4] The fibroblast is the most common cell creating collagen in animals.
Collagen is a protein that strengthens and supports many tissues in the body, including cartilage, bone, tendon, skin and the white part of the eye . The COL1A1 gene produces a component of type I collagen , called the pro-alpha1(I) chain.
Collagen, a key component of the animal extracellular matrix, is made through cleavage of pro-collagen by collagenase once it has been secreted from the cell. This stops large structures from forming inside the cell itself. In addition to being produced by some bacteria, collagenase can be made by the body as part of its normal immune response.
Chemical Structure of Type I Collagen. Type I collagen has a triple-helical form which is caused by its amino acid composition. Its specific domain follows an order of G-X-Y In which the X and Y slots are occupied by any amino acid other than glycine however these slots are typically occupied by both hydroxyproline and proline, not in any particular order. [5]
A fibroblast is a type of biological cell typically with a spindle shape [1] that synthesizes the extracellular matrix and collagen, [2] produces the structural framework for animal tissues, and plays a critical role in wound healing. [3] Fibroblasts are the most common cells of connective tissue in animals.
Type V Collagen is considered a regulatory fibril forming collagen. [5] Collagen V is associated with the COL5A1 gene which is the gene which provides instructions to produce Collagen V. Type V Collagen, like other collagens, is made up of procollagen molecules. Collagen V molecular isoforms are α1(V)α2(V)α3(V), α1(V)3, and α1(V)2 α2(V).
Though one's body produces peptides naturally, peptides are also found in many food and supplement sources. "All the food we eat is broken down by the body into amino acids," explains Stevenson.
The assembly of collagen fibrils, fibrillogenesis appears to be a self-assembly process although there is much speculation about the specifics of the mechanism through which the body produces collagen fibrils. [1] In the body, collagen fibrils are composed of several types of collagen as well as macromolecules.