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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.
Digestion of native collagen in the triple helical region at -Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3' Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum.
Collagen is the most abundant protein in the ECM, and is the most abundant protein in the human body. [ 17 ] [ 18 ] It accounts for 90% of bone matrix protein content. [ 19 ] Collagens are present in the ECM as fibrillar proteins and give structural support to resident cells.
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.
Type V collagen is a form of fibrillar [1] collagen associated with classical Ehlers-Danlos syndrome. It is found within the dermal/epidermal junction, placental tissues, as well as in association with tissues containing type I collagen. [2] Type V collagen is a part of the family of collagen proteins consisting of Collagen I- Collagen XXVIII.
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