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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.
The efficacy of allogeneic cultured keratinocytes and fibroblasts in bovine collagen (Gintuit) was evaluated in two clinical studies in adults with insufficient gingival tissue. [2] In each of the two studies, Gintuit was associated with an increase of at least 2 mm of gingival tissue in at least 50% of the study subjects.
Schematic of a CHP strand (labeled with an "X" tag) hybridizing to denatured collagen chains and forming a collagen triple helix. During disease progression, tissue development, or ageing, collagen can be extensively degraded by collagenolytic proteases, causing its triple helix to unfold at the physiological temperature due to reduced thermal stability.
Type II collagen is the basis for hyaline cartilage, including the articular cartilages at joint surfaces. It is formed by homotrimers of collagen, type II, alpha 1 chains. It makes up 50% of all protein in cartilage and 85–90% of collagen of articular cartilage.
Procollagen peptidase (EC 3.4.24.14, procollagen N-terminal peptidase, procollagen aminopeptidase, aminoprocollagen peptidase, aminoterminal procollagen peptidase, procollagen aminoterminal protease, procollagen N-terminal proteinase, type I/II procollagen N-proteinase, type III procollagen) is an endopeptidase involved in the processing of collagen.
Bovine somatotropin or bovine somatotrophin (abbreviated bST and BST), or bovine growth hormone (BGH), is a peptide hormone produced by cows' pituitary glands. [1] Like other hormones, it is produced in small quantities and is used in regulating metabolic processes. [ 1 ]
The CTX test measures for the presence and concentration of a crosslink peptide sequence of type I collagen, found, among other tissues, in bone. This specific peptide sequence relates to bone turnover because it is the portion that is cleaved by osteoclasts during bone resorption, and its serum levels are therefore proportional to osteoclastic ...
While degraded collagen could be an important marker of tissue damage, it is difficult to detect and target using conventional tools. As a result, a collagen hybridizing peptide is specifically hybridized to the degraded, unfolded collagen chains, can be used to image degraded collagen and inform tissue remodeling activity in various tissues. [16]
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