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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.
It is a rigid, non-soluble, fibrous protein that adds up to one-third of the proteins in the human body. Collagen is mostly made up of molecules packed together to form long and thin fibrils that support each other and ensure the skin is strong and elastic. [2] Various types of collagens have individual roles and structures.
The FDA approved the first human clinical trial of the collagen meniscus scaffold which was carried out at The Stone Clinic from 1991-1994. Recent 15-year follow-ups on these patients revealed continuing successful outcomes. The U.S. Food and Drug Administration gave U.S. approval for a collagen meniscus implant (CMI) device designed by Stone ...
PRP is derived from the patient's own blood and may contain growth factors that increase collagen production. [3] It can be applied topically to the entire treatment area during and after collagen induction therapy treatments or injected intradermally to scars. Efficacy of the combined treatments remains in question pending scientific studies ...
The C-terminal telopeptide (CTX), also known as carboxy-terminal collagen crosslinks, is the C-terminal telopeptide of fibrillar collagens such as collagen type I and type II. It is used as a biomarker in the serum to measure the rate of bone turnover .
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The N-terminal telopeptide (NTX), also known as amino-terminal collagen crosslinks, is the N-terminal telopeptide of fibrillar collagens such as collagen type I and type II. It is used as a biomarker to measure the rate of bone turnover. NTX can be measured in the urine (uNTX) or serum (serum NTX). [1]
The packing structure of collagen has not been defined to the same degree outside of the fibrillar collagen types, although it has been long known to be hexagonal. [ 33 ] [ 81 ] [ 82 ] As with its monomeric structure, several conflicting models propose either that the packing arrangement of collagen molecules is 'sheet-like', or is microfibrillar .