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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.
Atrophic non-union results in re-absorption and rounding of bone ends [6] due to inadequate blood supply and excessive mobility of the bone ends. [4] Mal-union: healing occurs but the healed bone has 'angular deformity, translation, or rotational alignment that requires surgical correction'. This is most common in long bones such as the femur. [10]
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 .
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.
The COL3A1 gene is located on the long (q) arm of chromosome 2 at 2q32.2, between positions 188 974 372 and 189 012 745. The gene has 51 exons and is approximately 40 kbp long. [7] The COL3A1 gene is in tail-to-tail orientation with a gene for another fibrillar collagen, namely COL5A2. [7]
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.