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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.
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.
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.
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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]
Collagen, type I, alpha 1, also known as alpha-1 type I collagen, is a protein that in humans is encoded by the COL1A1 gene. COL1A1 encodes the major component of type I collagen , the fibrillar collagen found in most connective tissues , including cartilage .
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 ...
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