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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.
Collagens are complex molecules that provide structure, strength, and elasticity to connective tissue. Type II and type XI collagen disorders are grouped together because both types of collagen are components of the cartilage found in joints and the spinal column, the inner ear, and the jelly-like substance that fills the eyeball (the vitreous ).
Collagen (/ ˈ k ɒ l ə dʒ ə n /) is the main structural protein in the extracellular matrix of the connective tissues of many animals. It is the most abundant protein in mammals, [1] making up 25% to 35% of protein content. Amino acids are bound together to form a triple helix of elongated fibril [2] known as a collagen helix.
Collagen alpha-2(XI) chain is a protein that in humans is encoded by the COL11A2 gene. [5] [6] [7] The COL11A2 gene produces one component of this type of collagen, called the pro-alpha2(XI) chain. Type XI collagen adds structure and strength to the tissues that support the body's muscles, joints, organs and skin (the connective tissue).
[1] [2] Alpha collagen is designed to be used as a supplement for osteoarthritis, based on the theory of the different environments of the extracellular matrix (ECM). The ECM of joint cartilage comprises many classes of macromolecules; collagen (type I, II, VI, X collagen fibrils) and proteoglycans.
In cases like this, the body will form a scar in the area using a special type of cartilage called fibrocartilage. [2] Fibrocartilage is a tough, dense, and fibrous material that helps fill in the torn part of the cartilage; however, it is not an ideal replacement for the smooth, glassy articular cartilage that normally covers the surface of ...
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