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
Cartilage is a resilient and smooth type of connective tissue. Semi-transparent and non-porous, it is usually covered by a tough and fibrous membrane called perichondrium. In tetrapods, it covers and protects the ends of long bones at the joints ...
and 85–90% of collagen of articular cartilage.
Type II collagen is organised into
fibril
Fibrils () are structural biological materials found in nearly all living organisms. Not to be confused with fibers or protein filament, filaments, fibrils tend to have diameters ranging from 10 to 100 nanometers (whereas fibers are micro to ...
s. This fibrillar network of
collagen
Collagen () is the main structural protein in the extracellular matrix of the connective tissues of many animals. It is the most abundant protein in mammals, making up 25% to 35% of protein content. Amino acids are bound together to form a trip ...
allows the cartilage to entrap the
proteoglycan
Proteoglycans are proteins that are heavily glycosylated. The basic proteoglycan unit consists of a "core protein" with one or more covalently attached glycosaminoglycan (GAG) chain(s). The point of attachment is a serine (Ser) residue to w ...
aggregate, as well as providing tensile strength to the tissue. Oral administration of native type II collagen induces oral tolerance to pathological immune responses and the administration of type II collagen tablets together with paracetamol might be more effective at reducing symptoms of osteoarthritis than paracetamol by itself.
See also
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Type I collagen
Type I collagen is the most abundant collagen of the human body, consisting of around 90% of the body's total collagen in vertebrates. Due to this, it is also the most abundant protein type found in all vertebrates. Type I forms large, eosinop ...
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Collagen, type III, alpha 1
References
External links
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Collagens
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