Type-II collagen
Type-II collagen is the main component of cartilage, a type of connective tissue found in many parts of the body. It is a fibrillar collagen that is primarily located in cartilage, but can also be found in the vitreous humor of the eye.
Structure[edit | edit source]
Type-II collagen is a triple helix structure, composed of three polypeptide chains, each of which is a left-handed helix. These three chains are wound together to form a right-handed superhelix, a structure that is stabilized by the presence of hydrogen bonds. Each chain is composed of repeating units of the amino acids glycine, proline, and hydroxyproline.
Function[edit | edit source]
The primary function of type-II collagen is to provide tensile strength and toughness to tissues that require resistance to mechanical forces, such as cartilage. It also plays a role in the development and maintenance of the extracellular matrix, a three-dimensional network of extracellular macromolecules such as collagen, enzymes, and glycoproteins that provide structural and biochemical support to surrounding cells.
Clinical significance[edit | edit source]
Mutations in the COL2A1 gene, which encodes the type-II collagen protein, can lead to a variety of disorders. These include achondrogenesis, hypochondrogenesis, Kniest dysplasia, and Stickler syndrome. In addition, degradation of type-II collagen is a key event in the progression of osteoarthritis.
See also[edit | edit source]
References[edit | edit source]
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Contributors: Prab R. Tumpati, MD