Type I collagen alpha-2 chain (COL1A2)

Type I collagen alpha-2 chain is one of the two unique polypeptide chains that assemble into the triple helix structure of type I collagen, the most abundant fibrillar collagen in the human body[1][2][3][5][7]. Synthesized from the COL1A2 gene, this chain combines with two alpha-1 chains (encoded by COL1A1) to form mature type I collagen fibers that provide structural support and tensile strength to connective tissues such as bone, tendon, skin, and the sclera. Mutations in the COL1A2 gene disrupt collagen synthesis or fiber assembly, resulting in connective tissue disorders—most notably various forms of osteogenesis imperfecta and certain subtypes of Ehlers-Danlos syndrome, which are characterized by bone fragility, joint hypermobility, and sometimes cardiovascular involvement[1][3][5]. The Type I collagen alpha-2 chain is classified as a structural extracellular matrix protein and is not a receptor, enzyme, transporter, or a typical druggable target. There are currently no approved therapies that directly target the COL1A2 protein or gene, but its mutations serve as important diagnostic biomarkers for associated connective tissue diseases[1][5].

Other names

Collagen alpha-2(I) chainAlpha-2 type I collagenCOL1A2