Collagen type I alpha 2 chain (COL1A2) (COL1A2)

Collagen type I alpha 2 (COL1A2) is a fundamental structural protein that constitutes one of the three polypeptide chains in type I collagen, the most abundant collagen in the human body [1][3]. It typically combines with two alpha 1 chains to form a triple-helical procollagen molecule, which is essential for providing tensile strength and structural integrity to tissues such as bone, skin, tendons, and the cornea [1][10]. Mutations in the COL1A2 gene are the primary cause of several hereditary connective tissue disorders, most notably osteogenesis imperfecta (brittle bone disease) and various subtypes of Ehlers-Danlos syndrome [1][15]. In addition to its role in genetic diseases, COL1A2 is frequently overexpressed in the tumor microenvironment of various cancers, including glioblastoma and ovarian cancer, where it promotes tumor cell proliferation, invasion, and chemoresistance [8][12]. Consequently, it has emerged as a therapeutic target for gene-editing strategies aimed at silencing mutant alleles and for pharmacological interventions designed to inhibit its pathological deposition in fibrosis and malignancy [6][14]. Monitoring COL1A2 expression and its degradation products also serves as a valuable clinical tool for assessing bone turnover and disease progression in both genetic and oncological contexts [4][16].

Other names

Alpha-2 type I collagenCollagen alpha-2(I) chainAlpha 2(I) procollagenOI4EDSCVEDSARTH2Osteogenesis imperfecta type IVAlpha 2 type I procollagen

Drugs targeting COL1A2 primarily act by inhibiting its transcription (e.g., via TGF-beta/SMAD pathway modulation), reducing its extracellular deposition in fibrotic or malignant tissues, or utilizing gene-targeting vectors to silence or correct mutant alleles in genetic connective tissue disorders [6][8][14].