COL1A1 comprises the pro-alpha 1 chains of type I collagen whose triple helix comprises two alpha 1 chains and one alpha 2 chain. Type I collagen is a fibril-forming collagen found in most connective tissues. Mutations in COL1A1 are associated with osteogenesis imperfecta types I-IV, Ehlers-Danlos syndrome type VIIA, Ehlers-Danlos syndrome Classical type, Caffey disease and idiopathic osteoporosis. COL1A1 mutations are also associated with a particular type of skin tumor called dermatofibrosarcoma protuberans, resulting from upregulated expression of the growth factor. A suppressive biological function of COL1A1 in glioma progression has also been reported. The expression of Collagen I is abundant in all tissues including skin and bone. Type I collagen has been used as a marker of osteoblastic differentiation.
COL1A1 comprises the pro-alpha 1 chains of type I collagen whose triple helix comprises two alpha 1 chains and one alpha 2 chain. Type I collagen is a fibril-forming collagen found in most connective tissues. Mutations in COL1A1 are associated with osteogenesis imperfecta types I-IV, Ehlers-Danlos syndrome type VIIA, Ehlers-Danlos syndrome Classical type, Caffey disease and idiopathic osteoporosis. COL1A1 mutations are also associated with a particular type of skin tumor called dermatofibrosarcoma protuberans, resulting from upregulated expression of the growth factor. A suppressive biological function of COL1A1 in glioma progression has also been reported. The expression of Collagen I is abundant in all tissues including skin and bone. Type I collagen has been used as a marker of osteoblastic differentiation.
COL1A1 comprises the pro-alpha 1 chains of type I collagen whose triple helix comprises two alpha 1 chains and one alpha 2 chain. Type I collagen is a fibril-forming collagen found in most connective tissues. Mutations in COL1A1 are associated with osteogenesis imperfecta types I-IV, Ehlers-Danlos syndrome type VIIA, Ehlers-Danlos syndrome Classical type, Caffey disease and idiopathic osteoporosis. COL1A1 mutations are also associated with a particular type of skin tumor called dermatofibrosarcoma protuberans, resulting from upregulated expression of the growth factor. A suppressive biological function of COL1A1 in glioma progression has also been reported. The expression of Collagen I is abundant in all tissues including skin and bone. Type I collagen has been used as a marker of osteoblastic differentiation.
