Collagen is an extracellular matrix protein that serves as a scaffold defining the shape and mechanical properties of many tissues and organs including skin, tendon, artery walls, fibrocartilage, bone and teeth. Type 1 collagen is the must abundant protein in mammals. Collagens are synthesized with N-terminal and C-terminal propeptides that are cleaved during maturation and secretion. After cleavage of the propeptides, the most N-terminal and C-terminal remaining sequences are known as telopeptides. Mutations in the collagen 1, alpha 1 gene (COL1A1) are known to cause osteogenesis imperfecta (aka brittle bone disease) (Byers 1989). Furthermore, mutations found in the fist 90 residues of the helical region of alpha 1 collagen have been implicated in the prevention or delayed removal of the procollagen N-propeptide leading to a combined osteogenesis imperfecta and Ehlers-Danlos syndrome (EDS) phenotype (Cabral et al., 2005).
