Compositional analysis of collagen from patients with diverse forms of osteogenesis imperfecta.
Collagen was extracted by pepsin treatment from various tissues and skin fibroblasts of 23 patients belonging to different types of osteogenesis imperfecta (OI), and characterized by molecular sieve and ion exchange chromatography, gel electrophoresis, and amino acid analysis. We found an elevated collagen III/I ratio in the skin of one patient with OI type I but almost normal values in skin fibroblasts of two other patients of this OI type. Five patients with OI type II had a normal collagen III/I ratio in their skin and skin fibroblasts, but the degree of hydroxylation of lysine residues in collagen I and III from their skin, bone, calvarium, and noncalcified calvarial tissue was increased. Patients belonging to OI types II, III, and IV had also considerable amounts of collagen III in their long bones, while bone tissue from controls contained only type I collagen. The content of type V in calcified tissues was virtually the same in controls and patients.
D000293:Adolescent; D000328:Adult; D002648:Child; D002675:Child, Preschool; D003094:Collagen / Q000378:metabolism*; D005347:Fibroblasts / Q000378:metabolism; D006801:Humans; D006901:Hydroxylysine / Q000378:metabolism; D007231:Infant, Newborn; D008239:Lysine / Q000378:metabolism; D010013:Osteogenesis Imperfecta / Q000378:metabolism*; D012867:Skin / Q000378:metabolism
D006901:Hydroxylysine; D003094:Collagen; D008239:Lysine