title: Correlation of clinical and molecular biological abnormalities in osteogenesis imperfecta.
abstract: Substitution of a glycine residue in the triple helix of the alpha 1(I) chain by either arginine, valine or alanine was associated with the type II lethal perinatal osteogenesis imperfecta phenotype. This phenotype was also produced by a frameshift mutation that resulted in an abnormal amino acid sequence of the carboxy-terminal propeptide of the pro-alpha 1(I) chain. The latter baby, however, showed some clinical and radiographic differences from the other babies with type II OI. The severity of the clinical and radiographic phenotypes are likely to be determined by both the type and site of the mutation as well as by the intra-uterine environment.
authors.affiliation: Department of Paediatrics, University of Melbourne, Victoria, Australia.
authors.forename: W
authors.initials: W
authors.lastname: Cole
authors.forename: D
authors.initials: D
authors.lastname: Chan
authors.forename: S
authors.initials: S
authors.lastname: Lamande
authors.forename: T
authors.initials: T
authors.lastname: Mascara
authors.forename: J
authors.initials: J
authors.lastname: Rogers
authors.forename: J
authors.initials: J
authors.lastname: Bateman
mesh_terms: D000409:Alanine / Q000235:genetics; D001120:Arginine / Q000235:genetics; D005838:Genotype; D005998:Glycine / Q000235:genetics; D006801:Humans; D007223:Infant; D009154:Mutation; D010013:Osteogenesis Imperfecta / Q000145:classification / Q000235:genetics*; D010641:Phenotype; D014633:Valine / Q000235:genetics
chemical_list: D001120:Arginine; D014633:Valine; D000409:Alanine; D005998:Glycine