A Gly238Ser substitution in the alpha 2 chain of type I collagen results in osteogenesis imperfecta type III.
In general, osteogenesis imperfecta (brittle bone disease) is caused by heterozygous mutations in the genes encoding the alpha 1 or alpha 2 chains of type I collagen (COL1A1 and COL1A2, respectively). In this study we screened these genes in a proband presenting with the severe form (type III) of osteogenesis imperfecta for mutations which might result in the phenotype. Single-strand conformation polymorphism mapping analysis was used to identify a region suspected of harbouring the mutation and subsequent sequence analysis revealed a heterozygous G to A transition in the alpha 2(I) gene of type I collagen in the individual. The resulting substitution of the glycine at position 238 of the alpha chain by serine is the most N-terminal yet reported for this chain.
Department of Genetics, University of Leicester, UK.
N J
NJ
Rose
K
K
Mackay
P H
PH
Byers
R
R
Dalgleish
D001483:Base Sequence; D002478:Cells, Cultured; D002675:Child, Preschool; D003094:Collagen / Q000235:genetics*; D005260:Female; D005998:Glycine / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D010013:Osteogenesis Imperfecta / Q000145:classification / Q000235:genetics*; D010641:Phenotype; D017354:Point Mutation; D016133:Polymerase Chain Reaction; D018807:Polymorphism, Single-Stranded Conformational; D012694:Serine / Q000235:genetics*
D012694:Serine; D003094:Collagen; D005998:Glycine