Three unrelated individuals with perinatally lethal osteogenesis imperfecta resulting from identical glycine 502 serine substitutions in the α2 chain of type I collagen

In general, osteogenesis imperfecta is caused by heterozygous mutations in either of the genes encoding the alpha 1 or alpha 2 chains of type I collagen (COL1A1 and COL1A2, respectively). Usually, these mutations are unique to the affected individual or individuals within a family. In this study, single-strand conformation polymorphism mapping analysis has been coupled with sequence analysis to identify a single base mutation in the alpha 2(I) gene of type I collagen; this mutation is identical in three unrelated individuals with perinatal lethal osteogenesis imperfecta. The heterozygous G to A transition at a CpG dinucleotide results in a Gly502Ser substitution in the alpha 2 chain of type I collagen.

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