A Gly238Ser substitution in the alpha 2 chain of type I collagen results in osteogenesis imperfecta type III.
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Rose NJ, Mackay K, Byers PH, Dalgleish R
A Gly238Ser substitution in the alpha 2 chain of type I collagen results in osteogenesis imperfecta type III.
Hum Genet. 1995 Feb;95(2):215-8.
- PubMed ID
- 7860070 [ View in PubMed]
- Abstract
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.