Substitution of cysteine for glycine-946 in the alpha 1(I) chain of type I procollagen causes lethal osteogenesis imperfecta.
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Kurosaka D, Hattori S, Hori H, Yamaguchi N, Hasegawa T, Akimoto H, Nagai Y
Substitution of cysteine for glycine-946 in the alpha 1(I) chain of type I procollagen causes lethal osteogenesis imperfecta.
J Biochem. 1994 May;115(5):853-7.
- PubMed ID
- 7961597 [ View in PubMed]
- Abstract
Procollagen synthesized by skin fibroblasts from a patient with a lethal variant of osteogenesis imperfecta has been characterized. After pepsin digestion of the type I procollagen, a portion of the alpha 1(I) chains was recovered as a disulfide-bonded dimer. Cyanogen bromide peptide mapping suggested that a new cysteine residue was present in the alpha 1(I)CB6 fragment. Sequencing of cloned cDNAs prepared using mRNA from the proband's fibroblasts demonstrated that some of the clones contained a single base mutation that converted the glycine codon in amino acid position 946 of the alpha 1(I) chain to a cysteine codon. The thermal stability of the molecules was markedly lower than that in the case of the normal control.