Novel amino acid substitution in the Y-position of collagen type II causes spondyloepimetaphyseal dysplasia congenita.
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Sulko J, Czarny-Ratajczak M, Wozniak A, Latos-Bielenska A, Kozlowski K
Novel amino acid substitution in the Y-position of collagen type II causes spondyloepimetaphyseal dysplasia congenita.
Am J Med Genet A. 2005 Sep 1;137A(3):292-7.
- PubMed ID
- 16088915 [ View in PubMed]
- Abstract
We report on monozygotic twins with short stature and severe spondyloepimetaphyseal dysplasia congenita (SEMDC) from the Polish population. Phenotype of the twin girls resembles spondyloepiphyseal dysplasia congenita Spranger-Wiedemann (SEDC-SW), but shortening of the stature is more severe and the cranioface is normal. The distinctive radiographic features, in spite of similarity to SEDC-SW, indicate different spinal and, notably, severe metaphyseal involvement. Molecular analysis of the COL2A1 gene revealed an A to G transition at nucleotide +79 of exon 41 that converted the codon for arginine at amino acid 792 to a codon for glycine (Arg792Gly). The twins were heterozygous for the mutation and neither parent had this change. The Arg792Gly substitution is located at the Y-position of Gly-X-Y triplet, and it is likely that this substitution decreased the thermal stability of the triple helix and may affect fibril growth by replacement of an arginine residue, which is important for a conformation of the triple helix.