Mutations in the COL1A1 and COL1A2 genes, encoding the proalpha1 and 2 chains of type I collagen, cause osteogenesis imperfecta (OI) or Ehlers-Danlos syndrome (EDS) arthrochalasis type. Although the majority of missense mutations in the collagen type I triple helix affect glycine residues in the Gly
A novel arginine-to-cysteine substitution in the triple helical region of the α1(I) collagen chain in a family with an osteogenesis imperfecta/Ehlers–Danlos phenotype
✍ Scribed by AM Lund; F Joensen; E Christensen; M Dunø; F Skovby; M Schwartz
- Book ID
- 110888520
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 167 KB
- Volume
- 73
- Category
- Article
- ISSN
- 0009-9163
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## Clinical Data on Patients KO was 35 years of age at the time her cell strain was sent to us. She was born to healthy unrelated parents and has two healthy siblings, both of whom have unaffected children, and no other individuals with 0 1 were identified in the family. She had many fractures at
A substitution of arginine for glycine at amino acid position 154 of the al(1) collagen chain was found in a father and his three children. The phenotype of the patients includes manifestations of types I and IIUIV osteogenesis imperfecta, but appears to be milder than that of the previously describ