Advanced search
1 file | 267.22 KB

Glycine to tryptophan substitution in type I collagen in a patient with OI type III: a unique collagen mutation.

(2000) JOURNAL OF MEDICAL GENETICS. 37(5). p.371-375
Author
Organization
Abstract
We report a unique glycine substitution in type I collagen and highlight the clinical and biochemical consequences. The proband is a 9 year old Turkish boy with severely deforming osteogenesis imperfecta (OI). Biochemical analysis of (pro) collagen type I from a skin fibroblast culture showed both normal and over-modified alpha chains. Molecular analysis showed a G>T transversion in the COL1A2 gene, resulting in the substitution of glycine by tryptophan at position 277 of the alpha 2(I) collagen chain. Glycine substitutions in type I collagen are the most frequent cause of the severe and lethal forms of OI. The phenotypic severity varies according to the nature and localisation of the mutation. Substitutions of glycine by tryptophan, which is the most voluminous amino acid, have not yet been identified in type I collagen or any other fibrillar collagen. The severe, though nonlethal Or phenotype associated with this mutation may appear surprising in view of the huge size of the tryptophan residue. The fact that the mutation resides within a so called "non-lethal" region of the alpha 2(I) collagen chain supports a regional model in phenotypic severity for alpha 2(I) collagen mutations, in which the phenotype is determined primarily by the nature of the collagen domain rather than the type of glycine substitution involved.

Downloads

  • J Med Genet-2000-Nuytinck-371-5.pdf
    • full text
    • |
    • open access
    • |
    • PDF
    • |
    • 267.22 KB

Citation

Please use this url to cite or link to this publication:

Chicago
Nuytinck, Lieve, T TUKEL, H KAYSERILI, MY APAK, and Anne De Paepe. 2000. “Glycine to Tryptophan Substitution in Type I Collagen in a Patient with OI Type III: a Unique Collagen Mutation.” Journal of Medical Genetics 37 (5): 371–375.
APA
Nuytinck, Lieve, TUKEL, T., KAYSERILI, H., APAK, M., & De Paepe, A. (2000). Glycine to tryptophan substitution in type I collagen in a patient with OI type III: a unique collagen mutation. JOURNAL OF MEDICAL GENETICS, 37(5), 371–375.
Vancouver
1.
Nuytinck L, TUKEL T, KAYSERILI H, APAK M, De Paepe A. Glycine to tryptophan substitution in type I collagen in a patient with OI type III: a unique collagen mutation. JOURNAL OF MEDICAL GENETICS. 2000;37(5):371–5.
MLA
Nuytinck, Lieve et al. “Glycine to Tryptophan Substitution in Type I Collagen in a Patient with OI Type III: a Unique Collagen Mutation.” JOURNAL OF MEDICAL GENETICS 37.5 (2000): 371–375. Print.
@article{126974,
  abstract     = {We report a unique glycine substitution in type I collagen and highlight the clinical and biochemical consequences. The proband is a 9 year old Turkish boy with severely deforming osteogenesis imperfecta (OI). Biochemical analysis of (pro) collagen type I from a skin fibroblast culture showed both normal and over-modified alpha chains. Molecular analysis showed a G>T transversion in the COL1A2 gene, resulting in the substitution of glycine by tryptophan at position 277 of the alpha 2(I) collagen chain. Glycine substitutions in type I collagen are the most frequent cause of the severe and lethal forms of OI. The phenotypic severity varies according to the nature and localisation of the mutation. Substitutions of glycine by tryptophan, which is the most voluminous amino acid, have not yet been identified in type I collagen or any other fibrillar collagen. The severe, though nonlethal Or phenotype associated with this mutation may appear surprising in view of the huge size of the tryptophan residue. The fact that the mutation resides within a so called "non-lethal" region of the alpha 2(I) collagen chain supports a regional model in phenotypic severity for alpha 2(I) collagen mutations, in which the phenotype is determined primarily by the nature of the collagen domain rather than the type of glycine substitution involved.},
  author       = {Nuytinck, Lieve and TUKEL, T and KAYSERILI, H and APAK, MY and De Paepe, Anne},
  issn         = {0022-2593},
  journal      = {JOURNAL OF MEDICAL GENETICS},
  language     = {eng},
  number       = {5},
  pages        = {371--375},
  title        = {Glycine to tryptophan substitution in type I collagen in a patient with OI type III: a unique collagen mutation.},
  url          = {http://dx.doi.org/10.1136/jmg.37.5.371},
  volume       = {37},
  year         = {2000},
}

Altmetric
View in Altmetric
Web of Science
Times cited: