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Recurrent mutations in the COL1A2 gene in patients with osteogenesis imperfecta
Author(s) -
Trummer T,
Brenner R,
Just W,
Vogel W,
Kennerknecht I
Publication year - 2001
Publication title -
clinical genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 102
eISSN - 1399-0004
pISSN - 0009-9163
DOI - 10.1034/j.1399-0004.2001.590507.x
Subject(s) - transversion , osteogenesis imperfecta , serine , point mutation , genetics , mutation , gene , cysteine , substitution (logic) , amino acid substitution , amino acid , biology , medicine , chemistry , biochemistry , anatomy , phosphorylation , computer science , programming language , enzyme
A new recurrent point mutation in the COL1A2 gene was found in a patient with type III osteogenesis imperfecta (OI). A G‐to‐T transversion in nucleotide position 1121 leads to an amino acid substitution Gly238Cys. This is the first report on the most N‐terminal cysteine substitution in COL1A2 reported so far. Until now, at this position, only serine substitutions were observed five times in unrelated patients showing a highly variable expression of OI. It is obvious that endogenic and/or exogenic modifiers are involved in this classical autosomal dominant (or rarely recessive) mendelian disorder. An apparent preferential substitution by cysteine and serine residues is discussed with reference to post‐transcriptional or post‐translational collagen assembly control.