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A new glycine substitution mutation in the COL7A1 gene in a Chinese family with dominant dystrophic epidermolysis bullosa
Author(s) -
Zhang X. J.,
Song Y. X.,
Zhang X. Q.,
Yang S.,
Li M.,
Li C. R.,
Yang C. J.,
Yang J.
Publication year - 2003
Publication title -
clinical and experimental dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.587
H-Index - 78
eISSN - 1365-2230
pISSN - 0307-6938
DOI - 10.1046/j.1365-2230.2003.01317.x
Subject(s) - genetics , mutation , anchoring fibrils , exon , glycine , biology , transition (genetics) , substitution (logic) , point mutation , allele , arginine , microbiology and biotechnology , gene , amino acid , anatomy , ultrastructure , computer science , programming language
Summary Dystrophic epidermolysis bullosa (DEB) is caused by mutations in the COL7A1 gene encoding type VII collagen, the major component of anchoring fibrils. The characteristic genetic lesion in dominant DEB (DDEB) is a glycine substitution in the collagenous domain of the protein. In this study, we identified a Chinese family with a four‐generation pedigree of DDEB, in whom a novel glycine substitution mutation in COL7A1 was demonstrated. A heterozygous nucleotide G→A transition at position 6208 in exon 74 of COL7A1 was detected, which resulted in a glycine to arginine substitution (G2070R) in the triple‐helical domain of type VII collagen. This substitution was not found in 110 unrelated normal alleles. This report emphasizes the predominance of glycine substitution mutations in DDEB and contributes to the expanding database on COL7A1 mutations.