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Epidermolysis bullosa simplex Dowling–Meara due to an arginine to cysteine substitution in exon 1 of keratin 14
Author(s) -
Premaratne Champi,
Klingberg Sandra,
Glass Ian,
Wright Kellie,
Murrell Dédée
Publication year - 2002
Publication title -
australasian journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.67
H-Index - 53
eISSN - 1440-0960
pISSN - 0004-8380
DOI - 10.1046/j.1440-0960.2002.00548.x
Subject(s) - epidermolysis bullosa simplex , keratin 6a , keratin 5 , keratin , keratin 14 , exon , epidermolysis bullosa , missense mutation , epidermolytic hyperkeratosis , mutation , microbiology and biotechnology , medicine , genetics , gene , biology , dermatology , intermediate filament , transgene , genetically modified mouse , cytoskeleton , cell
SUMMARY Epidermolysis bullosa simplex (EBS) is a blistering disorder affecting the basal layer of the epidermis usually inherited in an autosomal dominant fashion. Most cases are caused by mutations in the genes encoding keratin 5 (K5) and keratin 14 (K14) and are characterized by cytolysis within the basal layer of the epidermis. We report a patient manifesting the Dowling–Meara variant of EBS in whom we characterized a cytosine to thymine transition at codon 125 (R125C) in K14. This missense mutation is located at the amino terminus of the helical rod domain of the keratin 14 molecule, resulting in defective pairing with K5, thereby disrupting keratin tonofibril integrity.