IDENTIFICATION OF THE GLYCINE-TO-ARGININE SUBSTITUTION G2043R IN TYPE-VII COLLAGEN IN A FAMILY WITH DOMINANT DYSTROPHIC EPIDERMOLYSIS-BULLOSA FROM HUNGARY
Pb. Cserhalmifriedman et al., IDENTIFICATION OF THE GLYCINE-TO-ARGININE SUBSTITUTION G2043R IN TYPE-VII COLLAGEN IN A FAMILY WITH DOMINANT DYSTROPHIC EPIDERMOLYSIS-BULLOSA FROM HUNGARY, Experimental dermatology, 6(6), 1997, pp. 303-307
Epidermolysis bullosa (EB) represents a group of genodermatoses charac
terized by fragility and easy blistering of the skin. In the dystrophi
c forms of EB (DEB), blisters occur below the basement membrane, at th
e level of the anchoring fibrils. In the dominantly inherited forms (D
DEB), the predominant type of mutation detected thus far is the substi
tution of a glycine residue which occurs within the collagenous domain
of the molecule characterized by the repeating Gly-X-Y amino acid seq
uence. In this study, we searched for mutations in DDEB in a family fr
om Hungary, by PCR amplification of segments of COL7A1, followed by he
teroduplex analysis. Examination of the PCR fragment corresponding to
exon 73 revealed a heteroduplex in affected individuals from the famil
y. Sequence analysis revealed a G-to-A transition at nucleotide 6127 i
n the triple-helical domain of COL7A1, which converted a glycine resid
ue at amino acid position 2043 to an arginine. This report represents
the second incidence of this mutation, G2043R, described first in a fa
mily with DDEB from Italy.