Mutations in the 180–kD bullous pemphigoid antigen (BPAG2), a hemidesmosomal transmembrane collagen (COL17A1), in generalized atrophic benign epidermolysis bullosa

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Abstract
Junctional epidermolysis bullosa (JEB) is a heterogeneous autosomal recessively inherited blistering skin disorder associated with fragility at the dermal-epidermal junction1. Characteristic ultrastructural findings in JEB are abnormalities in the hemidesmosome-anchoring filament complexes1,2. These focal attachment structures, which extend from the intracellular compartment of the basal keratinocytes to the underlying basement membrane, have been shown to be hypoplastic or rudimentary in different forms of JEB2. Previously, in different JEB phenotypes, mutations have been found in the three genes for the anchoring filament component laminin5 (LAMA3, LAMBS, and LAMC2)3–6 and in the gene for the hemidesmosome-associated integrin β4 subunit7. Here, we describe the first mutations in the gene encoding the 180-kD bullous pemphigoid antigen (BPAG2), a transmembranous hemidesmosomal collagen, also known as type XVII collagen (COL17A1)8.The patient is affected with generalized atrophic benign epidermolysis bullosa (GABEB)9, a rare variant of JEB, and isacompound heterozygote for premature termination codons on both alleles. These novel findings emphasize the molecular heterogeneity of this group of genodermatoses, and attest to the importance of BPAG2 in maintaining adhesion between the epidermis and the dermis.

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