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Structural proteins of the dermal‐epidermal junction targeted by autoantibodies in pemphigoid diseases
Author(s) -
Goletz Stephanie,
Zillikens Detlef,
Schmidt Enno
Publication year - 2017
Publication title -
experimental dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.108
H-Index - 96
eISSN - 1600-0625
pISSN - 0906-6705
DOI - 10.1111/exd.13446
Subject(s) - plectin , anchoring fibrils , microbiology and biotechnology , integrin , transmembrane protein , basement membrane , laminin , intermediate filament , chemistry , hemidesmosome , cell adhesion , biology , extracellular matrix , cytoskeleton , cell , receptor , biochemistry
The dermal‐epidermal junction consists of a network of several interacting structural proteins that strengthen adhesion and mediate signalling events. This structural network consists of hemidesmosomal‐anchoring filament complexes connecting the basal keratinocytes to the basement membrane. The anchoring filaments in turn interact with the anchoring fibrils to attach the basement membrane to the underlying dermis. Several of these structural proteins are recognized by autoantibodies in pemphigoid diseases, a heterogeneous group of clinically and immunopathologically diverse entities. Targeted proteins include the two intracellular plakins, plectin isoform 1a and BP 230 (also called bullous pemphigoid antigen ( BPAG ) 1 isoform e ( BPAG 1e)). Plectin 1a and BP230 are connected to the intermediate filaments and to the cell surface receptor α6β4 integrin, which in turn is connected to laminin 332, a component of the anchoring filaments. Further essential adhesion proteins are BP 180, a transmembrane protein, laminin γ1 and type VII collagen. Latter protein is the major constituent of the anchoring fibrils. Mutations in the corresponding genes of these adhesion molecules lead to inherited epidermolysis bullosa emphasizing the importance of these proteins for the integrity of the dermal‐epidermal junction. This review will provide an overview on the structure and function of the proteins situated in the dermal‐epidermal junction targeted by autoantibodies.