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One gene but different proteins and diseases: the complexity of dystonin and bullous pemphigoid antigen 1
Author(s) -
Künzli Kseniia,
Favre Bertrand,
Chofflon Michel,
Borradori Luca
Publication year - 2016
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.12877
Subject(s) - gene isoform , bullous pemphigoid , gene , biology , exon , antigen , microbiology and biotechnology , genetics , antibody
Since the immunochemical identification of the bullous pemphigoid antigen 230 ( BP 230) as one of the major target autoantigens of bullous pemphigoid ( BP ) in 1981, our understanding of this protein has significantly increased. Cloning of its gene, development and characterization of animal models with engineered gene mutations or spontaneous mouse mutations have revealed an unexpected complexity of the gene encoding BP 230. The latter, now called dystonin ( DST ), is composed of at least 100 exons and gives rise to three major isoforms, an epithelial, a neuronal and a muscular isoform, named BPAG 1e (corresponding to the original BP 230), BPAG 1a and BPAG 1b, respectively. The various BPAG 1 isoforms play a key role in fundamental processes, such as cell adhesion, cytoskeleton organization, and cell migration. Genetic defects of BPAG 1 isoforms are the culprits of epidermolysis bullosa and complex, devastating neurological diseases. In this review, we summarize recent advances of our knowledge about several BPAG 1 isoforms, their role in various biological processes and in human diseases.