Premium
Heat shock protein 90: a pathophysiological factor and novel treatment target in autoimmune bullous skin diseases
Author(s) -
Tukaj Stefan,
Zillikens Detlef,
Kasperkiewicz Michael
Publication year - 2015
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.12760
Subject(s) - bullous pemphigoid , medicine , heat shock protein , immunology , autoimmunity , epidermolysis bullosa acquisita , autoimmune disease , pemphigus , pemphigus vulgaris , immune system , experimental autoimmune encephalomyelitis , rheumatoid arthritis , antibody , biology , biochemistry , gene
The chaperone heat shock protein 90 (Hsp90), a cell stress‐inducible molecule that regulates activity of many client proteins responsible for cellular growth, differentiation and apoptosis, has been proposed as an important therapeutic target in patients with malignancies. More recently, its active participation in (auto)immune processes has been recognized as evidenced by amelioration of inflammatory disease pathways through pharmacological inhibition of Hsp90 in rodent models of autoimmune encephalomyelitis, rheumatoid arthritis and systemic lupus erythematosus. Based on own current research results, this viewpoint essay provides important insights that Hsp90 is also involved as a notable pathophysiological factor in autoimmune blistering dermatoses including epidermolysis bullosa acquisita, bullous pemphigoid and possibly dermatitis herpetiformis. The observed in vitro , ex vivo and in vivo efficacy of anti‐Hsp90 treatment in experimental models of autoimmune bullous diseases and its underlying multimodal anti‐inflammatory mechanisms of interference with key contributors to autoimmune‐mediated blister formation supports the introduction of selective non‐toxic Hsp90 inhibitors into the clinical setting for the treatment of patients with these disorders.