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<p>Pemphigus vulgaris (PV) is a life-threatening autoimmune blistering disease caused by circulating autoantibodies against desmoglein (Dsg) 1 and Dsg 3. Whether acantholysis in PV results exclusively from antibody binding to Dsgs or involves additional factors remains controversial. Given that Fas-Ligand (FasL), an activator of apoptotic caspase-8, is increased in the serum and the skin of patients with PV, we investigated the role of caspases in anti-Dsg3-mediated acantholysis using both ex vivo and in vitro models. Our results demonstrated that anti-Dsg3 antibodies induced acantholysis ex vivo in the absence of caspase activation, primarily through the redistribution of Dsg3 to intracellular compartments. FasL-induced caspase activation led to a synergistic amplification of anti-Dsg3-mediated loss of cell adhesion by promoting Dsg3 cleavage. This dual mechanism provides new insights into the disease heterogeneity of PV.</p><p></p>

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Caspase-activation powers anti-Desmoglein 3-induced acantholysis in human epidermis

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年2月19日

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  • Morna F. Schmidt,
  • Maria A. Feoktistova,
  • Diana Panayotova-Dimitrova,
  • Eva Miriam Buhl,
  • Peter Boor,
  • Tim Ruhl,
  • Jens Waschke,
  • Ritva Tikkanen,
  • Martin Röcken,
  • Jens M. Baron,
  • Amir S. Yazdi

摘要

Pemphigus vulgaris (PV) is a life-threatening autoimmune blistering disease caused by circulating autoantibodies against desmoglein (Dsg) 1 and Dsg 3. Whether acantholysis in PV results exclusively from antibody binding to Dsgs or involves additional factors remains controversial. Given that Fas-Ligand (FasL), an activator of apoptotic caspase-8, is increased in the serum and the skin of patients with PV, we investigated the role of caspases in anti-Dsg3-mediated acantholysis using both ex vivo and in vitro models. Our results demonstrated that anti-Dsg3 antibodies induced acantholysis ex vivo in the absence of caspase activation, primarily through the redistribution of Dsg3 to intracellular compartments. FasL-induced caspase activation led to a synergistic amplification of anti-Dsg3-mediated loss of cell adhesion by promoting Dsg3 cleavage. This dual mechanism provides new insights into the disease heterogeneity of PV.