title: Cantharide acantholysis: endogenous protease activation leading to desmosomal plaque dissolution.
abstract: Using a method which allowed us to study the morphological consequences of the expression and the inhibition of proteases in living tissues, we demonstrated that the primary detectable cellular event in cantharide acantholysis is the dissolution of the dense plaque, leading to the detachment of tonofilaments from desmosomes. This process is inhibited by neutral serine protease inhibitors. This suggests that the desmosome-tonofilament complex, more precisely the desmosomal dense plaque, is the primary target of activated proteases during cantharide acantholysis, and can be disrupted by a specific epidermal protease-anti protease system. Cantharide acantholysis may be useful model for studying desmosomal turnover.
authors.affiliation: Laboratory of Dermatology, Hôpital Henri Mondor, Creteil, France.
authors.forename: B
authors.initials: B
authors.lastname: Bertaux
authors.forename: C
authors.initials: C
authors.lastname: Prost
authors.forename: M
authors.initials: M
authors.lastname: Heslan
authors.forename: L
authors.initials: L
authors.lastname: Dubertret
mesh_terms: D000051:Acantholysis / Q000139:chemically induced / Q000201:enzymology / Q000473:pathology*; D002193:Cantharidin; D002478:Cells, Cultured; D003896:Desmosomes / Q000648:ultrastructure; D006801:Humans; D007382:Intermediate Filaments / Q000648:ultrastructure; D010447:Peptide Hydrolases / Q000378:metabolism; D011480:Protease Inhibitors / Q000494:pharmacology; D012867:Skin / Q000648:ultrastructure*; D012871:Skin Diseases / Q000473:pathology*
chemical_list: D011480:Protease Inhibitors; D010447:Peptide Hydrolases; D002193:Cantharidin