Cantharide acantholysis: endogenous protease activation leading to desmosomal plaque dissolution
B Bertaux, C Prost, M Heslan… - British Journal of …, 1988 - Wiley Online Library
B Bertaux, C Prost, M Heslan, L Dubertret
British Journal of Dermatology, 1988•Wiley Online Librarysummary 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 …
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 …
Summary
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 a useful model for studying desmosomal turnover.
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