acantholysis/protease

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Cantharide acantholysis: endogenous protease activation leading to desmosomal plaque dissolution.

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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

Protease inhibitors prevent plasminogen-mediated, but not pemphigus vulgaris-induced, acantholysis in human epidermis.

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Pemphigus is an autoimmune blistering disease of the skin and mucous membranes. It is caused by autoantibodies directed against desmosomes, which are the principal adhesion structures between epidermal keratinocytes. Binding of autoantibodies leads to the destruction of desmosomes resulting in the

Effects of steroid, retinoid, and protease inhibitors on the formation of acantholysis induced in organ culture of skins from patients with benign familial chronic pemphigus.

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Skin explants from two lesional areas and four normal-appearing areas of four patients with benign familial chronic pemphigus (BFCP) were organ cultured with and without various reagents. After 24-h culturing of involved skin with medium only, dissociation of keratinocytes, which was also observed

Cantharidin-induced acantholysis: adhesion molecules, proteases, and related proteins.

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Acantholysis is a feature of disorders such as Hailey-Hailey disease and Darier's disease. Immunocytochemical studies have shown internalization of desmosomal components after acantholysis. Basal cytokeratins show suprabasal expression in lesional Darier's disease. The exact mechanisms of

Cantharidin-induced acantholysis in Darier's disease: does acantholysis initiate dyskeratosis?

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We have examined the action of cantharidin on the skin of patients with Darier's disease, and used immunohistological techniques to determine the distribution of desmosomal components, keratin intermediate filaments, and proteases in cantharidin-induced blisters. Cantharidin induced acantholysis,

Appearance of "pemphigus acantholysis factor" in human skin cultured with pemphigus antibody.

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These studies deal with the mechanism of pemphigus IgG-induced epidermal acantholysis. When normal human skin was culted with defined medium containing IgG from pemphigus serum, extensive epidermal acantholysis developed and heat-labile proteolytic enzyme(s) were recovered in the culture medium. The

Plasmin induces acantholysis in skin organ cultures.

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Addition of human plasminogen to three different pemphigus plasma samples showed a synergistic effect on acantholysis in the skin organ culture model. Human plasmin itself, without addition of pemphigus plasma, induced typical acantholytic changes in the skin explants, causing different types of

Urokinase plasminogen activator mRNA is induced by IL-1alpha and TNF-alpha in in vitro acantholysis.

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The role of urokinase type plasminogen activator (uPA) has been well documented in the pathogenesis of pemphigus vulgaris (PV). Activation of plasminogen into active serine protease plasmin initiates extracellular proteolysis leading to acantholysis but the mechanisms underlying this process are not

How does acantholysis occur in pemphigus vulgaris: a critical review.

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BACKGROUND Pemphigus vulgaris is a life-threatening autoimmune blistering disease targeting skin and mucous membranes, characterized by disruption of keratinocytes' adhesion termed acantholysis. Today multiple classes of targets are considered to play a role in the genesis of the acantholysis; of

Eosinophilic esophagitis-linked calpain 14 is an IL-13-induced protease that mediates esophageal epithelial barrier impairment.

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We recently identified a genome-wide genetic association of eosinophilic esophagitis (EoE) at 2p23 spanning the calpain 14 (CAPN14) gene, yet the causal mechanism has not been elucidated. We now show that recombinant CAPN14 cleaves a calpain-specific substrate and is inhibited by 4 classical calpain

Targeted disruption of the pemphigus vulgaris antigen (desmoglein 3) gene in mice causes loss of keratinocyte cell adhesion with a phenotype similar to pemphigus vulgaris.

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In patients with pemphigus vulgaris (PV), autoantibodies against desmoglein 3 (Dsg3) cause loss of cell-cell adhesion of keratinocytes in the basal and immediate suprabasal layers of stratified squamous epithelia. The pathology, at least partially, may depend on protease release from keratinocytes,

[Pathogenetic mechanisms in autoimmune diseases].

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In addition to an earlier review [Z. ges. inn. Med. 35 (1980) 58] newer concepts in the pathogenesis of autoimmune diseases are presented. Acantholysis in pemphigus is caused by proteases released from cells of stratified squamous epithelium stimulated by antibodies to cell membrane antigens. The

Pemphigus can be induced by topical phenol as well as by foods and drugs that contain phenols or thiols.

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Pemphigus is an autoimmune disease that results from the interaction between predisposing genetic factors and exogenous factors, the most common environmental factors being drugs and food. Topical phenol has induced pemphigus in one patient. Drugs and foods that induce pemphigus are divided into

A possible mechanism for phenol-induced pemphigus.

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A possible mechanism for phenol-induced pemphigus lesions in genetically predisposed individuals is proposed that accounts for in vitro observations and cases of biochemical acantholysis, as well as the in vivo acantholysis in pemphigus induced by phenols. The mechanism involves the induction of

Paederus fuscipes dermatitis. A histopathological study.

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Paederus fuscipes (PF) dermatitis is a self-healing blistering disorder of the skin caused by a small insect belonging to genus Paederus, family Staphylinidae, order Coleoptera. Crushing PF on the skin causes acute dermatitis within 24 hours, corresponding in shape and dimensions to the area

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