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epidermolysis bullosa/protease
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Increased neutral protease and collagenase activity in recessive dystrophic epidermolysis bullosa.
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The enzyme activities of normal-looking skin and blister fluid from a patient with recessive dystrophic epidermolysis bullosa (RDEB) were measured. Of the hydrolytic enzymes measured, both collagenase and neutral protease activities were considerably increased in the skin and blister fluid samples
Generalized dominant epidermolysis bullosa simplex: decreased activity of a gelatinolytic protease in cultured fibroblasts as a phenotypic marker.
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To characterize biochemical traits associated with various forms of epidermolysis bullosa (EB), we used skin fibroblast cultures to measure a gelatin-specific neutral metalloprotease. Compared to normal cultures, levels of this gelatinase were 7-fold decreased in cell cultures from 3 patients from 3
Proteases are responsible for blister formation in recessive dystrophic epidermolysis bullosa and epidermolysis bullosa simplex.
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The specific factors which induce blister formation in recessive dystrophic epidermolysis bullosa (RDEB) and epidermolysis bullosa simplex (EBS) were studied by culturing normal human skin with blister fluid from patients with RDEB and EBS. When skin from a healthy person was cultured with RDEB
Protease inhibitor therapy for recessive dystrophic epidermolysis bullosa. In vitro effect and clinical trial with camostat mesylate.
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Recently we reported that a kind of serine protease, SH protease, and collagenase might be involved in blister formation and, furthermore, that the cooperative action of these three proteases was essential for blister formation in recessive dystrophic epidermolysis bullosa. In this study we examined
[Proteases--inhibitor potential in epidermolysis bullosa hereditaria].
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Tumour serine proteases C1r and C1s as novel biomarkers and therapeutic targets in invasive sporadic and recessive dystrophic epidermolysis bullosa-associated cutaneous squamous cell carcinoma.
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[Epidermolysis bullosa acquisita].
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Epidermolysis bullosa acquisita (EBA) is a rare acquired subepidermal bullous autoimmune dermatosis, associated with autoantibodies against collagen type VII, the most important component of dermal anchoring fibrils. Blister induction occurs after binding of autoantibodies to collagen type VII,
The recombinant expression of full-length type VII collagen and characterization of molecular mechanisms underlying dystrophic epidermolysis bullosa.
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Type VII collagen is a major component of anchoring fibrils, attachment structures that mediate dermal-epidermal adherence in human skin. Dystrophic epidermolysis bullosa (DEB) is an inherited mechano-bullous disorder caused by mutations in the type VII collagen gene and perturbations in anchoring
Epidermolysis bullosa acquisita antigen: relationship between the collagenase-sensitive and -insensitive domains.
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To clarify the relationship of the 290 and 145 kDa chains of the epidermolysis bullosa acquisita (EBA) antigen, we subjected urea extracts of skin basement membrane zone (BMZ) proteins and isolated 290 and 145 kDa chains of the EBA antigen cut out of sodium dodecyl sulfate polyacrylamide gels to
Development and characterization of a recombinant truncated type VII collagen "minigene". Implication for gene therapy of dystrophic epidermolysis bullosa.
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Dystrophic epidermolysis bullosa (DEB) is an inherited mechano-bullous disorder of skin caused by mutations in the type VII collagen gene. The lack of therapy for DEB provides an impetus to develop gene therapy strategies. However, the full-length 9-kilobase type VII collagen cDNA exceeds the
Blister fluid from epidermolysis bullosa letalis induces dermal-epidermal separation in vitro.
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Normal human skin was cultured with blister fluid (BF) from 2 patients with epidermolysis bullosa letalis (EB letalis). After 12-24 h incubation, initial separation was observed at the dermal-epidermal junction. Complete separation was seen after 48-72 h incubation. Epidermal and dermal structures
Origin and properties of the blister formation factor in blister fluids from recessive dystrophic epidermolysis bullosa.
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The origin and properties of the blister formation factor in recessive dystrophic epidermolysis bullosa (RDEB) blister fluids were investigated. Organ cultures of normal human skin incubated with RDEB dermis extract or with RDEB fibroblast culture medium (FCM) produced a clear subepidermal blister
Characterization of molecular mechanisms underlying mutations in dystrophic epidermolysis bullosa using site-directed mutagenesis.
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Type VII collagen (C7) is a major component of anchoring fibrils, structures that mediate epidermal-dermal adherence. Mutations in gene COL7A1 encoding for C7 cause dystrophic epidermolysis bullosa (DEB), a genetic mechano-bullous disease. The biological consequences of specific COL7A1 mutations and
Granulocyte-derived elastase and gelatinase B are required for dermal-epidermal separation induced by autoantibodies from patients with epidermolysis bullosa acquisita and bullous pemphigoid.
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Epidermolysis bullosa acquisita (EBA) and bullous pemphigoid (BP) are two clinically and immunologically distinct autoimmune subepidermal blistering skin diseases associated with IgG autoantibodies against the dermal-epidermal junction. BP antibodies are directed against the hemidesmosomal antigens
A type VII collagen subdomain mutant is thermolabile and shows enhanced proteolytic degradability - Implications for the pathogenesis of recessive dystrophic epidermolysis bullosa?
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Type VII collagen is the major constituent of anchoring fibrils. It has a central collagenous domain that is surrounded by a small C-terminal non-collagenous domain (NC2) and a large N-terminal non-collagenous (NC1) domain. Mutations in type VII collagen can lead to hereditary skin blistering
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