granulomatosis with polyangiitis/protease

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Platelets are activated in ANCA-associated vasculitis via thrombin-PARs pathway and can activate the alternative complement pathway.

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BACKGROUND In this study, we investigated the mechanism of platelet activation in patients with antineutrophil cytoplasmic antibody (ANCA)-associated vasculitis (AAV), as well as the activation of the alternative complement pathway by platelets in AAV. METHODS CD62P and platelet-leukocyte aggregates

The Diagnostic Value of Alpha-1-Antitrypsin Phenotype in Patients with Granulomatosis with Polyangiitis.

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The deficiency of alpha-1 protease inhibitor, or alpha-1-antitrypsin (A1AT), predisposes to chronic lung diseases and extrapulmonary pathology. Besides classical manifestations, such as pulmonary emphysema and liver disease, alpha-1-antitrypsin deficiency (A1ATD) is also known to be associated with

Induction of proteinase 3-anti-neutrophil cytoplasmic autoantibodies by proteinase 3-homologous bacterial protease in mice.

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Proteinase 3 (PR3) is the principal target of antineutrophil cytoplasmic autoantibodies (ANCA) associated with granulomatosis with polyangiitis. The aim of this study was to investigate whether bacterial PR3-homologous protease can induce autoantibodies to PR3 and ANCA-associated pathology in mice.

Neutrophil-related and serum biomarkers in granulomatosis with polyangiitis support extracellular traps mechanism of the disease.

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OBJECTIVE Granulomatosis with polyangiitis (GPA) is an autoimmune disease with still unknown etiology. Recent studies indicate that neutrophils extra-cellular traps participate in the pathophysiology of GPA. This study investigates the levels of circulating NET formation markers and

A hydrophobic patch on proteinase 3, the target of autoantibodies in Wegener granulomatosis, mediates membrane binding via NB1 receptors.

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Proteinase 3 (PR3), the target antigen of antineutrophil cytoplasm autoantibodies, which are found in patients with Wegener granulomatosis, is a neutrophil serine protease localized within cytoplasmic granules. Recently, the human neutrophil antigen NB1 was identified as a specific neutrophil cell

Antineutrophil cytoplasmic antibodies (ANCA) and systemic vasculitis: update of assays, immunopathogenesis, controversies, and report of a novel de novo ANCA-associated vasculitis after kidney transplantation.

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OBJECTIVE To characterize antineutrophil cytoplasmic antibodies (ANCA), their major autoantigens, disease associations, and pathophysiology in systemic vasculitides. To describe a patient with a novel de novo ANCA-associated vasculitis after kidney transplantation. METHODS We reviewed and compiled

No association of G-463A myeloperoxidase gene polymorphism with MPO-ANCA-associated vasculitis.

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BACKGROUND The activation of neutrophils and monocytes by ANCA, resulting in the release of reactive oxygen species and proteases like myeloperoxidase (MPO), is essential to the pathogenesis of ANCA-associated vasculitis. As the A allele of the G-463A MPO gene polymorphism is associated with

Mechanisms and markers of vascular damage in ANCA-associated vasculitis.

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Much progress has been made in understanding the pathogenesis of anti-neutrophil cytoplasmic antibodies (ANCA)-associated small-vessel vasculitis and interaction between ANCA and micro-vascular endothelial cells are centre stage. The interactions of these key players culminate in respiratory burst

Concomitant thrombotic thrombocytopenic purpura and ANCA-associated vasculitis in an adolescent.

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Thrombotic thrombocytopenic purpura (TTP) rarely occurs with systemic vasculitis. A 17-year-old girl presented with non-bloody diarrhea, menorrhagia, and syncope. She had severe anemia (hemoglobin = 3.8 g/dl), thrombocytopenia (platelet = 7,000/mm(3)), and acute kidney injury (serum creatinine, Cr =

Lack of association of alpha-1 antichymotrypsin gene polymorphism with PR3-ANCA and MPO-ANCA associated vasculitis.

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In patients with PR3-ANCA associated vasculitides the carrier frequency of alpha1-antitrypsin (AAT) deficiency allele PI*Z is increased and linkage disequilibrium between polymorphic markers within a cluster of serine protease inhibitor (serpin) genes, including AAT gene, at chromosome 14q32.1 has

Toll-like receptor TLR2 and TLR9 ligation triggers neutrophil activation in granulomatosis with polyangiitis.

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OBJECTIVE The aim of the study was to characterize the expression of TLR2, TLR4 and TLR9 in PMNs of patients with granulomatosis with polyangiitis (GPA) and to elucidate the role of these receptors in GPA with respect to neutrophil activation. METHODS The expression of TLR2, TLR4 and TLR9 was

Treatment of granulomatosis with polyangiitis (Wegener's).

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Granulomatosis with polyangiitis is a systemic necrotizing vasculitis characterized by granulomatous inflammation of small vessels and is associated with autoantibodies to neutrophil cytoplasmic proteases, mainly proteinase 3. Potentially lethal if not promptly diagnosed and treated, most patients

Neutrophil proteinase 3 and dipeptidyl peptidase I (cathepsin C) as pharmacological targets in granulomatosis with polyangiitis (Wegener granulomatosis).

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Neutrophils are among the first cells implicated in acute inflammation. Leaving the blood circulation, they quickly migrate through the interstitial space of tissues and liberate oxidants and other antimicrobial proteins together with serine proteinases. Neutrophil elastase, cathepsin G, proteinase

Concomitant Granulomatosis with Polyangiitis and C3 Glomerulonephritis Causing Renal Failure.

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A 75-year-old male with no prior history of vasculitis or renal deficiency presented with a history of 36 hours of anterior epistaxis, one month of worsening shortness of breath, severe anemia requiring transfusion, thrombocytopenia, coagulopathy with INR 4.9, and renal failure requiring

Proteinase 3, protease-activated receptor-2 and interleukin-32: linking innate and autoimmunity in Wegener's granulomatosis.

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Proteinase 3 (PR3) is a multifunctional neutrophil-derived serine protease influencing cell cycle, differentiation, and cell death. This molecule is the main target antigen of autoantibodies in Wegener's granulomatosis (WG) known as antineutrophil cytoplasmic antibodies (PR3-ANCA). WG usually starts

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