Results 311 to 320 of about 357,202 (334)
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Membrane proteinase 3 and Wegener’s granulomatosis

Clinical Nephrology, 2005
Proteinase 3 (PR3) is found in neutrophil and monocyte lysosomal granules. Anti-neutrophil cytoplasmatic antibodies (ANCA) with specificity for PR3 are characteristic for patients with Wegener's granulomatosis. The interaction of ANCA with neutrophilic ANCA antigens is necessary for the development of ANCA-associated diseases.
Ralph Kettritz   +5 more
openaire   +3 more sources

Elafin is a potent inhibitor of proteinase 3

Biochemical and Biophysical Research Communications, 1991
Elafin, a human skin derived inhibitor of human leukocyte elastase, was tested for inhibitory activity against proteinase 3, an elastin degrading proteinase of neutrophils. The inhibitory activity of elafin was compared with antileukoprotease and eglin C. Elafin proved to be a potent inhibitor of elastin-FITC degradation showing an IC 50 of 9.5 x 10(-9)
Oliver Wiedow   +2 more
openaire   +3 more sources

Proteinase-3 as a biomarker of exacerbations in bronchiectasis

Respiratory infections, 2020
Introduction: Proteinase 3 (PR3) is a serine protease stored in the primary granules of neutrophils and similar in structure to neutrophil elastase (NE). We sought to investigate the role of PR3 in exacerbations of bronchiectasis. Methods: PR3 activity in sputum supernatant was measured using a proteaseTag immunoassay in 86 individuals in stable state
Yong Hua Gao   +7 more
openaire   +2 more sources

Distribution of the granulocyte serine proteinases proteinase 3 and elastase in human glomerulonephritis

American Journal of Kidney Diseases, 1995
The serine proteinases proteinase 3 (PR3) and elastase are target antigens of antineutrophil cytoplasmic autoantibodies (ANCAs), which are found in various systemic vasculitides with rapidly progressive glomerulonephritis (RPGN). The expression of both proteinases was studied immunohistologically (avidin-biotin complex method) with murine monoclonal ...
Wolfgang L. Gross   +17 more
openaire   +3 more sources

Immune Functions of Proteinase 3

Critical Reviews in Immunology, 2005
The primary function of neutrophil-derived serine proteases, neutrophil elastase, cathepsin G, and proteinase 3 (PR3) are thought to be the degradation of extracellular proteins at sites of inflammation, but excessive, prolonged, or inappropriate proteolytic activity causes harmful effects in the body.
openaire   +3 more sources

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

Immunologic Research, 2015
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.
Yong Chul Kim   +8 more
openaire   +3 more sources

ANCA antigens: Proteinase 3

1994
The antigen for the cANCA reactivity is the serine protease Proteinase 3 (PR-3). In 1988 several groups showed that the antigen was a protein with a molecular weight of 29 kDa [1–3] and in 1989 three groups showed by N-terminal sequencing that the antigen was PR-3 [4–6].
Allan Wiik, Jörgen Wieslander
openaire   +2 more sources

Generation of Anti-Proteinase 3 Monoclonal Antibodies and Development of Immunological Methods to Detect Endogenous Proteinase 3

Hybridoma, 2010
Proteinase 3 (PR3), a neutrophil granule serine protease, is the major autoantigen for autoantibodies in the systemic vasculitic disease, Wegener's granulomatosis. It is also found to be involved in various inflammatory diseases including Crohn's disease, rheumatoid arthritis, cystic fibrosis, and gingivitis.
Siyoung Lee   +8 more
openaire   +3 more sources

Selective Inhibitors of Human Neutrophil Proteinase 3

Current Pharmaceutical Design, 2012
Human neutrophil proteinase 3 (PR3) and elastase (HNE) are homologous serine proteinases involved in the proteolytic events associated with inflammation and infection. Their close structural and functional resemblance makes it difficult to understand their respective biological functions.
Marie-Claude Viaud-Massuard   +3 more
openaire   +3 more sources

Cleavage and inactivation of human C1 inhibitor by the human leukocyte proteinase, proteinase 3

European Journal of Immunology, 1993
AbstractIncubation of highly purified human C1 inhibitor with equally pure human leukocyte proteinase 3, resulted in a dose‐ and time‐dependent inactivation of C1 inhibitor hemolytic activity. Furthermore, this inactivation was accompanied by proteinase 3‐dependent cleavage of the C1 inhibitor into an 83 000 molecular weight fragment.
E. Christiaan Hagen   +7 more
openaire   +3 more sources

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