3.4.21.76: Myeloblastin
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For detailed information about Myeloblastin, go to the full flat file.
Word Map on EC 3.4.21.76
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3.4.21.76
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ancas
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myeloperoxidase
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elastase
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antineutrophil
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autoantibody
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anca-associated
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cathepsin
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pr3-anca
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polyangiitis
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autoimmune
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granule
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glomerulonephritis
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mpo-anca
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vasculitides
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remission
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autoantigens
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anti-pr3
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perinuclear
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polymorphonuclear
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cyclophosphamide
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azurophilic
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gpa
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crescent
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anti-mpo
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anca-positive
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lactoferrin
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pauci-immune
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churg-strauss
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granulomatous
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elafin
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vasculitic
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anti-myeloperoxidase
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rituximab
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small-vessel
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antibody-associated
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azurocidin
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anti-proteinase
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neutrophil-derived
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polyarteritis
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antinuclear
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mpo-anca-associated
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ethanol-fixed
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goodpasture
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drug development
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diagnostics
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chapel
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medicine
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analysis
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nsp4
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aspartate-specific
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necrotising
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nodosa
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anti-gbm
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anti-glomerular
- 3.4.21.76
-
ancas
- myeloperoxidase
- elastase
-
antineutrophil
- autoantibody
-
anca-associated
- cathepsin
-
pr3-anca
- polyangiitis
- autoimmune
- granule
- glomerulonephritis
-
mpo-anca
- vasculitides
-
remission
- autoantigens
- anti-pr3
-
perinuclear
-
polymorphonuclear
- cyclophosphamide
-
azurophilic
- gpa
-
crescent
-
anti-mpo
-
anca-positive
- lactoferrin
-
pauci-immune
-
churg-strauss
-
granulomatous
- elafin
-
vasculitic
-
anti-myeloperoxidase
- rituximab
-
small-vessel
-
antibody-associated
-
azurocidin
-
anti-proteinase
-
neutrophil-derived
- polyarteritis
-
antinuclear
-
mpo-anca-associated
-
ethanol-fixed
-
goodpasture
- drug development
- diagnostics
-
chapel
- medicine
- analysis
- nsp4
-
aspartate-specific
-
necrotising
- nodosa
- anti-gbm
-
anti-glomerular
Reaction
Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-/- > -Val-/- =
Synonyms
AGP7, C-ANCA antigen, hPR-3, human leukocyte proteinase 3, human PR3, human proteinase 3, Leukocyte proteinase 3, Leukocyte proteinase 4, membrane proteinase 3, membrane-associated proteinase 3, mP3, mPR3, myeloblastin, neutrophil protease PR3, neutrophil proteinase 3, neutrophil serine protease, neutrophilic serine protease proteinase 3, P29, p29b, PMNL proteinase, Pr 3, PR-3, PR3, protease 3, proteinase 3, Proteinase PR-3, Proteinase-3, proteinase3, PRTN3, SAP3, secreted aspartic proteinase 3, surface proteinase 3, Wegener autoantigen, Wegener's autoantigen, Wegener's granulomatosis autoantigen, Xenopus PR3, xPR-3
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
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knowledge of the protonation states of the ionizable residues in an enzyme like PR3 is a prerequisite to an accurate description of its structure and mechanism
diagnostics
anti-neutrophil cytoplasmic antibodies with proteinase 3 specificity are a useful laboratory biomarker for the diagnosis of granulomatosis with polyangiitis, i.e.Wegener's granulomatosis
drug development
medicine
additional information
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design of potent and highly specific substrates of proteinase 3 and other proteinases optimized in the prime site region
drug development
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design of inhibitors aimed at neutralizing the cleavage activity of PR3 toward endogenous annexin 1 and hence suitable for development as novel anti-inflammatory therapeutics
drug development
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optimized sequences, which allow close interaction with the extended active site of Pr3 for the development of peptide or pseudopeptide inhibitors that do not interfere with Pr3-related proteases
drug development
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recombinant PR3 variants have a great potential to study individual anti-PR3 responses and will advance the development of new epitope-based therapeutics
drug development
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either blocking the membrane presentation of PR3 or neutralizing the functions of its binding partners may generate novel therapeutic strategies for anti-neutrophil cytoplasmic autoantibodies-associated vasculitis
drug development
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further exploration of the S' subsites of Pr 3 may lead to the identification of highly selective, reversible competitive inhibitors of Pr 3 using a functionalized surrogate scaffold embellished with appropriate recognition elements
drug development
enzyme inhibitors may prove to be targets for the generation of agents in the treatment of neutrophilic inflammatory disease
drug development
proteinase 3-inhibiting antibodies may play a role in autoimmune vasculitis and can be exploited as highly selective inhibitors
drug development
enzyme Pr3 is a target for the generation of agents in the treatment of neutrophilic inflammatory disease
medicine
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major target autoantigen in patients with Wegener's granulomatosis, a systemic vasculitis
medicine
specific inhibition of PR3 activity to process IL-32 or neutralization of IL-32 by inactive PR3 or its fragments may reduce the consequences of IL-32 in immune regulated diseases
medicine
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down-regulation of anticoagulation during inflammation by rapid endothelial cell protein C receptor proteolysis by PR3
medicine
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in patients with Wegeners granulomatosis, epitope recognition by anti-neutrophil cytoplasmic antibodies (ANCA) is affected by the glycosylation status of PR3
medicine
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involved in autoimmune small vessel vasculitides, e. g. Wegener´s granulomatosis. PR3 is the main target autoatigen of antineutrophilic cytoplasmic antibodies (ANCA). Structure(charge)-based binding interactions between PR3-ANCA and conformational epitopes of PR3. Binding of PR3 to physiological molecules as well as to autoantibodies may induce and promote proinflammatory responses
medicine
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PR3 induces DC maturation via protease-activated receptor-2. Wegeners autoantigen PR3 interacts with a gateway receptor (protease-activated receptor-2) on iDCs in vitro, triggering their maturation and licenses them for a Th1-type response potentially favoring granuloma formation in Wegeners granulomatosis. PR3-anti-neutrophil cytoplasmic antibodies are strongly associated with Wegeners granulomatosis. PR3-anti-neutrophil cytoplasmic antibodies opsonization of apoptotic neutrophils results in effective phagocytosis by human monocyte-derived macrophages and leads to up-regulation of proinflammatory mediator production. An animal model for PR3-anti-neutrophil cytoplasmic antibodies-associated vasculitis that shows characteristics similar to human Wegeners granulomatosis is not yet available
medicine
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PR3- and CD177-expressing neutrophils constitute a subpopulation of neutrophils with an unknown role in the innate immune system, which may play an important role in diseases such as Wegeners granulomatosis and polycythemia vera
medicine
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PR3-anti-neutrophil cytoplasmic antibodies from Wegeners granulomatosis patients do not recognize the natively folded murine PR3
medicine
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proinflammatory role of membrane PR3 expression may involve interference with macrophage clearance of apoptotic neutrophils
medicine
responsible for eliminating intracellular pathogens and breaking down tissues at inflammatory sites. Possible molecular target for anti-inflammatory agents. Involved in degradation of ECM components and cleavage of inflammatory mediators, platlet activation, induction of endothelial cells and apoptosis, negative feedback regulation of granulopoiesis. Shows bactericidal properties. Is a target of auto-antibodies in Wegeners granulomatosis
medicine
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extra-intestinal pulmonary complications of ulcerative colitis with elevated proteinase-3 anti-neutrophil cytoplasmic antibody resembling Wegeners granulomatosis and spontaneous improvement
medicine
novel anti-proteinase-3-human native-human recombinant enzyme-linked immunosorbent assay (ELISA) with a very high sensitivity for the detection of proteinase-3-antineutrophil cytoplasmic antibodies (ANCA) in patients with ANCA-associated vasculitis with C-ANCA
medicine
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classic symptoms and clinical findings, together with serology titres positive for anti-neutrophil cytolplasmic antibody against proteinase 3 confirm the diagnosis of Wegener's Granulomatosis, which can occasionally involve other organs as the respiratory and renal tracts and in such cases a differential diagnosis of Wegener's Granulomatosis must be considered, as early recognition and treatment of this potentially fatal disease is paramount
medicine
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neutrophil-activating potential of cANCAs can vary in patients, depending on the association rates, target specificities, and titers of antibodies, as well as on local concentrations of human PR3 inhibitors
medicine
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only therapies based on the dual inhibition of caspase 1 and serine proteases will be successful in the management of complex inflammatory diseases in humans
medicine
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the substrate N-Boc-3-[2-[2-(1'-methyl)pyrrolo]benzoxazol-5-yl]-Ala-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide) may be used for the construction of a very reliable, inexpensive, and easy to use diagnostic test for PR3 determination
medicine
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affinity chromatography of neutrophil lysates using epoxy beads coated with Streptococcus sanguinis reveals involvement of PR3 in phagocytosis of Streptococcus sanguinis. Enzymatic cleavage of the glycosylphosphatidylinositol linker of NB1, a co-receptor for membrane-bound PR3, significantly reduces the phagocytosis. The neutralization of membrane-bound PR3 with antibody reduces both binding and phagocytosis of Streptococcus sanguinis. Protease activity is required for phagocytosis, and protease-activated receptor PAR2 is involved in signal transmission from PR3 during this process
medicine
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in all individuals tested, neutrophils are either double-positive or double-negative for mPR3 and CD177. The proportion of double-positive neutrophils is increased significantly in anti-neutrophil cytoplasmic antibodies-associated systemic vasculitis and systemic lupus erythematosus patients. The proportion of mPR3+/CD177+ cells is not correlated to general inflammation, renal function, age, sex, drug treatment and levels of circulating PR3. The increased membrane expression of PR3 found in anti-neutrophil cytoplasmic antibodies-associated systemic vasculitis is not linked directly to circulating PR3 or PR3 gene transcription, but is dependent upon CD177 expression and correlated with the transcription of the CD177 gene
