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Information on EC 3.4.24.87 - ADAMTS13 endopeptidase and Organism(s) Mus musculus and UniProt Accession Q769J6
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- 3.4.24.87
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thrombotic
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thrombocytopenic
- purpura
- ttp
- platelet
- multimers
-
hemolytic
- anemia
- endothelial
- metalloproteinase
- autoantibody
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microangiopathic
- rituximab
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remission
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uremic
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microvascular
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relapse
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life-threatening
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shear
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idiopathic
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- autoimmune
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thrombi
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bleeding
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hemostasis
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schistocytes
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intravascular
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relapsing
-
plasmapheresis
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ultra-large
-
hemostat
-
disintegrin-like
-
microcirculation
-
vwf:ag
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coombs
- plasmic
-
microthrombi
-
shiga
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hellp
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collagen-binding
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antiphospholipid
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microthrombosis
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d-dimers
- fviii
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prothrombotic
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apheresis
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hemolytic-uremic
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- eculizumab
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oklahoma
- analysis
- drug development
- diagnostics
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
The enzyme cleaves the von Willebrand factor at bond Tyr842-/-Met843 within the A2 domain
Synonyms
adamts13, adamts-13, von willebrand factor-cleaving protease, vwf-cp, vwf-cleaving protease, adamts 13, von willebrand factor cleaving protease, vwf cleaving protease, metalloprotease adamts-13, vwf protease, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
a disintegrin-like and metalloprotease with thrombospondin type I repeats 13
-
ADAMTS13
ADAMTS13
-
i.e. a disintegrin-like and metalloprotease with trombospondin type-1 repeats 13
CAS REGISTRY NUMBER
COMMENTARY
334869-10-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
FRET-VWF73 + H2O
?
-
fluorogenic von Willebrand factor-derived peptide substrate. The distal C-terminal domains of ADAMTS13 are not necessary for the cleavage of the VWF73-based peptide substrate
-
-
?
GST-VWF73 + H2O
?
-
labeled von Willebrand factor-derived peptide substrate. The distal C-terminal domains of ADAMTS13 are not necessary for the cleavage of the VWF73-based peptide substrate
-
-
?
von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
von Willebrand factor + H2O
von Willebrand factor fragments
-
ADAMTS13 cleaves von Willebrand factor to smaller less-active forms
-
-
?
von Willebrand factor + H2O
?
-
-
-
-
?
von Willebrand factor + H2O
?
-
specific cleavage of ultra-large von Willebrand factor multimers
-
-
?
von Willebrand factor + H2O
?
-
von Willebrand factor is also susceptible to cleavage by ADAMTS13 when incorporated in a thrombus
-
-
?
von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
-
ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain
-
-
?
von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
-
ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain. The wild-type mouse ADAMTS13 shows no activity with the recombinant human substrate in vitro, comparison to other mammal enzymes, overview
-
-
?
additional information
?
-
important role for ADAMTS13 in preventing excessive spontaneous Weibel-Palade body secretion, and in the regulation of leukocyte adhesion and extravasation during inflammation
-
-
?
additional information
?
-
-
assay on the fluorogenic substrate FRETS-vWF73
-
-
?
additional information
?
-
-
no activity in von Willebrand factor-deficient or ADAMTS13-deficient mice with the recombinant substrate of human origin. Differences in susceptibility to cleavage of recombinant von Willebrand factor by different species need to be considered when interpreting the physiology of human recombinant von Willebrand factor from results of tests in animal models
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
-
ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain
-
-
?
von Willebrand factor + H2O
von Willebrand factor fragments
-
ADAMTS13 cleaves von Willebrand factor to smaller less-active forms
-
-
?
additional information
?
-
important role for ADAMTS13 in preventing excessive spontaneous Weibel-Palade body secretion, and in the regulation of leukocyte adhesion and extravasation during inflammation
-
-
?
von Willebrand factor + H2O
?
-
von Willebrand factor is also susceptible to cleavage by ADAMTS13 when incorporated in a thrombus
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
ADAMTS-13 activity is evaluated in a model of sepsis induced by cecum ligature and puncture in wild-type and Vwf-/- mice. In wild-type mice, cecum ligature and puncture-induced sepsis elicits a significant ADAMTS-13 decrease, and a strong negative correlation exists between von Willebrand factor, VWF, and ADAMTS-13. In Vwf-/- mice, cecum ligature and puncture also induces severe sepsis, but ADAMTS-13 is not significantly diminished
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
determination of ADAMTS13 antigen and proteolytic activity in murine plasma, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
activity is undetectable in heart, brain, kidney and testis
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
-
ADAMTS13 is a multidomain protease that limits platelet thrombogenesis through the cleavage of von Willebrand factor and contributes to inhibition of platelet aggregation. Accelerated thrombus growth occurs in truncated mutant Adamts13S/S mice compared with wild-type full-length Adamts13L/L mice, indicating that the distal C-terminally truncated form of mouse ADAMTS13 has significantly reduced activity in vivo
physiological function
-
ADAMTS13 may protect the brain from ischemia by regulating VWF-platelet interactions after reperfusion, limiting platelet-dependent thrombus growth. ADAMTS13 may ameliorate ischemic brain damage in acute stroke
physiological function
-
ADAMTS13 negatively regulates both thrombosis and inflammation. ADAMTS13 deficiency results in larger infarctions after focal cerebral ischemia in mice, but only in mice that have von Willebrand factor
physiological function
-
antithrombotic properties of ADAMTS-13, complete ADAMTS-13 deficiency promotes thrombus formation and embolization in activated murine microvenule endothelium
additional information
-
ADAMTS-13 activity is evaluated in a model of sepsis induced by cecum ligature and puncture in wild-type and Vwf-/- mice. In wild-type mice, cecum ligature and puncture-induced sepsis elicits a significant ADAMTS-13 decrease, and a strong negative correlation exists between von Willebrand factor, VWF, and ADAMTS-13. In Vwf-/- mice, cecum ligature and puncture also induces severe sepsis, but ADAMTS-13 is not significantly diminished
additional information
-
ADAMTS13 deficiency causes progressive decline of postischemic rCBF, with a resultant exacerbation of ischemic brain injury, role of ADAMTS13 in a transient middle cerebral arterial occlusion model of ischemia-reperfusion injury in the mouse brain using Adamts-/- mice, and comparison of effect of Adamts13 gene deletion on brain ischemia in male Adamts13-/- and wild-type mice, overview
additional information
-
ADAMTS13 deficiency results in more and larger circulating platelet aggregates of von Willebrand factor mutants mVWF/R1306Q and mVWF/V1316M, whereas the full multimer range remains present in the mutant mice. The gain-of-function mutations of the von Willebrand factor leads to the Von Willebrand disease-type 2B, VWD-type 2B, resulting in enhanced platelet binding. Clinical manifestations include increased bleeding tendency, loss of large multimers, thrombocytopenia, and circulating platelet aggregates. The VWD-type 2B phenotype depends on the mutations and ADAMTS13, establishment of a mouse model, overview
additional information
-
genetic or acquired deficiency of plasma ADAMTS13 activity leads to a potentially fatal syndrome, thrombotic thrombocytopenic purpura, TTP
additional information
-
infusion of a high dose of recombinant human ADAMTS13 into a wild-type mouse immediately before reperfusion reduces infarct volume and improves functional outcome without producing cerebral hemorrhage. Recombinant ADAMTS13 does not enhance bleeding in a hemorrhagic stroke model
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ATS13_MOUSE
1426
1
155357
Swiss-Prot
Secretory Pathway (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
generation of a congenic mouse model expressing the C-terminally truncated form of ADAMTS13 on 129/Sv genetic background, presence of IAP insertion in the Adamts13 gene of the congenic Adamts13S/S mice by PCR, and detection an IAP chimeric transcript by Northern blotting of RNA from liver, overview. The distal C-terminally truncated form of mouseADAMTS13 does not completely lose the activity. In vivo thrombus growth is accelerated in Adamts13S/S mice, overview
additional information
-
plasma ADAMTS13 proteolytic activity on average can be restored in Adamts13-/- mice to approximately 25% of wild-type level by autologous transplantation of hematopoietic progenitor cells transduced ex vivo with a self-inactivating lentiviral vector encoding a full-length murine Adamts13 and an enhanced GFP reporter gene
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzyme forms in HEK-293 cells and CHO cells
-
gene Adamts13, DNA and amino acid sequence determination and analysis, expression of truncated ADAMTS13 in 129/Sv transgenic mice
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gene Adamts13, DNA and amino acid sequence determination, construction of self-inactivated lentiviral vector, and expression of functional His-tagged ADAMTS13 cDNA in COS-7 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
ADAMTS13 deficiency leads to the fatal disorder thrombotic thrombocytopenic purpura. Cyclosporin A, an inhibitor of cyclophilin B, reduces the secretion of ADAMTS13 and leads to conformational changes in the protein resulting in diminished ADAMTS13 proteolytic activity. Cyclophilin B and ADAMTS13 show a direct, functional interaction
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bruno, K.; Voelkel, D.; Plaimauer, B.; Antoine, G.; Pable, S.; Motto, D.G.; Lemmerhirt, H.L.; Dorner, F.; Zimmermann, K.; Scheiflinger, F.
Cloning, expression and functional characterization of the full-length murine ADAMTS13
J. Thromb. Haemost.
3
1064-1073
2005
Mus musculus, Mus musculus BALB/c
Chauhan, A.K.; Walsh, M.T.; Zhu, G.; Ginsburg, D.; Wagner, D.D.; Motto, D.G.
The combined roles of ADAMTS13 and VWF in murine models of TTP, endotoxemia, and thrombosis
Blood
111
3452-3457
2008
Mus musculus
Chung, M.C.; Popova, T.G.; Jorgensen, S.C.; Dong, L.; Chandhoke, V.; Bailey, C.L.; Popov, S.G.
Degradation of circulating von Willebrand factor and its regulator ADAMTS13 implicates secreted Bacillus anthracis metalloproteases in anthrax consumptive coagulopathy
J. Biol. Chem.
283
9531-9542
2008
Homo sapiens, Mus musculus
Chauhan, A.K.; Kisucka, J.; Brill, A.; Walsh, M.T.; Scheiflinger, F.; Wagner, D.D.
ADAMTS13: a new link between thrombosis and inflammation
J. Exp. Med.
205
2065-2074
2008
Mus musculus (Q769J6)
Laje, P.; Shang, D.; Cao, W.; Niiya, M.; Endo, M.; Radu, A.; DeRogatis, N.; Scheiflinger, F.; Zoltick, P.W.; Flake, A.W.; Zheng, X.L.
Correction of murine ADAMTS13 deficiency by hematopoietic progenitor cell-mediated gene therapy
Blood
113
2172-2180
2009
Mus musculus
Banno, F.; Chauhan, A.; Kokame, K.; Yang, J.; Miyata, S.; Wagner, D.; Miyata, T.
The distal carboxyl-terminal domains of ADAMTS13 are required for regulation of in vivo thrombus formation
Blood
113
5323-5329
2009
Mus musculus
Zhao, B.Q.; Chauhan, A.K.; Canault, M.; Patten, I.S.; Yang, J.J.; Dockal, M.; Scheiflinger, F.; Wagner, D.D.
von Willebrand factor-cleaving protease ADAMTS13 reduces ischemic brain injury in experimental stroke
Blood
114
3329-3334
2009
Homo sapiens, Mus musculus
Fujioka, M.; Hayakawa, K.; Mishima, K.; Kunizawa, A.; Irie, K.; Higuchi, S.; Nakano, T.; Muroi, C.; Fukushima, H.; Sugimoto, M.; Banno, F.; Kokame, K.; Miyata, T.; Fujiwara, M.; Okuchi, K.; Nishio, K.
ADAMTS13 gene deletion aggravates ischemic brain damage: a possible neuroprotective role of ADAMTS13 by ameliorating postischemic hypoperfusion
Blood
115
1650-1653
2010
Mus musculus
Rayes, J.; Hollestelle, M.J.; Legendre, P.; Marx, I.; de Groot, P.G.; Christophe, O.D.; Lenting, P.J.; Denis, C.V.
Mutation and ADAMTS13-dependent modulation of disease severity in a mouse model for von Willebrand disease type 2B
Blood
115
4870-4877
2010
Mus musculus
Varadi, K.; Rottensteiner, H.; Vejda, S.; Weber, A.; Muchitsch, E.M.; Turecek, P.L.; Ehrlich, H.J.; Scheiflinger, F.; Schwarz, H.P.
Species-dependent variability of ADAMTS13-mediated proteolysis of human recombinant von Willebrand factor
J. Thromb. Haemost.
7
1134-1142
2009
Canis lupus familiaris, Cavia porcellus, Oryctolagus cuniculus, Macaca fascicularis, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Lerolle, N.; Dunois-Larde, C.; Badirou, I.; Motto, D.G.; Hill, G.; Bruneval, P.; Diehl, J.L.; Denis, C.V.; Baruch, D.
von Willebrand factor is a major determinant of ADAMTS-13 decrease during mouse sepsis induced by cecum ligation and puncture
J. Thromb. Haemost.
7
843-850
2009
Mus musculus
Hershko, K.; Simhadri, V.L.; Blaisdell, A.; Hunt, R.C.; Newell, J.; Tseng, S.C.; Hershko, A.Y.; Choi, J.W.; Sauna, Z.E.; Wu, A.; Bram, R.J.; Komar, A.A.; Kimchi-Sarfaty, C.
Cyclosporin A impairs the secretion and activity of ADAMTS13 (a disintegrin and metalloprotease with thrombospondin type 1 repeat)
J. Biol. Chem.
287
44361-44371
2012
Mus musculus (Q769J6), Homo sapiens (Q76LX8), Homo sapiens
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