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Information on EC 3.4.24.24 - gelatinase A and Organism(s) Rattus norvegicus and UniProt Accession P33436
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3.4.24.24 gelatinase ASpecify your search results
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- 3.4.24.24
- mmp-9
- metalloproteinases
-
zymography
- metastasis
- timp-2
- endothelial
- angiogenesis
- artery
- fibrosis
- necrosis
-
gelatinolytic
-
invasiveness
-
transwell
-
basement
- tnf
- mt1-mmp
- plasminogen
- cardiac
- neutrophil
- aortic
- vessel
- integrins
- fibronectin
- upa
- melanoma
- laminin
- matrigel
- vimentin
- myocardial
-
interstitial
- proteinases
- lymph
- ventricular
- e-cadherin
-
nude
-
angiogenic
- aneurysm
- mesenchymal
- stromelysins
-
anti-metastatic
- fak
- medicine
- elastin
- cox-2
- synthesis
- urokinase
- collagenases
-
urokinase-type
-
collagenolytic
- tgf-beta1
- diagnostics
-
lipocalin
-
boyden
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
mmp-2, gelatinase, matrix metalloproteinase-2, matrix metalloproteinase 2, gelatinase a, type iv collagenase, metalloproteinase-2, progelatinase, collagenase iv, mmp 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
72 kDa Gelatinase
-
-
-
-
72 kDa Gelatinase type A
-
-
-
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72-kDa Gelatinase
-
-
-
-
Collagenase IV
-
-
-
-
Collagenase type IV
-
-
-
-
Matrix metalloproteinase 2
-
-
-
-
MMP 2
-
-
-
-
Type IV collagen metalloproteinase
-
-
-
-
Type IV collagenase
-
-
-
-
Type IV collagenase/gelatinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
146480-35-5
-
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
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
interleukin 1beta
-
increases enzyme expression and activity in cardiac microvascular endothelial cells, involvement of PKC and/or MAPK signaling cascades, overview, the activation is inhibited by 52% by Gö6976, a PKC inhibitor, at 100 nM, while inhibitors SN50 and SP600125 have no effect on the activation
-
additional information
-
implantation of 9L glioma cells into brain increases the expression of MMP-2, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
quantitative MMP-2 expression analysis of untreated and induced cells, 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
distribution and activation of matrix metalloproteinase-2 in skeletal muscle fibers, quantification of MMP2 in muscle, overview. On average, about 57% of the MMP2, along with most of the GAPDH, in the skinned fibers is freely diffusible in the cytosol, about 6% of the MMP2 dissociates with the subsequent 10-min Triton X-100 treatment, and about 37% of the MMP2 remains in the skinned fiber
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aged arterial wall, colocalization of activated enzyme and transforming growth factor TGF-beta1. Treatment of young aortic rings with activated enzyme enhances active transforming growth factor TGF-beta-1, collagen, and fibronectin expression to the level of untreated old counterparts
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expression analysis in brain after implantation of 9L glioma cells, overview
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vascular smooth muscle, colocalization of activated enzyme and transforming growth factor TGF-beta1. Treatment of vascular smooth muscle cells in vitro with activated enzyme enhances active transforming growth factor TGF-beta-1, collagen, and fibronectin expression to the level of untreated old counterparts
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activity of MMP-2 in odontogenic region of the rat incisor tooth after post shortening procedure, overview
additional information
additional information
in rat soleus muscle and other tissues, pro- and active MMP2 show gelatinase activity, as well as a higher band that has been reported previously to represent a rodent-specific glycosylated MMP2
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
aortic stiffness is an independent risk factor for development of cardiovascular diseases. Activation of renin-angiotensin-aldosterone system (RAAS) including angiotensin converting enzyme (ACE) activity leads to overproduction of angiotensin II (ANGII) from its precursor angiotensin I (ANGI). ANGII leads to overexpression and activation of matrix metalloproteinase-2 (MMP2), which is critically associated with pathophysiology of aortic stiffness
physiological function
-
in adult rats, in opposite to development of tooth, the MMP-9 and MMP-2 present in the odontogenic region does not seem to play a direct role in the remodeling matrix, even after post-shortening procedures which to lead an acceleration of the eruption process in the incisor
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). MMP2_RAT
662
1
74149
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
66000
-
x * 72000, pro-MMP-2, SDS-PAGE, x * 66000, activated MMP-2, SDS-PAGE
72000
-
x * 72000, pro-MMP-2, SDS-PAGE, x * 66000, activated MMP-2, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
down
peptide isoleucine-tryptophan (Ile-Trp) inhibits expression and activity of matrix metalloproteinase-2 in rat aorta
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in vitro, both angiotensin II (ANGII) and ANGI stimulation significantly increase expression of MMP2
peptide Ile-Trp isoleucine-tryptophan inhibits expression and activity of matrix metalloproteinase-2 in rat aorta, mechanism of action, overview. The inhibitor significantly inhibits ANGI, but not ANGII mediated increase in expression of MMP2, while losartan also blocks effects of ANGII. Signaling pathways regulating MMP2 expression in endothelial cells and smooth muscle cells are similarly inhibited after treatment with Ile-Trp or captopril. Ile-Trp not only inhibits the MMP2 expression, but also its activation assessed with gelatin zymography
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
during gastric ulcer healing, enzyme expression as well as matrix metalloproteinase MMP-3 and MMP-13 are induced in stromal cells of the gastric mucosa bordering the ulcer. Gelatinolytic activity is increased during the healing and is associated with extracellular matrix of the healing mucosa and newly formed vessels. Enzyme mRNA is homogenously distributed in all layers of the ulcer bed
medicine
-
endogenous urokinase plasminogen activator from cultured hepatic stellate cells significantly induces the active forms of enzyme and matrix metalloproteinase MMP-9 in cirrhotic tissue slices. Transfection of hepatic stellate cells with urokinase plasminogen activator gene results in overactivation of enzyme and matrix metalloproteinases MMP-3 and MMP-9
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, M.; Zhao, D.; Spinetti, G.; Zhang, J.; Jiang, L.Q.; Pintus, G.; Monticone, R.; Lakatta, E.G.
Matrix metalloproteinase 2 activation of transforming growth factor-beta1 (TGF-beta1) and TGF-beta1-type II receptor signaling within the aged arterial wall
Arterioscler. Thromb. Vasc. Biol.
26
1503-1509
2006
Rattus norvegicus
Calabro, A.; Grappone, C.; Pellegrini, G.; Evangelista, S.; Tramontana, M.; Schuppan, D.; Herbst, H.; Milani, S.
Spatial and temporal pattern of expression of interstitial collagenase, stromelysin/transin, gelatinase A, and TIMP-1 during experimental gastric ulcer healing
Digestion
70
127-138
2004
Rattus norvegicus
Gonzalez-Cuevas, J.; Bueno-Topete, M.; Armendariz-Borunda, J.
Urokinase plasminogen activator stimulates function of active forms of stromelysin and gelatinases (MMP-2 and MMP-9) in cirrhotic tissue
J. Gastroenterol. Hepatol.
21
1544-1554
2006
Rattus norvegicus
Mountain, D.J.; Singh, M.; Menon, B.; Singh, K.
Interleukin-1beta increases expression and activity of matrix metalloproteinase-2 in cardiac microvascular endothelial cells: role of PKCalpha/beta1 and MAPKs
Am. J. Physiol. Cell Physiol.
292
C867-C875
2007
Rattus norvegicus
Zhao, J.X.; Yang, L.P.; Wang, Y.F.; Qin, L.P.; Liu, D.Q.; Bai, C.X.; Nan, X.; Shi, S.S.; Pei, X.J.
Gelatinolytic activity of matrix metalloproteinase-2 and matrix metalloproteinase-9 in rat brain after implantation of 9L rat glioma cells
Eur. J. Neurol.
14
510-516
2007
Rattus norvegicus
Gomes, J.R.; Omar, N.F.; dos Santos Neves, J.; Narvaes, E.A.; Novaes, P.D.
Immunolocalization and activity of the MMP-9 and MMP-2 in odontogenic region of the rat incisor tooth after post shortening procedure
J. Mol. Histol.
42
153-159
2011
Rattus norvegicus, Rattus norvegicus Wistar
Ren, X.; Lamb, G.D.; Murphy, R.M.
Distribution and activation of matrix metalloproteinase-2 in skeletal muscle fibers
Am. J. Physiol. Cell Physiol.
317
C613-C625
2019
Homo sapiens (P08253), Homo sapiens, Rattus norvegicus (P33436)
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