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Information on EC 3.4.24.22 - stromelysin 2 and Organism(s) Homo sapiens and UniProt Accession P09238

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.22 stromelysin 2
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P09238 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Similar to stromelysin 1, but action on collagen types III, IV and V is weak
Synonyms
mmp-10, mmp10, stromelysin-2, matrix metalloproteinase-10, matrix metalloproteinase 10, stromelysin 2, transin 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Matrix metalloproteinase 10
-
stromelysin 2
-
Matrix metalloproteinase 10
Matrix metalloproteinase-10
MMP-10
Proteoglycanase 2
-
-
-
-
ST-2
-
-
stromelysin-2
Transformation-associated protein 34A
-
-
-
-
Transin 2
-
-
-
-
Transins, 2
-
-
-
-
additional information
-
MMP-10 or stromelysin-2 is a member of the stromelysin family of enzymes
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
140610-48-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2 + H2O
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu + norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2
show the reaction diagram
-
-
-
?
Ac-Pro-Leu-Gly-(2-mercapto-4-methyl-pentanoyl)-Leu-Gly-OC2H5 + H2O
?
show the reaction diagram
-
-
-
?
Aggrecan core protein + H2O
?
show the reaction diagram
-
-
-
-
?
Azocoll + H2O
?
show the reaction diagram
-
-
-
-
?
Cartilage link protein + H2O
?
show the reaction diagram
-
cleaved at His16-Ile17 bond
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
Elastin + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
Gelatin + H2O
?
show the reaction diagram
procollagenase + H2O
?
show the reaction diagram
-
-
-
-
?
proMMP-1 + H2O
MMP-1 + propeptide
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
procollagenase + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
zinc metalloproteinase
Zinc
-
zinc metalloenzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
-
GM6001
-
a broad-spectrum MMP inhibitor
N-isobutyl-N-(4-methoxy-phenylsulfonyl)glycyl hydroxamic acid
-
i.e. NNGH, study of binding mode. Interaction of inhibitor with Zn1 atom and S1’ subsite
PAI-1
-
functions as an upstream regulator of a MMP-10-initiated collagenolytic phenotype, it blocks conversion of MMP-10 to its active form. Neutralization of endogenous PAI-1 with function blocking antibodies accelerates both collagenolysis and activation of MMP-10
-
Specific tissue inhibitor of metalloproteinases
-
TIMP-1
-
TIMP-2
-
tissue inhibitor of metalloproteinases 1
TIMP-1, the protein is expressed in HEK 293E cells, enzyme binding structure analysis and mechanism of inhibition, detailed overview and comparison to stromelysin-1, EC 3.4.24.17
-
tissue inhibitor of metalloproteinases 2
-
additional information
the endogenous tissue inhibitors of metalloproteinases (TIMPs) regulate proteolytic activity by binding tightly to the MMP active site. While each of the four TIMPs can inhibit most MMPs, binding data reveal tremendous heterogeneity in affinities of different TIMP/MMP pairs. Identification of a group of highly conserved contacts at the heart of MMP/TIMP complexes that define the conserved mechanism of inhibition, as well as a second category of diverse adventitious contacts at the periphery of the interfaces
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.8
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000011
tissue inhibitor of metalloproteinases 1
catalytic enzyme domain, pH 7.0, 37°C
-
0.0000058
tissue inhibitor of metalloproteinases 2
catalytic enzyme domain, pH 7.0, 37°C
-
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
activity against aggrecan at pH 5.5 is double that at pH 6.0
7.5 - 8
-
azocoll
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
6.0: 25% of activity maximum, 7.5-8.0: activity maximum, azocoll
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
HUVEC, quantitative RT-PCR of MMPs, overview
Manually annotated by BRENDA team
-
MMP-10 is notably increased in neurons of the ischemic brain but not in healthy areas
Manually annotated by BRENDA team
-
induction of enzyme expression by TNF-alpha and EGF
Manually annotated by BRENDA team
-
SV40-transformed
Manually annotated by BRENDA team
-
colon adenocarcinoma cell line
Manually annotated by BRENDA team
-
proenzyme expression is markedly induced in endothelial cells undergoing capillary tube morphogenesis. Enzyme-induced activation of matrix metalloproteinase MMP-1 correlates with tube regression and gel contraction
Manually annotated by BRENDA team
-
expression of matrix metalloproteinases MMP-1, MMP-7 and MMP-10 by migrating enterocytes bordering intestinal ulcers
Manually annotated by BRENDA team
-
neoplastic
Manually annotated by BRENDA team
-
keratinocyte cell line, induction of enzyme and matrix metalloproteinases MMP-1 and MMP-3 by UVA, induction is suppressed by beta-carotene. beta-Carotene dose-dependently quenches 1O2-mediated induction of enzyme and MMP-1
Manually annotated by BRENDA team
-
MMP-10 and MMP-1 are up-regulated in HaCaT II-4 cells
Manually annotated by BRENDA team
-
colon adenocarcinoma cell line
Manually annotated by BRENDA team
-
MMP-10 protein levels are higher in the tumor tissues than in the adjacent normal tissues
Manually annotated by BRENDA team
-
postmortem or following surgery
Manually annotated by BRENDA team
-
no differences in MMP-10 in the plasma of hypertensive versus normotensive subjects
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
colon adenocarcinoma cell line
Manually annotated by BRENDA team
-
induction of enzyme expression by TNF-alpha and EGF
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
overexpressed MMP10 localizes to the cytoplasm
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
evolution
despite their similar substrate specificities, the stromelysins show differential patterns of transcriptional regulation and tissue distribution that hint at distinct physiological functions in processes such as skeletal development, wound healing, and vascular remodeling
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MMP10_HUMAN
476
0
54151
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
-
x * 56000, pro-MMP-10, SDS-PAGE, x * 42000, mature MMP-10, SDS-PAGE
56000
-
x * 56000, pro-MMP-10, SDS-PAGE, x * 42000, mature MMP-10, SDS-PAGE
additional information
-
synthesized as preproenzyme of 476 amino acids and secreted from cells as the proenzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 56000, pro-MMP-10, SDS-PAGE, x * 42000, mature MMP-10, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
additional information
-
potential glycosylation site at Asn100, but is unlikely to be a glycoprotein as it does not bind concanavalin A
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified active human MMP-10 catalytic domain in complex with inhibitor protein TIMP-2, hanging drop vapor diffusion method, mixing of proteins in a 1:1.1 (mol/mol) ratio, 4.5-5.5 mg/ml protein in 20 mM Tris, pH 8.5 and 150 mM NaCl, are mixed with reservoir solution containing 0.1 M HEPES, pH 7.5, and 25% w/v PEG 2000 monomethyl ether, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement, comparison and analysis of the crystal structure of the human MMP-10/TIMP-1 complex, PDB ID 3V96
purified isolated catalytic enzyme domain in complex with inhibitor TIMP1, 1:1.2 (mol/mol) mixture of enzyme protein and fully deglycosylated TIMP-N30A mutant is concentrated to achieve a final protein concentration of 4-5 mg/ml. Crystals are grown by hanging drop vapor diffusion method at room temperature in 0.1 M sodium dihydrogen phosphate, pH 6.5, 12% w/v PEG 8000, 2 weeks, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement
recombinant catalytic domain, in complex with inhibitor N-isobutyl-N-(4-methoxy-phenylsulfonyl)glycyl hydroxamic acid, i.e. NNGH. Comparison with structure of matrix metalloproteinase MMP-3
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
down
-
aldose reductase inhibitor, fidarestat, normalizes high-glucose level-mediated suppression of MMP-10 expression, it downregulates MMP-10 expression
medicine
-
cells resistant to protein kinase C potentiated, transcription factor p53 mediated apoptosis express a higher level of matrix metalloproteinases MMP-9 and MMP-10. Matrix metalloproteinases function confers protection from protein kinase C/p53 induced apoptosis and are implicated in tumor cell resistance
up
-
a high glucose level decreases MMP-10 expression in corneal epithelial cells
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, prostromelysin 2, 50 mM Tris-HCl, pH 7.5, 0.15 M NaCl, 10 mM CaCl2, 0.02% w/v NaN3, 0.05% Brij 35, stable for 4 weeks
-
4°C, prostromelysin 2, 50 mM Tris-HCl, pH 7.5, 0.15 M NaCl, 10 mM CaCl2, 0.02% w/v NaN3, 0.05% Brij 35, stable for 2 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme MMP-10 catalytic domain from Escherichia coli strain BL21 (DE3), by anion exchange chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
MMP-10 DNA and amino acid sequence determination and expression analysis in HUVECs, transcriptional regulation of MMP-10 by Ets transcription factors, overview
MMP-10 real-time PCR quantitative expression analysis
expression analysis
-
expression analysis of MMP10 in cancerous and healthy oral tissues, overview
-
expression of the enzyme catalytic domain in Escherichia coli strain BL21 (DE3)
gene MMP-10, semi-quantitative RT-PCR expression analysis
-
transin and transin-2 genes have very similar structures. The most striking difference is the much larger size of the intron separating exons 6 and 7 of the transin gene compared to the size of the corresponding intron in the transin-2 gene
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
PD98059 and SP600125, ERK and JNK inhibitors, respectively, repress VEGF-induced MMP-10 expression to mRNA expression levels lower than the basal expression of MMP-10
the gene for matrix metalloproteinase 10 is the most significantly upregulated gene in patients with systemic sclerosis (SSc)-associated pulmonary hypertension (PH)
VEGF165 induces MMP-10 expression about 2fold. LY294002 inhibits VEGF-induced MMP-10 expression, indicating the involvement of PI3K in VEGF-induced MMP-10 expression
enhanced collagen degradation, in case of epithelial-to-mesenchymal transition stimulated by transforming growth factor-beta as well as epidermal growth factor receptor, is coupled to a significant increase in matrix metalloproteinase MMP-10 expression and is involved a proteolytic axis composed of plasmin, MMP-10, and MMP-1, ec 3.4.24.7
-
high expression of MMP-10 is frequently observed and is significantly correlated with the invasiveness and metastasis in head and neck squamous cell carcinoma cases
-
increased MMP-10 levels in severe sepsis
-
MMP-10 expression is downregulated with age, overview
-
neuronal MMP-10 is upregulated after stroke in brain in the infarcted tissue compared to healthy control areas, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
diagnostic value of MMP-10 in patients with systemic sclerosis (SSc)-associated pulmonary hypertension (PH)
diagnostics
medicine
-
melanoma inhibitory activity and matrix metalloproteinase-10 are novel prognostic factors in patients with gastric cancer. Immunostaining for both melanoma inhibitory activity, MIA, and enzyme is correlated with poor prognosis in advanced gastric cancer. Patients with gastric cancer show high levels of enzyme in sera
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nagase, H.
Human stromelysins 1 and 2
Methods Enzymol.
248
449-470
1995
Homo sapiens
Manually annotated by BRENDA team
Muller, D.; Quantin, B.; Gesnel, M.C.; Millon-Collard, R.; Abecassis, J.; Breathnach, R.
The collagenase gene family in humans consists of at least four members
Biochem. J.
253
187-192
1988
Homo sapiens
Manually annotated by BRENDA team
Nicholson, R.; Murphy, G.; Breathnach, R.
Human and rat malignant-tumor-associated mRNAs encode stromelysin-like metalloproteinases
Biochemistry
28
5195-5203
1989
Homo sapiens
Manually annotated by BRENDA team
Meyer, E.; Vollmer, J.Y.; Bovey, R.; Stamenkovic, I.
Matrix metalloproteinases 9 and 10 inhibit protein kinase C-potentiated, p53-mediated apoptosis
Cancer Res.
65
4261-4272
2005
Homo sapiens
Manually annotated by BRENDA team
Wertz, K.; Seifert, N.; Hunziker, P.B.; Riss, G.; Wyss, A.; Lankin, C.; Goralczyk, R.
beta-Carotene inhibits UVA-induced matrix metalloprotease 1 and 10 expression in keratinocytes by a singlet oxygen-dependent mechanism
Free Radic. Biol. Med.
37
654-670
2004
Homo sapiens
Manually annotated by BRENDA team
Saunders, W.B.; Bayless, K.J.; Davis, G.E.
MMP-1 activation by serine proteases and MMP-10 induces human capillary tubular network collapse and regression in 3D collagen matrices
J. Cell Sci.
118
2325-2340
2005
Homo sapiens
Manually annotated by BRENDA team
Bertini, I.; Calderone, V.; Fragai, M.; Luchinat, C.; Mangani, S.; Terni, B.
Crystal structure of the catalytic domain of human matrix metalloproteinase 10
J. Mol. Biol.
336
707-716
2004
Homo sapiens
Manually annotated by BRENDA team
Aung, P.P.; Oue, N.; Mitani, Y.; Nakayama, H.; Yoshida, K.; Noguchi, T.; Bosserhoff, A.K.; Yasui, W.
Systematic search for gastric cancer-specific genes based on SAGE data: melanoma inhibitory activity and matrix metalloproteinase-10 are novel prognostic factors in patients with gastric cancer
Oncogene
25
2546-2557
2006
Homo sapiens
Manually annotated by BRENDA team
Salmela, M.T.; Pender, S.L.; Karjalainen-Lindsberg, M.L.; Puolakkainen, P.; Macdonald, T.T.; Saarialho-Kere, U.
Collagenase-1 (MMP-1), matrilysin-1 (MMP-7), and stromelysin-2 (MMP-10) are expressed by migrating enterocytes during intestinal wound healing
Scand. J. Gastroenterol.
39
1095-1104
2004
Homo sapiens
Manually annotated by BRENDA team
Zhang, X.; Zhu, S.; Luo, G.; Zheng, L.; Wei, J.; Zhu, J.; Mu, Q.; Xu, N.
Expression of MMP-10 in lung cancer
Anticancer Res.
27
2791-2795
2007
Homo sapiens
Manually annotated by BRENDA team
Barksby, H.E.; Milner, J.M.; Patterson, A.M.; Peake, N.J.; Hui, W.; Robson, T.; Lakey, R.; Middleton, J.; Cawston, T.E.; Richards, C.D.; Rowan, A.D.
Matrix metalloproteinase 10 promotion of collagenolysis via procollagenase activation: implications for cartilage degradation in arthritis
Arthritis Rheum.
54
3244-3253
2006
Homo sapiens
Manually annotated by BRENDA team
Miyata, Y.; Iwata, T.; Maruta, S.; Kanda, S.; Nishikido, M.; Koga, S.; Kanetake, H.
Expression of matrix metalloproteinase-10 in renal cell carcinoma and its prognostic role
Eur. Urol.
52
791-797
2007
Homo sapiens
Manually annotated by BRENDA team
Orbe, J.; Montero, I.; Rodriguez, J.A.; Beloqui, O.; Roncal, C.; Paramo, J.A.
Independent association of matrix metalloproteinase-10, cardiovascular risk factors and subclinical atherosclerosis
J. Thromb. Haemost.
5
91-97
2007
Homo sapiens
Manually annotated by BRENDA team
Richardson, S.M.; Doyle, P.; Minogue, B.M.; Gnanalingham, K.; Hoyland, J.A.
Increased expression of matrix metalloproteinase-10, nerve growth factor and substance P in the painful degenerate intervertebral disc
Arthritis Res. Ther.
11
R126
2009
Homo sapiens
Manually annotated by BRENDA team
Yen, C.Y.; Chen, C.H.; Chang, C.H.; Tseng, H.F.; Liu, S.Y.; Chuang, L.Y.; Wen, C.H.; Chang, H.W.
Matrix metalloproteinases (MMP) 1 and MMP10 but not MMP12 are potential oral cancer markers
Biomarkers
14
244-249
2009
Homo sapiens
Manually annotated by BRENDA team
Wilkins-Port, C.E.; Ye, Q.; Mazurkiewicz, J.E.; Higgins, P.J.
TGF-beta1 + EGF-initiated invasive potential in transformed human keratinocytes is coupled to a plasmin/MMP-10/MMP-1-dependent collagen remodeling axis: role for PAI-1
Cancer Res.
69
4081-4091
2009
Homo sapiens
Manually annotated by BRENDA team
Friese, R.S.; Rao, F.; Khandrika, S.; Thomas, B.; Ziegler, M.G.; Schmid-Schoenbein, G.W.; OConnor, D.T.
Matrix metalloproteinases: discrete elevations in essential hypertension and hypertensive end-stage renal disease
Clin. Exp. Hypertens.
31
521-533
2009
Homo sapiens
Manually annotated by BRENDA team
Lorente, L.; Martin, M.M.; Labarta, L.; Diaz, C.; Sole-Violan, J.; Blanquer, J.; Orbe, J.; Rodriguez, J.A.; Jimenez, A.; Borreguero-Leon, J.M.; Belmonte, F.; Medina, J.C.; Lliminana, M.C.; Ferrer-Agueero, J.M.; Ferreres, J.; Mora, M.L.; Lubillo, S.; Sanchez, M.; Barrios, Y.; Sierra, A.; Paramo, J.A.
Matrix metalloproteinase-9, -10, and tissue inhibitor of matrix metalloproteinases-1 blood levels as biomarkers of severity and mortality in sepsis
Crit. Care
13
R158
2009
Homo sapiens
Manually annotated by BRENDA team
Tomomatsu, T.; Takamura, Y.; Kubo, E.; Akagi, Y.
Aldose reductase inhibitor counteracts the attenuated adhesion of human corneal epithelial cells induced by high glucose through modulation of MMP-10 expression
Diabetes Res. Clin. Pract.
86
16-23
2009
Homo sapiens
Manually annotated by BRENDA team
Boyd, S.; Virolainen, S.; Paerssinen, J.; Skoog, T.; van Hogerlinden, M.; Latonen, L.; Kylloenen, L.; Toftgard, R.; Saarialho-Kere, U.
MMP-10 (Stromelysin-2) and MMP-21 in human and murine squamous cell cancer
Exp. Dermatol.
18
1044-1052
2009
Homo sapiens, Mus musculus, Mus musculus ICR
Manually annotated by BRENDA team
Komosinska-Vassev, K.; Olczyk, P.; Winsz-Szczotka, K.; Kuznik-Trocha, K.; Klimek, K.; Olczyk, K.
Age- and gender-dependent changes in connective tissue remodeling: physiological differences in circulating MMP-3, MMP-10, TIMP-1 and TIMP-2 Level
Gerontology
57
44-52
2010
Homo sapiens
Manually annotated by BRENDA team
Heo, S.H.; Choi, Y.J.; Ryoo, H.M.; Cho, J.Y.
Expression profiling of ETS and MMP factors in VEGF-activated endothelial cells: role of MMP-10 in VEGF-induced angiogenesis
J. Cell. Physiol.
224
734-742
2010
Homo sapiens (P09238), Homo sapiens
Manually annotated by BRENDA team
Kaner, R.J.; Santiago, F.; Crystal, R.G.
Up-regulation of alveolar macrophage matrix metalloproteinases in HIV1(+) smokers with early emphysema
J. Leukoc. Biol.
86
913-922
2009
Homo sapiens
Manually annotated by BRENDA team
Cuadrado, E.; Rosell, A.; Penalba, A.; Slevin, M.; Alvarez-Sabin, J.; Ortega-Aznar, A.; Montaner, J.
Vascular MMP-9/TIMP-2 and neuronal MMP-10 up-regulation in human brain after stroke: a combined laser microdissection and protein array study
J. Proteome Res.
8
3191-3197
2009
Homo sapiens
Manually annotated by BRENDA team
Deraz, E.M.; Kudo, Y.; Yoshida, M.; Obayashi, M.; Tsunematsu, T.; Tani, H.; Siriwardena, S.B.; Kiekhaee, M.R.; Qi, G.; Iizuka, S.; Ogawa, I.; Campisi, G.; Lo Muzio, L.; Abiko, Y.; Kikuchi, A.; Takata, T.
MMP-10/stromelysin-2 promotes invasion of head and neck cancer
PLoS ONE
6
e25438
2011
Homo sapiens
Manually annotated by BRENDA team
Liu, H.; Qin, Y.; Bi, J.; Guo, A.; Fu, L.; Guan, X.
Overexpression of matrix metalloproteinase 10 is associated with poor survival in patients with early stage of esophageal squamous cell carcinoma
Dis. Esophagus
25
656-663
2012
Homo sapiens
Manually annotated by BRENDA team
Batra, J.; Robinson, J.; Soares, A.; Fields, A.; Radisky, D.; Radisky, E.
Matrix metalloproteinase-10 (MMP-10) interaction with tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2: Binding studies and crystal structure
J. Biol. Chem.
287
15935-15946
2012
Homo sapiens (P01033), Homo sapiens
Manually annotated by BRENDA team
Batra, J.; Soares, A.; Mehner, C.; Radisky, E.
Matrix metalloproteinase-10/TIMP-2 structure and analyses define conserved core interactions and diverse exosite interactions in MMP/TIMP complexes
PLoS ONE
8
e75836
2013
Homo sapiens (P16035)
Manually annotated by BRENDA team
Avouac, J.; Guignabert, C.; Hoffmann-Vold, A.M.; Ruiz, B.; Dorfmuller, P.; Pezet, S.; Amar, O.; Tu, L.; Van Wassenhove, J.; Sadoine, J.; Launay, D.; Elhai, M.; Cauvet, A.; Subramaniam, A.; Resnick, R.; Hachulla, E.; Molberg, Oe.; Kahan, A.; Humbert, M.; Allanore, Y.
Role of stromelysin 2 (matrix metalloproteinase 10) as a novel mediator of vascular remodeling underlying pulmonary hypertension associated with systemic sclerosis
Arthritis Rheumatol.
69
2209-2221
2017
Mus musculus (O55123), Mus musculus, Homo sapiens (P09238), Homo sapiens
Manually annotated by BRENDA team
Kadeh, H.; Heydari, F.; Saravani, S.; Ghodsi, I.N.
Protein expression of stromelysin-2 in head and neck squamous cell carcinomas
Asian Pac. J. Cancer Prev.
16
7843-7846
2015
Homo sapiens
Manually annotated by BRENDA team