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Information on EC 3.4.24.22 - stromelysin 2
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3.4.24.22 stromelysin 2Specify your search results
Word Map
- 3.4.24.22
- metalloproteinases
- mmp-9
- collagen
- metastasis
- timps
- endothelial
- stromelysin-1
- gelatinase
- cartilage
-
basement
- keratinocytes
-
zymography
- matrilysin
- diagnostics
- collagenase-1
-
collagenolytic
- medicine
- sdc1
- metalloelastase
The enzyme appears in 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
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Matrix metalloproteinase 10
Matrix metalloproteinase-10
MMP-10
MMP10
Proteoglycanase 2
-
-
-
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stromelysin 2
stromelysin-2
Transformation-associated protein 34A
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-
-
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Transin 2
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-
-
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Transins, 2
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-
-
-
additional information
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MMP-10 or stromelysin-2 is a member of the stromelysin family of enzymes
Matrix metalloproteinase 10
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-
-
-
Matrix metalloproteinase-10
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-
-
-
MMP-10
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-
-
-
MMP-10
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Similar to stromelysin 1, but action on collagen types III, IV and V is weak
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
140610-48-6
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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
(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
-
-
-
?
Ac-Pro-Leu-Gly-(2-mercapto-4-methyl-pentanoyl)-Leu-Gly-OC2H5 + H2O
?
-
-
-
?
platelet-derived growth factor receptor alpha + H2O
?
cleavage into two fragments of about 40 and 80 kDa, cleavage site is VPAS416.417ILDL in the extracellular domain
-
-
?
ADAMTS-like protein 1 + H2O
?
i.e. punctin-1, an extracellular matrix protein. cooperative processing of ADAMTSL1 by both MMP10 and MMP2, EC 3.4.24.24
-
-
?
ADAMTS-like protein 1 + H2O
?
recombinant recombinant human ADAMTSL1 (isoform 1), generation of a 40 kDa N-terminal cleavage fragment, cleavage site is MPYD372.373LYHP
-
-
?
ADAMTS-like protein 1 + H2O
?
i.e. punctin-1, an extracellular matrix protein. cooperative processing of ADAMTSL1 by both MMP10 and MMP2, EC 3.4.24.24
-
-
?
ADAMTS-like protein 1 + H2O
?
recombinant recombinant human ADAMTSL1 (isoform 1), generation of a 40 kDa N-terminal cleavage fragment, cleavage site is MPYD372.373LYHP
-
-
?
collagen alpha-1(l) + H2O
?
cleavage site is GPPG993-/-994LAGP
-
-
?
collagen alpha-2(I) + H2O
?
cleavage sites are GPQG871-/-872LLGA, EPGP902-/-903LGIS and GPAG991-/-992SVGP
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-
?
collagen alpha-2(I) + H2O
?
cleavage sites are GPQG871-/-872LLGA, EPGP902-/-903LGIS and GPAG991-/-992SVGP
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-
?
additional information
?
-
-
participates in activation of procollagenase proMMP-1
-
-
?
additional information
?
-
-
expression of the collagenase gene family, of which the stromelysin-2 gene is one, might play a role in cancer
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme is involved in intestinal re-epithelialization in vivo and up-regulated by cytokines involved in wound repair
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-
?
additional information
?
-
-
matrix metalloproteinase MMP-1 zymogen activation by enzyme and other serine proteases is central to endothelial cell-mediated collagen degradation and capillary tube regression in 3D collagen matrices
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-
?
additional information
?
-
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active MMP-10 does not cleave collagen type 1 directly, it does activate the collagenase MMP-1, EC 3.4.24.7. The ability of active MMP-10 to superactivate MMP-1 creates a plasmin/MMP-10/MMP-1 proteolytic axis effectively enhances collagen type 1 degradation
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-
?
additional information
?
-
-
MMP-10 is a potent activator of a number of MMP pro-enzymes, including pro-MMP-1, -7, -8, -9 and -13
-
-
?
additional information
?
-
-
recombinant MMP-10 decreases integrin alpha3beta1-expression and cell adhesion of SV40-transformed human corneal epithelial cells, overview
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-
?
additional information
?
-
-
stromelysins are enzymatically active against proteoglycans, procollagenase, and fibronectin
-
-
?
additional information
?
-
the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9
-
-
?
additional information
?
-
-
the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9
-
-
?
additional information
?
-
-
MMPs belong to a family of over 20 neutral endopeptidases that are collectively able to cleave all extracellular matrix components as well as many non-extracellular matrix proteins. The stromelysins, MMP-3, MMP-10 and MMP-11, have a domain arrangement similar to that of collagenases, but they do not cleave interstitial collagens
-
-
?
additional information
?
-
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expression of transin and transin-2 in tumor cells might play a role in tumor invasion
-
-
?
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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
ADAMTS-like protein 1 + H2O
?
i.e. punctin-1, an extracellular matrix protein. cooperative processing of ADAMTSL1 by both MMP10 and MMP2, EC 3.4.24.24
-
-
?
ADAMTS-like protein 1 + H2O
?
i.e. punctin-1, an extracellular matrix protein. cooperative processing of ADAMTSL1 by both MMP10 and MMP2, EC 3.4.24.24
-
-
?
additional information
?
-
-
participates in activation of procollagenase proMMP-1
-
-
?
additional information
?
-
-
expression of the collagenase gene family, of which the stromelysin-2 gene is one, might play a role in cancer
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme is involved in intestinal re-epithelialization in vivo and up-regulated by cytokines involved in wound repair
-
-
?
additional information
?
-
-
matrix metalloproteinase MMP-1 zymogen activation by enzyme and other serine proteases is central to endothelial cell-mediated collagen degradation and capillary tube regression in 3D collagen matrices
-
-
?
additional information
?
-
-
active MMP-10 does not cleave collagen type 1 directly, it does activate the collagenase MMP-1, EC 3.4.24.7. The ability of active MMP-10 to superactivate MMP-1 creates a plasmin/MMP-10/MMP-1 proteolytic axis effectively enhances collagen type 1 degradation
-
-
?
additional information
?
-
-
MMP-10 is a potent activator of a number of MMP pro-enzymes, including pro-MMP-1, -7, -8, -9 and -13
-
-
?
additional information
?
-
-
recombinant MMP-10 decreases integrin alpha3beta1-expression and cell adhesion of SV40-transformed human corneal epithelial cells, overview
-
-
?
additional information
?
-
-
stromelysins are enzymatically active against proteoglycans, procollagenase, and fibronectin
-
-
?
additional information
?
-
the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9
-
-
?
additional information
?
-
-
the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9
-
-
?
additional information
?
-
-
MMPs belong to a family of over 20 neutral endopeptidases that are collectively able to cleave all extracellular matrix components as well as many non-extracellular matrix proteins. The stromelysins, MMP-3, MMP-10 and MMP-11, have a domain arrangement similar to that of collagenases, but they do not cleave interstitial collagens
-
-
?
additional information
?
-
-
expression of transin and transin-2 in tumor cells might play a role in tumor invasion
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
the active site of the domain possesses the conserved zinc-binding motif HEXXHXXGXXH, in which the imidazole side chains of His217, His221, and His227 coordinate the catalytic zinc ion
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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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
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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
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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
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TIMP-1
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TIMP-1 from brain is upregulated in in the infarcted tissue compared to healthy control areas, overview
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tissue inhibitor of metalloproteinases 2
TIMP-2, the protein is expressed in HEK 293E cells
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tissue inhibitor of metalloproteinases 2
TIMP-2, conserved mechanism of inhibition, interactions and conformation analysis, and structural changes induced by complex formation with the enzyme's catalytic domain, detailed overview
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
purified proMMP-10-catalytic domain is activated overnight in the presence of the organomercurial compound 4-aminophenyl mercuric acetate
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additional information
-
purified proMMP-10-catalytic domain is activated overnight in the presence of the organomercurial compound 4-aminophenyl mercuric acetate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2
-
-
additional information
additional information
enzyme cleavage site specificity and kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.8
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2
-
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
inhibition kinetics using the isolated enzyme's catalytic domain, overview
-
additional information
additional information
-
inhibition kinetics using the isolated enzyme's catalytic domain, overview
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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lymphoma cell, expression of enzyme is induced upon contact of cell with endothelial cells
brenda
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lymphoma cell, expression of enzyme is induced upon contact of cell with endothelial cells. Enzyme expression is also induced following exposure to interleukins IL-4, IL-6, and IL-13, but not IL-1
brenda
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MMP-10 is notably increased in neurons of the ischemic brain but not in healthy areas
brenda
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expression of matrix metalloproteinases MMP-1, MMP-7 and MMP-10 by migrating enterocytes bordering intestinal ulcers
brenda
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transformed embryo cell line, can be induced by a tumor promoter
brenda
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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
brenda
-
MMP-10 protein levels are higher in the tumor tissues than in the adjacent normal tissues
brenda
-
no differences in MMP-10 in the plasma of hypertensive versus normotensive subjects
brenda
HUVEC, quantitative RT-PCR of MMPs, overview
brenda
additional information
-
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
brenda
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in dysplastic epithelium MMP-10 is never expressed in basal keratinocytes
brenda
-
in dysplastic epithelium MMP-10 is never expressed in basal keratinocytes
-
brenda
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alveolar mucosa stromelysin 2/MMP-10 expression is highest in the HIV1- and HIV1+ smokers with early emphysema, where it is significantly higher than in HIV1- healthy smokers, overview
brenda
enzyme Mmp10 is required for maintenance of a highly tumorigenic, cancer-initiating, metastatic stem-like cell population in lung cancer. Mmp10 and Notch4 expression in primary and metastatic lung tumors
brenda
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enzyme Mmp10 is required for maintenance of a highly tumorigenic, cancer-initiating, metastatic stem-like cell population in lung cancer. Mmp10 and Notch4 expression in primary and metastatic lung tumors
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brenda
isolated resident alveolar and bone marrow-derived macrophages (BMDM)
brenda
-
isolated resident alveolar and bone marrow-derived macrophages (BMDM)
-
brenda
-
quantitative detection of pro- and active forms of MMP-10 in blood from healthy subjects of both genders and different ages, overview. MMP-10 and TIMP-2 serum levels are age-dependently decreased. No significant differences among serum MMP-10 results for males versus females
brenda
antibody cross-reactivity due to the extreme similarity between MMP-3 (EC 3.4.24.17) and MMP-10 proteins
brenda
Mus musculus C57BL/KsOlaHsd-Db/+
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antibody cross-reactivity due to the extreme similarity between MMP-3 (EC 3.4.24.17) and MMP-10 proteins
-
brenda
-
head and neck squamous cell carcinoma (HNSCC)
brenda
additional information
-
gene expression of interleukin-1, nerve growth factor, and tumour necrosis factor-alpha does not correlate with matrix metalloproteinase-10 in human nucleus pulposus, but expression of substance P does correlate with MMP-10 expression, overview
brenda
additional information
-
relationships between MMP-10 and TIMP-2 serum profiles, overview
brenda
additional information
MMP10 is overexpressed in the serum and pulmonary arteries of patients with SSc-associated PH, and its blockade alleviates PH in the Fra-2-Tg mouse model. Immunohistochemic analysis
brenda
additional information
-
MMP10 is overexpressed in the serum and pulmonary arteries of patients with SSc-associated PH, and its blockade alleviates PH in the Fra-2-Tg mouse model. Immunohistochemic analysis
brenda
additional information
-
stromelysin-2 expression analysis in 81 specimens, including 61 head and neck squamous cell carcinomas (different histological grades) and 20 non neoplastic epithelium, evaluation by immunohistochemistry
brenda
additional information
-
with increasing epidermal hyperplasia, the amount of inflammatory infiltration increased and MMP-10 is also detected in suprabasal keratinocytes as the mice aged
brenda
additional information
strong positive correlation between tumor Mmp10 expression and metastatic behavior in many human tumor types. Oncosphere cultures exhibit Mmp10-dependent tumor-initiating activity in vivo
brenda
additional information
-
strong positive correlation between tumor Mmp10 expression and metastatic behavior in many human tumor types. Oncosphere cultures exhibit Mmp10-dependent tumor-initiating activity in vivo
brenda
additional information
MMP10 (stromelysin-2) is not expressed in developing or normal adult tissues, including lung
brenda
additional information
-
MMP10 (stromelysin-2) is not expressed in developing or normal adult tissues, including lung
brenda
additional information
MMP10 is overexpressed in the serum and pulmonary arteries of patients with SSc-associated PH, and its blockade alleviates PH in the Fra-2-Tg mouse model. Immunohistochemic analysis
brenda
additional information
-
MMP10 is overexpressed in the serum and pulmonary arteries of patients with SSc-associated PH, and its blockade alleviates PH in the Fra-2-Tg mouse model. Immunohistochemic analysis
brenda
additional information
-
strong positive correlation between tumor Mmp10 expression and metastatic behavior in many human tumor types. Oncosphere cultures exhibit Mmp10-dependent tumor-initiating activity in vivo
-
brenda
additional information
-
MMP10 (stromelysin-2) is not expressed in developing or normal adult tissues, including lung
-
brenda
additional information
-
with increasing epidermal hyperplasia, the amount of inflammatory infiltration increased and MMP-10 is also detected in suprabasal keratinocytes as the mice aged
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
evolution
sequence comparisons of MMP-3 (EC 3.4.22.17) and MMP-10, high similarity
evolution
Mus musculus C57BL/KsOlaHsd-Db/+
-
sequence comparisons of MMP-3 (EC 3.4.22.17) and MMP-10, high similarity
-
malfunction
-
association between MMP-9, MMP-10, TIMP-1, and MMP-9/TIMP-1 ratios and parameters of sepsis severity, overview
malfunction
-
MMP-10 may be important in the initial stages of squamous cell cancer progression and induced in the stroma relating to the general host-response reaction to skin cancer. Contribution of MMP-10 to squamous cell cancer development in the FVB/NTg(KRT5-Nfkbia)3Rto mouse line, overview
malfunction
MMP-10 plays a critical role in VEGF-induced angiogenesis, overview
malfunction
-
ectopic overexpression of MMP-10 promotes the invasion of head and neck squamous cell carcinoma cells, and knockdown of MMP-10 suppressed the invasion of head and neck squamous cell carcinoma cells
malfunction
-
Mmp10 knockout mice show a significant reduction in lung tumor number and size after urethane exposure or genetic activation of oncogenic Kras
malfunction
RNAi-mediated knockdown of Mmp10 leads to a loss of stem cell marker gene expression and inhibition of oncosphere growth, clonal expansion, and transformed growth in vitro. Enzyme Mmp10-deficient cultures show a severe defect in tumor initiation
malfunction
in acute Pseudomonas aeruginosa infection, 50% of Mmp10-/- mice die and all show sustained weight loss (morbidity), but lethality and morbidity in Mmp10-/- mice are not due to impaired bacterial clearance. Mmp10-/- mice die due to altered or excessive inflammation
malfunction
-
oropharyngeal aspiration of long multiwalled carbon nanotubes (MWCNTs) (0.08 mg/mouse) by wild-type mice induces expression of Mmp10 mRNA, which is accompanied by a robust inflammatory response characterized by elevated expression of Tnfa, Il6, and Il1b. In Mmp10-/- mice, absence of MMP-10 leads to impaired pulmonary clearance of MWCNTs and reduced macrophage cell survival. Exposure of wild-type bone marrow-derived macrophages (BMDMs) and alveolar macrophages to MWCNTs caused a rapid, dose-dependent upregulation of Mmp10 mRNA expression, which was accompanied by expression of pro-inflammatory products (Il6 and Il1b). These products were further enhanced in Mmp10-/- macrophages, resulting in increased caspase-3-dependent cell death compared with wild-type cells. Absence of Mmp-10 confers sensitivity to apoptosis in BMDMs without an increase in endocytosis
malfunction
the gene for matrix metalloproteinase 10 is the most significantly upregulated gene in patients with systemic sclerosis (SSc)-associated pulmonary hypertension (PH). Lack of effect of MMP10 blockade on the development and severity of pulmonary fibrosis but reversal of PH in Fra-2-Tg mice, lung expression patterns. Substantial increase in the levels of MMP10 in the remodeled vessels of Fra-2-Tg mice, efficacy of MMP10 inhibition on the development of PH in Fra-2-Tg mice. MMP10 inhibition acts through the regulation of cell proliferation and apoptosis to alleviate vascular remodeling and the signs of PH
malfunction
the gene for matrix metalloproteinase 10 is the most significantly upregulated gene in patients with systemic sclerosis (SSc)-associated pulmonary hypertension (PH). MMP10 inhibition acts through the regulation of cell proliferation and apoptosis to alleviate vascular remodeling and the signs of PH
malfunction
-
MMP-10 may be important in the initial stages of squamous cell cancer progression and induced in the stroma relating to the general host-response reaction to skin cancer. Contribution of MMP-10 to squamous cell cancer development in the FVB/NTg(KRT5-Nfkbia)3Rto mouse line, overview
-
malfunction
-
RNAi-mediated knockdown of Mmp10 leads to a loss of stem cell marker gene expression and inhibition of oncosphere growth, clonal expansion, and transformed growth in vitro. Enzyme Mmp10-deficient cultures show a severe defect in tumor initiation
-
malfunction
-
in acute Pseudomonas aeruginosa infection, 50% of Mmp10-/- mice die and all show sustained weight loss (morbidity), but lethality and morbidity in Mmp10-/- mice are not due to impaired bacterial clearance. Mmp10-/- mice die due to altered or excessive inflammation
-
metabolism
-
MMP-10 is a potent activator of a number of MMP pro-enzymes, including pro-MMP-1, -7, -8, -9 and -13
metabolism
fibroblast secretome cleavage analysis, analysis of the MMP10 substrate degradome, overview
metabolism
matrix metalloproteinases (MMPs) play central roles in vertebrate tissue development, remodeling, and repair. 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
metabolism
macrophage MMP10 promotes the ability of M2 macrophages to clear scar tissues in normal skin wounds by controlling the expression of collagenolytic MMPs, particularly MMP13
metabolism
-
fibroblast secretome cleavage analysis, analysis of the MMP10 substrate degradome, overview
-
metabolism
-
macrophage MMP10 promotes the ability of M2 macrophages to clear scar tissues in normal skin wounds by controlling the expression of collagenolytic MMPs, particularly MMP13
-
physiological function
-
matrix metalloproteinases play a role in infectious diseases through extracellular matrix degradation, which favors the migration of immune cells from the bloodstream to sites of inflammation
physiological function
-
MMP-10 may be important in the initial stages of squamous cell cancer progression and induced in the stroma relating to the general host-response reaction to skin cancer. MMP-10 is expressed in Bowen's disease
physiological function
-
role for MMP-10 in the TGF-beta- and EGF-stimulated collagen remodelling process
physiological function
-
MMP-10 efficiently reduces infarct size in experimental stroke by enhancing fibrinolysis via a thrombin-activatable fibrinolysis inhibitormediated mechanism
physiological function
-
MMP-10 plays an important role in the invasion and metastasis of head and neck squamous cell carcinoma
physiological function
role for the enzyme in the maintenance, tumorigenicity, and proliferation of mouse lung cancer stem-like cells, overview
physiological function
the enzyme functions in skeletal development, wound healing, and vascular remodeling. It is also implicated in lung tumorigenesis and tumor progression. Regulation of enzyme MMP-10 by tissue inhibitors of metalloproteinases
physiological function
the enzyme performs ectodomain shedding of platelet-derived growth factor receptor alpha as well as sequential processing of type I collagen
physiological function
-
the enzyme plays an important role in esophageal squamous cell carcinoma progression in the early stage
physiological function
MMP10 regulates macrophage activation. macrophage MMP10 serves a beneficial function in response to acute Pseudomonas aeruginosa infection. Whereas wild-type mice survive infection with minimal morbidity, while 50% of Mmp10-/- mice die and all show sustained weight loss (morbidity). MMP10 serves a beneficial role in response to acute infection by moderating the pro-inflammatory response of resident and infiltrating macrophages. MMP10 serves a protective role in acute infection by moderating the pro-inflammatory activity of macrophages
physiological function
-
stromelysin-2 (MMP-10) has roles in modulating macrophage activation and function. MMP-10 facilitates clearance and moderates inflammation and cell death following lung exposure to long multiwalled carbon nanotubes. Multiwalled carbon nanotubes (MWCNTs) are nanomaterials composed of multiple layers of graphene cylinders with unique properties that make them valuable for a number of industries that possibly initiate pathology similar to that of asbestos. MMP-10 protects against MWCNT-associated losses of macrophages via apoptosis, and MMP-10 facilitates clearance of MWCNTs, overview
physiological function
-
the enzyme performs ectodomain shedding of platelet-derived growth factor receptor alpha as well as sequential processing of type I collagen
-
physiological function
-
role for the enzyme in the maintenance, tumorigenicity, and proliferation of mouse lung cancer stem-like cells, overview
-
physiological function
-
MMP10 regulates macrophage activation. macrophage MMP10 serves a beneficial function in response to acute Pseudomonas aeruginosa infection. Whereas wild-type mice survive infection with minimal morbidity, while 50% of Mmp10-/- mice die and all show sustained weight loss (morbidity). MMP10 serves a beneficial role in response to acute infection by moderating the pro-inflammatory response of resident and infiltrating macrophages. MMP10 serves a protective role in acute infection by moderating the pro-inflammatory activity of macrophages
-
additional information
-
gene expression of interleukin-1, nerve growth factor, and tumour necrosis factor-alpha does not correlate with matrix metalloproteinase-10 in human nucleus pulposus, but expression of substance P does correlate with MMP-10 expression, overview
additional information
-
interleukin-10 positively correlates with inhibitor TIMP-1 and MMP-10 in sepsis patients
additional information
-
MMP-10 is not associated with keratinocyte apoptosis or atypia
additional information
transcriptional regulation of MMP-10 by Ets transcription factors
additional information
-
transcriptional regulation of MMP-10 by Ets transcription factors
additional information
-
overexpression of matrix metalloproteinase 10 is associated with poor survival in patients with early stage of esophageal squamous cell carcinoma. Although the overexpression of MMP10 is not significantly associated with disease-specific survival rate for all tested esophageal squamous cell carcinomas, it is significantly associated with poorer disease-specific survival in early stage of esophageal squamous cell carcinomas
additional information
strong positive correlation between tumor Mmp10 expression and metastatic behavior in many human tumor types
additional information
-
strong positive correlation between tumor Mmp10 expression and metastatic behavior in many human tumor types
additional information
the active site of the domain possesses the conserved zinc-binding motif HEXXHXXGXXH, in which the imidazole side chains of His217, His221, and His227 coordinate the catalytic zinc ion, and Glu218 is positioned to function as a general acid/base in the hydrolysis reaction
additional information
-
the active site of the domain possesses the conserved zinc-binding motif HEXXHXXGXXH, in which the imidazole side chains of His217, His221, and His227 coordinate the catalytic zinc ion, and Glu218 is positioned to function as a general acid/base in the hydrolysis reaction
additional information
biologic functions and differentially expressed genes identified by microarray analysis in patients with SSc-associated PH as compared to SSc patients without PH and healthy controls, overview
additional information
-
biologic functions and differentially expressed genes identified by microarray analysis in patients with SSc-associated PH as compared to SSc patients without PH and healthy controls, overview
additional information
peptide specific affinity-purified antibodies. Antibody cross-reactivity due to the extreme similarity between MMP-3 (EC 3.4.24.17) and MMP-10 proteins, lab-made antibodies for MMP-10 (D248/6 or IW13)
additional information
-
peptide specific affinity-purified antibodies. Antibody cross-reactivity due to the extreme similarity between MMP-3 (EC 3.4.24.17) and MMP-10 proteins, lab-made antibodies for MMP-10 (D248/6 or IW13)
additional information
Mus musculus C57BL/KsOlaHsd-Db/+
-
peptide specific affinity-purified antibodies. Antibody cross-reactivity due to the extreme similarity between MMP-3 (EC 3.4.24.17) and MMP-10 proteins, lab-made antibodies for MMP-10 (D248/6 or IW13)
-
additional information
-
MMP-10 is not associated with keratinocyte apoptosis or atypia
-
additional information
-
strong positive correlation between tumor Mmp10 expression and metastatic behavior in many human tumor types
-
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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). MMP10_HUMAN
476
0
54151
Swiss-Prot
Secretory Pathway (Reliability: 1)
MMP10_MOUSE
476
0
53911
Swiss-Prot
Secretory Pathway (Reliability: 1)
MMP10_RAT
476
0
54222
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A061I711_CRIGR
393
0
44367
TrEMBL
other Location (Reliability: 2)
S5SNL7_PINIB
226
0
25498
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6R476_ROSCH
371
0
40509
TrEMBL
Secretory Pathway (Reliability: 4)
TIMP1_HUMAN
207
0
23171
Swiss-Prot
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
synthesized as preproenzyme of 476 amino acids and secreted from cells as the proenzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
additional information
-
potential glycosylation site at Asn100, but is unlikely to be a glycoprotein as it does not bind concanavalin A
proteolytic modification
-
activation of proenzyme by serine proteases such as plasma kallikrein, trypsin, neutrophil elastase, cathepsin G, tryptase or chymase
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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
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
V94G
-
constitutively active mutant, mice expressing the mutant in keratinocytes have no alterations in skin architecture, and the healing rate of skin wounds is normal. Histologically, deposition of new matrix is reduced and keratinocytes at the migrating epidermal tip are scattered, the staining pattern of laminin-5 at the wound site is altered
additional information
additional information
-
mice injected with lymphoma cells constitutively expressing enzyme developed thymic lymphoma more rapidly than those injected with control lymphoma cells
additional information
-
stromelysin-2 deficiency does not affect adipose tissue formation in a mouse model of nutritionally induced obesity, no effect on total body weight or on subcutaneous adipose tissue mass of mice kept on a high fat diet for 15 weeks, while or gonadal adipose tissue development is reduced, phenotype, overview. Significantly reduced MMP-3 expression in MMP-10-deficient adipose tissues not affecting blood vessel size
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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
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme MMP-10 catalytic domain from Escherichia coli strain BL21 (DE3), by anion exchange chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ectopical overexpression of C-terminally Strep-tagged mouse MMP-10 in Hep-G2 cells and in COS-7 cells
expression of the enzyme catalytic domain in Escherichia coli strain BL21 (DE3)
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
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
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
loss or knockdown of transcription factor CHF1/Hey2 in vascular smooth muscle cells leads to increased expression and activity of MMP10 at baseline. CHF1/Hey2 regulates MMP10 expression through multiple E boxes
-
Mmp10 is overexpressed in lung tumors induced by either the smoke carcinogen urethane or oncogenic Kras
-
neuronal MMP-10 is upregulated after stroke in brain in the infarcted tissue compared to healthy control areas, overview
-
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
stromelysin-2 is slightly downregulated in obese adipose tissue compared to non-obese adipose tissue
-
strong positive correlation between tumor Mmp10 expression and metastatic behavior in many human tumor types
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
strong positive correlation between tumor Mmp10 expression and metastatic behavior in many human tumor types
strong positive correlation between tumor Mmp10 expression and metastatic behavior in many human tumor types
-
-
the gene for matrix metalloproteinase 10 is the most significantly upregulated gene in patients with systemic sclerosis (SSc)-associated pulmonary hypertension (PH)
the gene for matrix metalloproteinase 10 is the most significantly upregulated gene in patients with systemic sclerosis (SSc)-associated pulmonary hypertension (PH)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
medicine
diagnostics
-
circulating MMP-10 may be useful to identify subclinical atherosclerosis in subjects free from cardiovascular disease
diagnostics
-
MMP10 is a potential oral cancer marker in neck tissue and gingiva
diagnostics
-
MMP10 expression in tumor tissues is a potential independent prognostic factor for early stage esophageal squamous cell carcinoma patients
diagnostics
diagnostic value of MMP-10 in patients with systemic sclerosis (SSc)-associated pulmonary hypertension (PH)
diagnostics
diagnostic value of MMP-10 in patients with systemic sclerosis (SSc)-associated pulmonary hypertension (PH)
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
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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
brenda
Breathnach, R.; Matrisian, L.M.; Gesnel, M.C.; Staub, A.; Leroy, P.
Sequences coding for part of oncogene-induced transin are highly conserved in a related rat gene
Nucleic Acids Res.
15
1139-1151
1987
Rattus norvegicus
brenda
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
brenda
Nicholson, R.; Murphy, G.; Breathnach, R.
Human and rat malignant-tumor-associated mRNAs encode stromelysin-like metalloproteinases
Biochemistry
28
5195-5203
1989
Homo sapiens
brenda
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
brenda
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
brenda
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
brenda
Van Themsche, C.; Alain, T.; Kossakowska, A.E.; Urbanski, S.; Potworowski, E.F.; St-Pierre, Y.
Stromelysin-2 (matrix metalloproteinase 10) is inducible in lymphoma cells and accelerates the growth of lymphoid tumors in vivo
J. Immunol.
173
3605-3611
2004
Mus musculus
brenda
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
brenda
Krampert, M.; Bloch, W.; Sasaki, T.; Bugnon, P.; Ruelicke, T.; Wolf, E.; Aumailley, M.; Parks, W.C.; Werner, S.
Activities of the matrix metalloproteinase stromelysin-2 (MMP-10) in matrix degradation and keratinocyte organization in wounded skin
Mol. Biol. Cell
15
5242-5254
2004
Mus musculus
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Lijnen, H.R.; Van Hoef, B.; Rodriguez, J.A.; Paramo, J.A.
Stromelysin-2 (MMP-10) deficiency does not affect adipose tissue formation in a mouse model of nutritionally induced obesity
Biochem. Biophys. Res. Commun.
389
378-381
2009
Mus musculus
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Wu, L.; Chien, W.M.; Hartman, M.E.; Moussavi-Harami, F.; Liu, Y.; Chin, M.T.
Regulation of MMP10 expression by the transcription factor CHF1/Hey2 is mediated by multiple E boxes
Biochem. Biophys. Res. Commun.
415
662-668
2011
Mus musculus
brenda
Orbe, J.; Barrenetxe, J.; Rodriguez, J.A.; Vivien, D.; Orset, C.; Parks, W.C.; Birkland, T.P.; Serrano, R.; Purroy, A.; Martinez de Lizarrondo, S.; Angles-Cano, E.; Paramo, J.A.
Matrix metalloproteinase-10 effectively reduces infarct size in experimental stroke by enhancing fibrinolysis via a thrombin-activatable fibrinolysis inhibitor-mediated mechanism
Circulation
124
2909-2919
2011
Mus musculus
brenda
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
brenda
Regala, R.; Justilien, V.; Walsh, M.; Weems, C.; Khoor, A.; Murray, N.; Fields, A.
Matrix metalloproteinase-10 promotes Kras-mediated bronchio-alveolar stem cell expansion and lung cancer formation
PLoS ONE
6
e26439
2011
Mus musculus
brenda
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
brenda
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
brenda
Schlage, P.; Egli, F.; Nanni, P.; Wang, L.; Kizhakkedathu, J.; Apte, S.; Keller, U.
Time-resolved analysis of the matrix metalloproteinase 10 substrate degradome
Mol. Cell. Proteomics
13
580-593
2014
Mus musculus (O55123), Mus musculus BALB/c (O55123)
brenda
Justilien, V.; Regala, R.; Tseng, I.; Walsh, M.; Batra, J.; Radisky, E.; Murray, N.; Fields, A.
Matrix metalloproteinase-10 is required for lung cancer stem cell maintenance, tumor initiation and metastatic potential
PLoS ONE
7
e35040
2012
Mus musculus (O55123), Mus musculus, Mus musculus C57BL/6 (O55123)
brenda
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)
brenda
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
brenda
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
brenda
Vandivort, T.C.; Birkland, T.P.; Domiciano, T.P.; Mitra, S.; Kavanagh, T.J.; Parks, W.C.
Stromelysin-2 (MMP-10) facilitates clearance and moderates inflammation and cell death following lung exposure to long multiwalled carbon nanotubes
Int. J. Nanomedicine
12
1019-1031
2017
Mus musculus
brenda
McMahan, R.S.; Birkland, T.P.; Smigiel, K.S.; Vandivort, T.C.; Rohani, M.G.; Manicone, A.M.; McGuire, J.K.; Gharib, S.A.; Parks, W.C.
Stromelysin-2 (MMP10) moderates inflammation by controlling macrophage activation
J. Immunol.
197
899-909
2016
Mus musculus (O55123), Mus musculus, Mus musculus C57BL/6J (O55123)
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Mirastschijski, U.; Dinesh, N.; Baskaran, S.; Wedekind, D.; Gavrilovic, J.; Murray, M.Y.; Bevan, D.; Kelm, S.
Novel specific human and mouse stromelysin-1 (MMP-3) and stromelysin-2 (MMP-10) antibodies for biochemical and immunohistochemical analyses
Wound Repair Regen.
27
309-323
2019
Mus musculus (O55123), Mus musculus, Mus musculus C57BL/KsOlaHsd-Db/+ (O55123)
brenda
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Release 2023.1 (January 2023)
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