Information on EC 3.4.24.22 - stromelysin 2

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The expected taxonomic range for this enzyme is: Euarchontoglires

EC NUMBER
COMMENTARY
3.4.24.22
-
RECOMMENDED NAME
GeneOntology No.
stromelysin 2
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Similar to stromelysin 1, but action on collagen types III, IV and V is weak
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Matrix metalloproteinase 10
-
-
-
-
Matrix metalloproteinase 10
-
-
Matrix metalloproteinase-10
-
-
-
-
Matrix metalloproteinase-10
-
-
MMP-10
-
-
-
-
MMP-10
P09238
-
MMP-10
Mus musculus ICR
-
-
-
MMP10
-
-
Proteoglycanase 2
-
-
-
-
stromelysin-2
-
-
stromelysin-2
-
-
stromelysin-2
Mus musculus ICR
-
-
-
Transformation-associated protein 34A
-
-
-
-
Transin 2
-
-
-
-
Transins, 2
-
-
-
-
MMP10
-
-
additional information
-
MMP-10 or stromelysin-2 is a member of the stromelysin family of enzymes
CAS REGISTRY NUMBER
COMMENTARY
140610-48-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
catalytic domain, expression in Escherichia coli
-
-
Manually annotated by BRENDA team
patients with gastric cancer
-
-
Manually annotated by BRENDA team
patients with ischemic colitis
-
-
Manually annotated by BRENDA team
K5-IkBa mice
-
-
Manually annotated by BRENDA team
male C57BL/6J mice
-
-
Manually annotated by BRENDA team
Mus musculus ICR
K5-IkBa mice
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
P09238
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
Mus musculus ICR
-
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
-
physiological function
-
role for MMP-10 in the TGF-beta- and EGF-stimulated collagen remodelling process
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
-
MMP-10 efficiently reduces infarct size in experimental stroke by enhancing fibrinolysis via a thrombin-activatable fibrinolysis inhibitor–mediated mechanism
physiological function
-
MMP-10 plays an important role in the invasion and metastasis of head and neck squamous cell carcinoma
metabolism
-
MMP-10 is a potent activator of a number of MMP pro-enzymes, including pro-MMP-1, -7, -8, -9 and -13
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
P09238
transcriptional regulation of MMP-10 by Ets transcription factors
additional information
Mus musculus ICR
-
MMP-10 is not associated with keratinocyte apoptosis or atypia
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
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
-
type III
-
-
-
Collagen + H2O
?
show the reaction diagram
-
type IV
-
-
-
Collagen + H2O
?
show the reaction diagram
-
type V, not: type I
-
-
-
Elastin + H2O
?
show the reaction diagram
-
-
-
-
-
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
-
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
negligible
-
-
-
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
-
procollagenase + H2O
?
show the reaction diagram
-
-
-
-
?
proMMP-1 + H2O
MMP-1 + propeptide
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
type I, III and V, slight activity with type IV
-
-
-
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
?
-
-
expression of transin and transin-2 in tumor cells might play a role in tumor invasion
-
-
-
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
?
-
-
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
?
-
-
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
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
procollagenase + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
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
?
-
-
expression of transin and transin-2 in tumor cells might play a role in tumor invasion
-
-
-
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
?
-
-
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
?
-
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Zinc
-
zinc metalloenzyme
Zn2+
-
-
Zn2+
-
MMP-10 is a zinc-containing endoproteinase
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
Specific tissue inhibitor of metalloproteinases
-
-
-
TIMP-1
-
increased levels in severe sepsis
-
TIMP-1
-
-
-
TIMP-1
-
TIMP-1 from brain is upregulated in in the infarcted tissue compared to healthy control areas, overview
-
TIMP-2
-
relationships between MMP-10 and TIMP-2 serum profiles, overview
-
TIMP-2
-
highly produced in brain microvessels
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.8
-
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
-
activity against aggrecan at pH 5.5 is double that at pH 6.0
7.5
8
-
azocoll
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
6.0: 25% of activity maximum, 7.5-8.0: activity maximum, azocoll
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
lymphoma cell, expression of enzyme is induced upon contact of cell with endothelial cells
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
subcutaneous and gonadal adipose tissue
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
-
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
Mus musculus ICR
-
-
-
Manually annotated by BRENDA team
-
transformed embryo cell line, can be induced by a tumor promoter
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
-
of Bowen's disease patients
Manually annotated by BRENDA team
-
in dysplastic epithelium MMP-10 is never expressed in basal keratinocytes
Manually annotated by BRENDA team
Mus musculus ICR
-
in dysplastic epithelium MMP-10 is never expressed in basal keratinocytes
-
Manually annotated by BRENDA team
-
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
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
-
increased MMP-10 levels in severe sepsis
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Mus musculus ICR
-
-
-
Manually annotated by BRENDA team
-
in situ detection, overview
Manually annotated by BRENDA team
-
head and neck squamous cell carcinoma (HNSCC)
Manually annotated by BRENDA team
Mus musculus ICR
-
-
-
Manually annotated by BRENDA team
-
at all ages in normal and acanthotic skin
Manually annotated by BRENDA team
-
colon adenocarcinoma cell line
Manually annotated by BRENDA team
P09238
HUVEC, quantitative RT-PCR of MMPs, overview
Manually annotated by BRENDA team
-
induction of enzyme expression by TNF-alpha and EGF
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
-
relationships between MMP-10 and TIMP-2 serum profiles, overview
Manually annotated by BRENDA team
additional information
-
selective cell-dependent MMP secretion
Manually annotated by BRENDA team
additional information
Mus musculus ICR
-
with increasing epidermal hyperplasia, the amount of inflammatory infiltration increased and MMP-10 is also detected in suprabasal keratinocytes as the mice aged
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is secreted
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
synthesized as preproenzyme of 476 amino acids and secreted from cells as the proenzyme
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 56000, pro-MMP-10, SDS-PAGE, x * 42000, mature MMP-10, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
activation of proenzyme by serine proteases such as plasma kallikrein, trypsin, neutrophil elastase, cathepsin G, tryptase or chymase
proteolytic modification
-
pro-MMP-10 is a plasmin substrate
proteolytic modification
-
MMP-10 is activated from a pro-MMP-10 form
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 ACCESSION NO.
LITERATURE
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
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression analysis
-
expression analysis of MMP10 in cancerous and healthy oral tissues, overview
-
MMP-10 DNA and amino acid sequence determination and expression analysis in HUVECs, transcriptional regulation of MMP-10 by Ets transcription factors, overview
P09238
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 ACCESSION NO.
LITERATURE
MMP-10 expression is downregulated with age, 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
P09238
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
-
increased MMP-10 levels in severe sepsis
-
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
P09238
neuronal MMP-10 is upregulated after stroke in brain in the infarcted tissue compared to healthy control areas, overview
-
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
-
stromelysin-2 is slightly downregulated in obese adipose tissue compared to non-obese adipose tissue
-
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
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
down
-
aldose reductase inhibitor, fidarestat, normalizes high-glucose level-mediated suppression of MMP-10 expression, it downregulates MMP-10 expression
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
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
additional information
P09238
MMP-10 knockdown by siRNA
up
-
a high glucose level decreases MMP-10 expression in corneal epithelial cells
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
medicine
-
enzyme overexpression promotes tumor development