3.4.24.23: matrilysin
This is an abbreviated version!
For detailed information about matrilysin, go to the full flat file.
Word Map on EC 3.4.24.23
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3.4.24.23
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metalloproteinases
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mmp-2
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metastasis
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timp-1
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colorectal
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fibrosis
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collagen
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endothelial
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node
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gelatinase
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e-cadherin
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clinicopathological
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zymography
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interstitial
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gastric
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epithelium
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tumour
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adenocarcinoma
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pulmonary
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basement
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prostate
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invasiveness
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tumorigenesis
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beta-catenin
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gelatin
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carcinogenesis
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resect
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mt1-mmp
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cyclin
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c-myc
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adenoma
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plasminogen
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transwell
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osteopontin
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metalloelastase
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stromelysin-1
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laminin-5
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hemopexin-like
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pharmacology
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upa
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drug development
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alpha-defensins
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collagenase-3
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analysis
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medicine
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diagnostics
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gelatinolytic
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matrix-degrading
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paneth
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membrane-type
- 3.4.24.23
- metalloproteinases
- mmp-2
- metastasis
- timp-1
- colorectal
- fibrosis
- collagen
- endothelial
- node
- gelatinase
- e-cadherin
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clinicopathological
-
zymography
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interstitial
- gastric
- epithelium
- tumour
- adenocarcinoma
- pulmonary
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basement
- prostate
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invasiveness
- tumorigenesis
- beta-catenin
- gelatin
- carcinogenesis
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resect
- mt1-mmp
- cyclin
- c-myc
- adenoma
- plasminogen
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transwell
- osteopontin
- metalloelastase
- stromelysin-1
- laminin-5
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hemopexin-like
- pharmacology
- upa
- drug development
- alpha-defensins
- collagenase-3
- analysis
- medicine
- diagnostics
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gelatinolytic
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matrix-degrading
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paneth
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membrane-type
Reaction
Cleavage of Ala14-/-Leu and Tyr16-/-Leu in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha2(I) > alpha1(I) =
Synonyms
cyclic matrix metalloproteinase, human matrix metalloproteinase 7, matrilysin, matrilysin 1, matrilysin-1, Matrin, matrix metallopeptidase 7, matrix metalloprotease-7, Matrix metalloproteinase 7, Matrix metalloproteinase pump 1, Matrix metalloproteinase-7, matrix-metalloproteinase-7, metalloproteinase-7, MMP, MMP 7, MMP-7, MMP7, More, Proteinase, metallo-, pump-1, Proteinase, PUMP-1, PUMP, PUMP-1, Pump-1 protease, Putative (or punctuated) metalloproteinase-1, Putative metalloproteinase, Uterine metalloendopeptidase, Uterine metalloproteinase
ECTree
3.4.24.23 matrilysinAdvanced search results
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results (Source Tissue
Source Tissue on EC 3.4.24.23 - matrilysin
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SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
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immunohistochemical expression analysis of MMP-7 in the tumor epithelium and stroma, overview
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immunohistochemical expression analysis of MMP-7 in the tumor epithelium and stroma, overview
MMP-7 activity is higher in amnion from premature rupture of membranes compared to cesarean delivery, overview
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immunohistochemic detection of MMP7 expression in biliary tract cancer, semi-quantitative RT-PCR and real-time RT-PCR, overview
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the matrix metalloproteinases MMP-2, MMP-3, MMP-7, MMP-9, and MMP-13 are highly expressed in the tumor-bone microenvironment, and, of these, MMP-7 and MMP-9 are found to be localized to bone-resorbing osteoclasts in human breast-to-bone metastases
early stage primary cancers, MMP-7 correlates with breast cancer development, overexpression of MMP-7 and ErbB4, overview
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induction of enzyme expression by TNF-alpha and interleukin IL-1beta
MMP7 is secreted mainly by tumor cells instead of matrix cells in colorectal cancer
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expression of matrix metalloproteinases MMP-1, MMP-7 and MMP-10 by migrating enterocytes bordering intestinal ulcers
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low expression of MMP-7, which is induced by physiological processes such as wound healing, but also malignant transformation of epidermal cells
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i.e. ELF, proMMP-7 protein is not detectable in any of the 3 HIV1- groups, including HIV1- smokers with early emphysema. In contrast, ELF pro-MMP-7 is readily detectable in the ELF of HIV1+ smokers with early emphysema
expression and activity of MMP-7 in fetal membranes during premature rupture of membranes, immunohistochemic analysis, overview
MMP-7 expression analysis of 106 different samples, higher enzyme levels in squamous compared to adenocarcinomas, MMP-7 expression increases the cell proliferation and is correlated to Wnt1 expression,overview
high constitutive secretion of proMMP-7 in the EAC cell line, dependent on phosphatidylinositol (PI) 3-kinase, inhibited by PI 3-kinase inhibitor LY294002 but not by inhibitors of protein kinase C, or MAP kinase activation
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strong expression of MMP-7 in epithelial dysplasia with a two-phase appearance: a clear demarcation of MMP-7-immunopositive (+) lower dysplastic/basaloid cells from non-positive upper keratinized cells
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exclusive detection of active enzyme in conditioned medium of dissociated cells, detection of proenzyme only in conditioned medium of non-dissociated cells. Enzyme protein is greatly reduced by treatment with the epidermal growth factor receptor inhibitor AG1478 and the mitogen activated protein kinase kinase inhibitor U0126
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MMP-7 expression analysis semiquantitatively by immunohistochemistry in prostate cancer. E1AF, an ets-oncogene family transcription factor, expression correlates with that of MMP-7
invasive prostate cancer cells, high enzyme expression level
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induction of enzyme expression by TNF-alpha and interleukin IL-1beta
additional information
MMP-7 expression analysis, the expression level is increased compared to normal cells
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carcinoma in situ, MMP-7+ cells are spread over the whole epithelial layer
MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, overview
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MMP7 is induced upon mucosal injury in several tissues, e.g. in colon mucosa, overview
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MMP-7 overexpression in carcinomas compared to healthy tissue, mucosal, tubular, tubulovillous, or villous colonic adenoma subtypes, MMP-7 expression analysis, overview
MMP7 s generally not expressed by normal differentiated epithelial colon cells, but has been shown to be up-regulated in human colon adenomas and adenocarcinomas
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more expression of cyclooxygenase 2 and matrix metalloproteinase 7 is correlated in colorectal cancer, analysis of COX-2 and MMP-7 RNA in feces from patients, overview
MMP7 is secreted mainly by tumor cells instead of matrix cells in colorectal cancer
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YAP is a critical regulatory factor in upregulating MMP-7 expression on the stiffer substrate in colorectal cancer
sprouting, of different cancers, the endothelial enzyme is associated with CD34 and/or CD105 expression
pro-MMP-7 is diffusely distributed in epithelial cells of the endometrium, while the mature enzyme is located at the plasma membrane
vaginal-cervical epithelial cells secrete constitutively MMP-7 into the luminal solution
primary airway epithelial cell air-liquid interface culture. Tissue inhibitor of metalloproteinase TIMP-1 and matrilysin co-localize and co-immunoprecipitate in wounded primary airway epithelial cultures. TIMP-1-deficient cultures migrate faster, and epithelial cells spread to a greater extent compared with wild-type cultures. TIMP-1 also inhibits matrilysin-mediated cell migration and spreading in vitro. In vivo, TIMP-1 deficiency enhances airway re-epithelialization after naphthalene injury. TIMP-1 and matrilysin co-localize in airway epithelial cells adjacent to the wound edge
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expression of MMP-7 in the normal oral mucosal epithelium is restricted mainly to the parabasal layers
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primary specimen, overexpression of MMP-7, realtime PCR, RT-PCR or Western blotting analysis
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wild-type HCT-116 and oxaliplatin-resistant RHCT-116 p53 positive- and p53 negative cell lines
LN5 and MMP7 are coexpressed in HT29 cells, as well as in HT29 xenograft tumors and human colorectal adenocarcinomas, distribution, overview
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MMP-7 expression analysis in estrogen-dependently proliferating cells, overview
higher expression in epithelium compared to stroma, expression in proximal and distal convoluted tubules and collecting duct, and weakly in renal corpuscles and mesangial cells, podocytes, and Bowman's capsule of glomerules, overview
MMP-7 is induced in renal tubules following ischemia/reperfusion injury or cisplatin administration, and in folic acid-induced acute kidney injury (AKI)
MMP-7 is induced in renal tubules following ischemia/reperfusion injury or cisplatin administration, and in folic acid-induced acute kidney injury (AKI)
expression analysis in kidneys after transplantation, overview
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HIV1- smokers with early emphysema have a trend toward increased relative alveolar matrilysin/MMP-7 gene expression compared with HIV1- healthy smokers and HIV1- healthy nonsmokers. HIV1+ smokers with early emphysema have significantly higher relative expression of alveolar mucosa MMP-7 than both HIV1- healthy smokers and HIV1- healthy nonsmokers. HIV1+ smokers with early emphysema have increased expression over and above the increase in HIV- smokers with early emphysema, overview
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expression levels of fibulin-5 and MMP-7 are inversely correlated in lung tumors
esophageal, expression of proMMP-7 but not secretion in myofibroblasts
infundibulum, magnum, isthmus, and shell gland. Developmental changes, overview
Gallus gallus Hy-Line Brown
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infundibulum, magnum, isthmus, and shell gland. Developmental changes, overview
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higher expression of MMP-7 in RCC subtypes, i.e. chromophobe, renal papillary and oncocytomas, compared to benign epithelial neoplasias, overview
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analysis of expression of MMP-7 by immunohistochemistry, overview
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from patients from Canada and Finland. Average indices of MMP-7 in epithelial cells are higher than in myoepithelial cells, but a significant association to the disease does not exist
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cancer patients have higher serum levels of MMP-3 and MMP-7 than those with duodenal ulcer and gastritis, overview
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circulating MMP-7 serum concentration is significantly elevated in patients with distant metastasis of prostate cancer, overview
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the serum MMP-7 level is significantly higher in the patients with cholangiocarcinoma compared to benign biliary tract disease patients
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MMP-7 positivity is reduced from carcinoma cells but instead appears in stromal cells
stimulated by VEGF, no MMP-7 expression in unstimulated HUVEC
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MMP-7 levels in eutopic and ectopic endometriose, overview. MMP-7 expression levels are significantly higher in the endometrial epithelial cells from women with deep infiltrating endometriosis compared with those isolated from the endometria of patients with only superficial peritoneal endometriosis, uterine myomas or normal endometrium, in the proliferative, late secretory and menstrual phases. MMP-7 protein expression is detected in the ectopic endometrial epithelial cells of samples of deep infiltrating endometriosis, of ovarian endometriosis, of black peritoneal lesions, and of red peritoneal lesions. MMP-7 protein expression in epithelial cells is significantly higher in red peritoneal lesions compared with that of deep infiltrating endometriosis, ovarian endometriosis and black peritoneal lesions, in all phases of the menstrual cycle, quantitative real-time RT-PCR and immunohistochemical analysis, overview
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MMP7 expression during the menstrual cycle in the human endometrium and fallopian tube, overview. The level of MMP7 secretion is highest in the secretory phase, although the difference from the proliferative phase does not reach statistical significance, neither in the endometrium nor in the fallopian tube
additional information
quantitative enzyme tissue expression analysis in the chicken oviduct during maturation. The MMP-7 mRNA expression is significantly higher on plastic than that on a gel substrate
additional information
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quantitative enzyme tissue expression analysis in the chicken oviduct during maturation. The MMP-7 mRNA expression is significantly higher on plastic than that on a gel substrate
additional information
Gallus gallus Hy-Line Brown
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quantitative enzyme tissue expression analysis in the chicken oviduct during maturation. The MMP-7 mRNA expression is significantly higher on plastic than that on a gel substrate
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additional information
MMP-7 content is elevated in tumors compared to helathy mucosa
additional information
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MMP-7 content is elevated in tumors compared to helathy mucosa
additional information
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heparan sulfate proteoglycans, especially perlecan, are extracellular docking molecules for MMP-7
additional information
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matrilysin-1 is expressed in injured lung and in cancer but not in normal epithelia and cell line BEAS-2B
additional information
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MMP-7 activity is significantly higher in atherosclerotic plaques than internal mammary arteries
additional information
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MMP-7 expression analysis in gastric cancer cell lines, overview
additional information
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MMP-7 expression analysis in healthy persons and liver cirrhosis patients, overview
additional information
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MMP7 basal expression is higher in the oxaliplatin-resistant compared to the parental cell lines
additional information
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quantitative enzyme expression in ulcerative colitis patients and healthy humans, 35 samples, overview
additional information
in colon cancer in neoplastic cells but not in stromal cells, enzyme expression and immunohistochemic analysis, overview
additional information
profile of metalloproteinases expression changes during colorectal cancer development, expecially of MMP-7, MMP-9, MMP-1, and their inhibitor TIMP-1, overview
additional information
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profile of metalloproteinases expression changes during colorectal cancer development, expecially of MMP-7, MMP-9, MMP-1, and their inhibitor TIMP-1, overview
additional information
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MMP-7 is overexpressed in a variety of epithelial cancers, such as stomach, liver, pancreatic, and colon cancer
additional information
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pulmonary CD103+ dendritic cells are significantly increased in bleomycin-injured wild-type compared with Mmp7-/- mice, and CD103+ leukocytes
additional information
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pulmonary CD103+ dendritic cells are significantly increased in bleomycin-injured wild-type compared with Mmp7-/- mice, and CD103+ leukocytes
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additional information
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no MMP-7 in gingival fibroblasts isolated and cultured from gingiva. Coculture of aorta fiboblasts with fibroblasts from gingiva lead to inhibition of the secreted MMP-7 and reduction of its level at least in part due to the formation of MMP-7/TIMP-1 complexes, after 21 days MMP-7 is completely inhibited, the effect is less with dermal fibroblasts, overview. siRNA TGF-beta1 inhibits the inhibition efficiency of GF on MMP-7
