3.4.24.17: stromelysin 1
This is an abbreviated version!
For detailed information about stromelysin 1, go to the full flat file.
Word Map on EC 3.4.24.17
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3.4.24.17
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metalloproteinases
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mmp-1
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cartilage
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arthritis
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joint
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osteoarthritis
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rheumatoid
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synovial
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chondrocytes
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necrosis
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timps
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articular
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gelatinase
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tnf
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interleukin-1
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knee
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zymography
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degeneration
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aggrecan
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proteoglycans
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c-reactive
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interstitial
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gelatin
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plasminogen
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proteinases
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cox-2
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synoviocytes
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il-1beta
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fibroblast-like
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cruciate
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intervertebral
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ligament
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matrilysin
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pulposus
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matrix-degrading
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adamts-4
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synovitis
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thrombospondin
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intra-articular
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subchondral
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emmprin
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chondroprotective
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photoaging
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collagenases
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diagnostics
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medicine
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aggrecanase
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prommp-9
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neoepitope
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gelatinolytic
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mt1-mmp
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collagenolytic
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drug development
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analysis
- 3.4.24.17
- metalloproteinases
- mmp-1
- cartilage
- arthritis
- joint
- osteoarthritis
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rheumatoid
- synovial
- chondrocytes
- necrosis
- timps
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articular
- gelatinase
- tnf
- interleukin-1
- knee
-
zymography
- degeneration
- aggrecan
- proteoglycans
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c-reactive
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interstitial
- gelatin
- plasminogen
- proteinases
- cox-2
- synoviocytes
- il-1beta
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fibroblast-like
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cruciate
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intervertebral
- ligament
- matrilysin
- pulposus
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matrix-degrading
- adamts-4
- synovitis
- thrombospondin
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intra-articular
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subchondral
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emmprin
-
chondroprotective
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photoaging
- collagenases
- diagnostics
- medicine
- aggrecanase
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prommp-9
-
neoepitope
-
gelatinolytic
- mt1-mmp
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collagenolytic
- drug development
- analysis
Reaction
preferential cleavage where P1', P2' and P3' are hydrophobic residues =
Synonyms
Collagen-activating protein, Collagenase activating protein, matrix metalloprotease-3, Matrix metalloproteinase 3, matrix metalloproteinase-3, matrixin, MMP-3, MMP3, Neutral proteoglycanase, Procollagenase activator, Proteoglycanase, PTR1 protein, ST1, Stromelysin, stromelysin-1, Transin
ECTree
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analysis
diagnostics
the enzyme, together with gelolin, is a potential biomarker for Alzheimer's disease
drug development
human enzyme MMP-3, i.e. stromelysin-1, is an anti-cancer drug target
medicine
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generation of specific recombinant human monoclonal antibody SP3, which may serve as building block for the development of antibody-based therapy strategies in mouse models of pathology
analysis
unspecific staining in tissue sections of both animal strains with commercial anti-MMP-3 antibody JM3523 and positive but enzyme unspecific staining with the anti-MMP-3 antibody MAB 548 in both MMP-3 wild-type and MMP-3-deficient mouse skin wounds
analysis
Mus musculus BL10
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unspecific staining in tissue sections of both animal strains with commercial anti-MMP-3 antibody JM3523 and positive but enzyme unspecific staining with the anti-MMP-3 antibody MAB 548 in both MMP-3 wild-type and MMP-3-deficient mouse skin wounds
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analysis
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generation of specific recombinant human monoclonal antibody SP3, which may serve as building block for the development of antibody-based therapy strategies in mouse models of pathology
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attractive target for pharmaceutical design, implicated in diseases such as arthritis and cancer
medicine
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important target for inhibitor design and synthesis because of the widespread implications in arthritis, cancer, and cardiovascular disease
medicine
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MMP inhibitor development is the target of considerable effort within the pharmaceutical industry, MMP activity can contribute to the pathologies of cancer invasion and metastasis, arthritis, autoimmune disease, tissue ulceration, or cardiovascular disease
medicine
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MMP proteolysis contributes to tissue degeneration and inflammation in osteo and rheumatoid arthritis and may also play a role in the spread of such diseases, abnormally high concentrations of MMPs have been identified in human tissue surrounding invasive carcinomas, indicating a local imbalance in the MMP-TIMP equilibrium which directly enables tumor metastasis through EMP degradation and blood vessel formation
medicine
overexpression of MMps is associated with a variety of diseases ranging from periodontal disease and arthritis to tumor invasion and metastasis
medicine
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proteolytic activity of the enzyme is precisely regulated by endogenous tissue inhibitors, disruption of this balance results in diseases such as arthritis, atherosclerosis, tumour growth and metastasis
medicine
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development of natural pharmacological inhibitors of enzyme: Proenzyme is proteolytically activated by plasmin. C18 unsaturated fatty acids are inhibitory, with elaidic acid totally abolishing the activation. Inhibitory effect result from binding of unsaturated fatty acids to kringle 5
medicine
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during gastric ulcer healing, enzyme expression as well as matrix metalloproteinase MMP-2 and MMP-13 are induced in stromal cells of the gastric mucosa bordering the ulcer. Enzyme mRNA is confined to the upper layers of the granulation tissue
medicine
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enzyme may be involved in the pathogenesis of endometriosis. Endometrial expression of enzyme, matrix metalloproteinases MMP-2 and MMP-11 and tissue inhibitor metalloproteinases TIMP-1 and TIMP-2 are similar in women with endometriosis and in those with peritoneal endometriosis. Expression of enzyme and matrix metalloproteinases MMP-2 and MMP-11 is higher in colorectal endometriosis than in ovarian and peritoneal endometriosis
medicine
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enzyme overexpression im lymphoma transfectants significantly improves their ability to migrate through the matrix. Animals injected with lymphoma cells expressing enzyme constitutively develop thymic lymphoma more rapidly than those injected with control cells. Local expression of enzyme promotes lymphoma progression
medicine
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no significant elevation in serum levels of enzyme and tissue inhibitor proteinase TIMP-1 of patients with malignant melanoma compared to control. Enzyme levels are significantly different in sera of males and females
medicine
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significantly higher levels of enzyme, soluble Fas and soluble Fas ligand are found in sera from patients with active untreated adult onset Stills disease compared to healthy control. Serum levels of enzyme, soluble Fas and soluble Fas ligand fluctuate and are parallel to disease activity
medicine
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wild-type and enzyme null mutant animals, chemical carcinogenesis by 1-methyl-3-nitro-1-nitroso-guanidine or by 7,12-dimethylbenz[a]anthracene and 12-O-tetradecanoylphorbol-13-acetate. No difference in tumor onset or incidence between wild-type and enzyme null mutant animal, but tumors originating on mutant mice have enhanced initial tumor growth coupled with with an elevated proliferative index and reduced vasculature density
medicine
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the 5A/6A polymorphism of the MMP3 gene influences arterial remodeling of the common carotid artery in healthy subjects, but not in patients with diabetes mellitus. Therefore, the significance of the 5A/6A polymorphism as a marker of risk in this high cardiovascular risk population seems to be somehow blunted
medicine
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serum MMP-3 is significantly elevated in ankylosing spondylitis patients with active disease