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
-
rheumatoid
- synovial
- chondrocytes
- necrosis
- timps
-
articular
- gelatinase
- tnf
- interleukin-1
- knee
-
zymography
- degeneration
- aggrecan
- proteoglycans
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c-reactive
-
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
-
subchondral
-
emmprin
-
chondroprotective
-
photoaging
- collagenases
- diagnostics
- medicine
- aggrecanase
-
prommp-9
-
neoepitope
-
gelatinolytic
- mt1-mmp
-
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
3.4.24.17 stromelysin 1Advanced search results
results (
results (Source Tissue
Source Tissue on EC 3.4.24.17 - stromelysin 1
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SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
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subcutaneous and gonadal adipose tissue. Significantly reduced MMP-3 expression in MMP-10-deficient adipose tissues
MMP-3 has been identified in predentin and in dentin, where it localizes within the intertubular dentin, along the collagen fibrils
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clinical phenotypes with Helicobacter pylori infection are strongly related to inflammatory cytokines, MMP-3, and pepsinogen secretion
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elevated expression of hippocampal enzyme mRNA and protein after traumatic brain injury. Enzyme is primarily localized to cell bodies within the deafferented dendritic laminae. Traumatic brain injury alone elevates enzyme protein over the stratum lacunosum moleculare, inner molecular layer and hilus, while traumatic brain injury plus bilateral entorhinal cortical lesion increases enzyme protein within the deafferented stratum lacunosum moleculare and dentate molecular layer
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enzyme expression in transiently induced during specific intercellular contact with endothelial cells. Enzyme expression is tightly regulated upon lymphoma cell/stromal cell interaction
the enzyme expression is associated with expression of Rac1b, a tumorigenic splice isoform of Rac1, in all stages of pancreatic cancer, analysis of 140 specimen, overview
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no differences in MMP-3 in the plasma of hypertensive versus normotensive subjects
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pro- and active form of MMP-3 are predominantly expressed in purified first trimester villous trophoblasts, in invasive cytotrophoblasts of differentiating explant cultures and in trophoblastic SGHPL-4 cells. Reduced MMP-3 expression in invasive trophoblasts of patients with severe preeclampsia
additional information
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MMP-3 is upregulated in the infarcted tissue compared to healthy control areas
age-dependent increase in the central nervous system expression of MMP-3 in Twitcher mice suffering globoid cell leukodystrophy
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age-dependent increase in the central nervous system expression of MMP-3 in Twitcher mice suffering globoid cell leukodystrophy
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cultured skin fibroblast. Induction of enzyme and matrix metalloproteinase MMP-1 expression by heat shock. Suppression of induction by the inhibition of extracellular signal-regulated kinase and c-Jun N-terminal kinase and by specific inhibition of interleukin IL-6 by monoclonal antibody
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gingival, gingival fibroblasts produce MMP-3 in response to inflammatory cytokines, such as TNF and interleukin-1
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collagen-induced arthritis hind paw sections as a model of human rheumatoid arthritis
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collagen-induced arthritis hind paw sections as a model of human rheumatoid arthritis
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quantitative detection of pro- and active forms of MMP-3 in blood from healthy subjects of both genders and different ages, overview. MMP-3 and TIMP-1 serum levels are age-dependently increased, the relationship between age and MMP-3 serum levels is stronger in men compared to women
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serum MMP-3 is significantly elevated in ankylosing spondylitis patients with active disease
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, antibody cross-reactivity due to the extreme similarity between MMP-3 and MMP-10 (EC 3.4.24.22) proteins
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, antibody cross-reactivity due to the extreme similarity between MMP-3 and MMP-10 (EC 3.4.24.22) proteins
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additional information
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the enzyme is not readily detected in normal cells in culture or tissue homogenates, but its synthesis is greatly enhanced in mesenchymal cells when they are treated with cytokines such as interleukin-1 and tumor necrosis factor alpha, growth factors, phorbol myristate, acetate and several other stimuli
additional information
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the enzyme is not readily detected in normal cells in culture or tissue homogenates, but its synthesis is greatly enhanced in mesenchymal cells when they are treated with cytokines such as interleukin-1 and tumor necrosis factor alpha, growth factors, phorbol myristate, acetate and several other stimuli
additional information
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comparison of basal and interleukin-1beta-dependent MMP-3 expression in SGHPL-4 cells and decidual fibroblasts, overview
additional information
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MMP-3 is strongly expressed in tumor and arthritis specimens, expression patterns of MMP-3 in a variety of healthy, cancerous and arthritic murine tissues, overview
additional information
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MMP-3 is strongly expressed in tumor and arthritis specimens, expression patterns of MMP-3 in a variety of healthy, cancerous and arthritic murine tissues, overview
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additional information
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the enzyme is not readily detected in normal cells in culture or tissue homogenates, but its synthesis is greatly enhanced in mesenchymal cells when they are treated with cytokines such as interleukin-1 and tumor necrosis factor alpha, growth factors, phorbol myristate, acetate and several other stimuli
additional information
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the enzyme is not readily detected in normal cells in culture or tissue homogenates, but its synthesis is greatly enhanced in mesenchymal cells when they are treated with cytokines such as interleukin-1 and tumor necrosis factor alpha, growth factors, phorbol myristate, acetate and several other stimuli
