3.4.24.B7: matrix metalloproteinase-26
This is an abbreviated version!
For detailed information about matrix metalloproteinase-26, go to the full flat file.
Word Map on EC 3.4.24.B7
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3.4.24.B7
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endometrial
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timp-4
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mmp-1
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matrilysins
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menstrual
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medicine
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pro-mmp-9
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olomouc
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metalloelastase
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palacky
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metalloproteinase-4
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prodomain
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diagnostics
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synthesis
- 3.4.24.B7
- endometrial
- timp-4
- mmp-1
- matrilysins
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menstrual
- medicine
- pro-mmp-9
-
olomouc
- metalloelastase
-
palacky
-
metalloproteinase-4
- prodomain
- diagnostics
- synthesis
Reaction
proteolytic degradation of proteins =
Synonyms
endometase, endometase/matrilysin-2, M10.029, matrilysin 2, matrilysin-2, matrilysis-2/MMP-26, matrix metalloproteinase-26, metalloproteinases-26, MMP-26, MMP-26/endometase/matrilysin-2, More
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General Information
General Information on EC 3.4.24.B7 - matrix metalloproteinase-26
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malfunction
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silencing of the MMP-26 gene significantly retardes the invasiveness of A-549 cells
physiological function
additional information
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MMP-26 is implicated in genesis, progression, invasion and metastasis of several types of human cancers
physiological function
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MMP-26 may possess critical roles in the processes of tumor invasion, angiogenesis, and metastasis
physiological function
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MMP-26 participates in activation other members of the MMP family
physiological function
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MMP-26 plays an important role in local invasion, and angiogenesis. MMP-26 contributes to tumor development and to the restoration of tissue injury. The spreading cell ratio of MMP-26 transfected cells is significantly higher than parental U251 cells
physiological function
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the matrilysins, also known as MMP-7 or matrilysin-1 and MMP-26 or matrilysin-2, are involved in cell proliferation, apoptosis, invasion, and metastasis. Matrilysin-2 plays a role in the process of tissue remodeling and growth in the studied tumors, but it does not relate to the their distinct patterns of aggressiveness
physiological function
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MMP-26 contributes to A-549 cell invasion and migration in vitro. MMP-26 plays an important role in local through coordination with MMP-9
physiological function
MMP-26 plays an important role of in matrix modulation during disc health and degeneration
physiological function
MMP26 is a marker of the predecidual, secretory endometrium. During the second half of the late secretory phase, and during decidualization, MMP26 loses its response to progesterone concurrent with the loss of epithelial progesterone receptor. The decline in MMP26 levels between the mid- and late secretory phases may play a role in the receptive window for embryo implantation
physiological function
MMP26-transfected MCF-7 cells demonstrate increased atypia, including unusual mitotic figures, glucogen pools and special lysosomes in the cytoplasm. The adherence and spreading ability of MMP26-transfected cells are significantly increased compared with cells in the control group. The migration and invasion ability of MMP26-transfected cells is dramatically accelerated compared with the control group, but markedly reduced in the presence of anti-MMP26 antibody. MMP26 also increases the malignant phenotype in vivo. The number of vessel branches and the total length of vessels induced by MMP26-transfected cells are significantly increased compared to those induced by nontransfected cells
physiological function
overexpression of MMP26 in SW-1353 chondrosarcoma cells increases cell invasiveness, while inhibition of MMP26 decreases cell invasiveness. Inhibition of Wnt signaling significantly decreases the effect of MMP26 on cancer cell invasion
physiological function
MMP-26 expression levels in androgen-repressed human prostate cancer cells, transfected with sense or anti-sense MMP-26 cDNA, and in benign, neoplastic, and invasive prostate cancer tissues are directly correlated with those of the pro-apoptotic marker Bax. The MMP-26 protein levels are upregulated in high grade prostate intraepithelial neoplasia and decrease during the course of disease progression
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MMP-26 and MMP-9 may contribute to the more aggressive behavior of squamous cell carcinomas in organ transplant recipients
additional information
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under physiological conditions, a lipid or membrane microenvironment may regulate enzymatic activity