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Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis.
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Human MMP11 ELISA Kit for Sandwich ELISA - ABIN414770
Hsin, Chen, Tang, Lin, Chou, Lin, Yang: High level of plasma matrix metalloproteinase-11 is associated with clinicopathological characteristics in patients with oral squamous cell carcinoma. in PLoS ONE 2014
In this study, matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI-MSI (show MSI1 ELISA Kits)) has been used for the first time to investigate the distribution of MMP-11 in human breast cancer tissues in order to show a possible correlation between cancerous and healthy samples, by differential proteomics and using such differences for possible cancer diagnosis and/or prognosis.
Authors evaluated the expression of known targets of miR (show MLXIP ELISA Kits)-125a and found that sirtuin-7 (show SIRT7 ELISA Kits), matrix metalloproteinase-11, and c-Raf (show RAF1 ELISA Kits) were up-regulated in tumor tissue by 2.2-, 3-, and 1.7-fold, respectively. Overall, these data support a tumor suppressor role for miR (show MLXIP ELISA Kits)-125a.
Results revealed that MMP-11 high expression in oral squamous cell carcinoma (OSCC) samples can predict the progression, especially lymph node metastasis, and the survival of OSCC patients.
A new prognostic model for HR-/HER2 (show ERBB2 ELISA Kits)+ breast cancer based on the expression of MMP11 and CD2 (show CD2 ELISA Kits) was developed and the distant metastasis-free survival for patients in the high-risk group according to our model was significantly lower than that for those in the low-risk group.
HMGA1 (show HMGA1 ELISA Kits) and MMP-11 may play a key role in the proliferation and progression of skin tumors in humans.
These results demonstrated that miR (show MLXIP ELISA Kits)-145 has an inhibitory role in TNBC malignancy by targeting MMP11 and Rab27a (show RAB27A ELISA Kits), which might be potential therapeutic and diagnostic targets for TNBC.
the data demonstrate that miR125a5p functions as a tumor suppressor gene and serves an important role in inhibiting osteosarcoma cell migration, invasion and EMT (show ITK ELISA Kits) by targeting MMP11.
MMP-11 overexpression is associated with aggressive tumor phenotype and unfavorable clinical outcome in urothelial carcinomas.
Our study established that high serum levels of MMP-11 are associated with poor clinical outcome and may serve as a prognostic biomarker in colon cancer patients.
Overexpression of MMP-11 was discovered in sera of cancer patients compared with normal control group as well as in multiple tumor tissue specimens, such as gastric cancer, breast cancer, and pancreatic cancer. At present, some evidence supports that MMP-11 may work as a significant tumor biomarker for early detection of cancer, tumor staging, prognostic analysis, monitoring recurrence [review]
Strikingly, MMP11 overexpression protects against type 2 diabetes while Mmp11-/- mice exhibit hallmarks of metabolic syndrome.
Results show that MMP-11 has a paracrine function during mammary gland development that might be harnessed to promote tumor progression, exposing a new link between development and malignancy.
point-out the paradoxical role of MMP11 in favoring the onset and growth of lung metastases but limiting lung foci number, and inhibiting the cancer cell dissemination to other organs
investigation of a potential role of MMP-11 in adipose tissue development
The increased levels of ST-3 in the thymus may be due to the presence of macrophages responsible for clearance of apoptotic cells
downregulated by deglycosylation of CD147 in hepatocarcinoma cells
These data together provide compelling evidence into the function of MMP-11 and suggest that MMP-11 act as a tumor lymphatic metastasis-associated gene.
These findings reveal that the tumor biological marker CD147 functionally mediates MMP-11, VEGF-A (show VEGFA ELISA Kits) expression and tumor lymphatic metastasis.
Mmp11 exhibits collagenolytic function against collagen VI under normal conditions.
Our study describes the identification of MMP11 as a novel broadly expressed tumor associated antigen as target candidate for cancer immunotherapy.
Transgenic tadpoles were prepared with an elastase promoter driving either the ST3 gene or the constitutively active form of Notch (show NOTCH1 ELISA Kits) (IC).
analysis of substrate specificity for stromelysin-3: alpha1-PI is unlikely to be a physiological substrate
ST3 regulates cell fate and tissue morphogenesis through direct or indirect extracellular matrix remodeling
Laminin receptor precursor cleavage by ST3 plays a role in both physiological and pathological processes.
thyroid hormone (show PTH ELISA Kits) regulation of Xenopus laevis Stromelysin-3 is mediated by a DNA element in the first intron
Mutational analysis of the cleavage of the cancer-associated laminin receptor by stromelysin-3 reveals the contribution of flanking sequences to site recognition and cleavage efficiency.
ST3 expression, in the absence of T3 hormone, caused significant muscle cell death in the tail of premetamorphic transgenic tadpoles
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP's, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix.
, stromelysin III
, matrix metalloproteinase 11
, matrix metalloproteinase-11
, stromelysin 3
, Matrix metalloproteinase 11 (stromelysin 3)
, gene 14
, Matrix metalloproteinase-11