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TIMP metallopeptidase inhibitor 2

TIMP-2, Tissue Inhibitor of Metalloproteinase-2
This gene is a member of the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases involved in degradation of the extracellular matrix. In addition to an inhibitory role against metalloproteinases, the encoded protein has a unique role among TIMP family members in its ability to directly suppress the proliferation of endothelial cells. As a result, the encoded protein may be critical to the maintenance of tissue homeostasis by suppressing the proliferation of quiescent tissues in response to angiogenic factors, and by inhibiting protease activity in tissues undergoing remodelling of the extracellular matrix. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: MMP-2, MMP-9, HAD, CAN, V1a
Papers using TIMP-2 antibodies
Antiangiogenic mechanisms of diet-derived polyphenols
Peng Robert Y. et al., In Evidence-based Complementary and Alternative Medicine : eCAM, 2001
... TIMP-2 antibodies were obtained from Abcam (Taipei, Taiwan) ...
Papers on TIMP-2
Role of matrix metalloproteinases in the pathogenesis of childhood gastroenteritis.
Yoshikawa et al., Japan. In J Med Virol, Feb 2016
At the time of hospital admission, all viral GE patients demonstrated increased MMP-9 and decreased MMP-2 and TIMP-2 serum levels.
Cell-cycle arrest and acute kidney injury: the light and the dark sides.
Chawla et al., Pittsburgh, United States. In Nephrol Dial Transplant, Jan 2016
We recently reported results from multi-center studies where two urinary markers of cell-cycle arrest, tissue inhibitor of metalloproteinases-2 (TIMP-2) and insulin-like growth factor-binding protein 7 (IGFBP7) were validated for development of AKI well ahead of clinical manifestations-azotemia and oliguria.
Inflammatory markers in pediatric stroke: An attempt to better understanding the pathophysiology.
Swiss Neuropediatric Stroke Registry Study Group et al., Canada. In Eur J Paediatr Neurol, Jan 2016
Median levels of MMP-1, MMP-2, TIMP-1, TIMP-2, sE-selectin, sICAM-1, sVCAM-1, IL-8, IL-10, TNF-alpha, VEGF, Fetuin A were found to be higher in the neonatal group when compared with older children.
Analysis of the correlations between oxidative stress, gelatinases and their tissue inhibitors in the human subjects with obstructive sleep apnea syndrome.
Caimi et al., Palermo, Italy. In J Physiol Pharmacol, Dec 2015
We measured the parameters of oxidative stress, such as lipid peroxidation, protein oxidation, total antioxidant status (TAS), nitric oxide metabolites (NOx), and the plasma concentrations of the gelatinases (MMP-2 and MMP-9) and their tissue inhibitors (TIMP-1 and TIMP-2).
Lipid-induced hepatocyte-derived extracellular vesicles regulate hepatic stellate cell via microRNAs targeting PPAR-γ.
Feldstein et al., San Diego, United States. In Cell Mol Gastroenterol Hepatol, Dec 2015
RESULTS: Hepatocyte-derived EVs released during lipotoxicity are efficiently internalized by HSCs resulting in their activation, as shown by marked up-regulation of pro-fibrogenic genes (Collagen-I, α-SMA and TIMP-2), proliferation, chemotaxis and wound healing responses.
Biomarkers of drug-induced acute kidney injury in the adult.
Endre et al., Brisbane, Australia. In Expert Opin Drug Metab Toxicol, Nov 2015
Clinical biomarkers of cell cycle arrest, tissue inhibitor of metalloproteinase-2 and insulin-like growth factor binding protein 7 show promise but need further validation in clinical trials.
Anticancer and antimetastatic effects of cordycepin, an active component of Cordyceps sinensis.
Yoshikawa et al., Nishinomiya, Japan. In J Pharmacol Sci, 2015
Cordycepin also showed an antimetastatic action through inhibiting platelet aggregation induced by cancer cells and suppressing the invasiveness of cancer cells via inhibiting the activity of matrix metalloproteinase (MMP)-2 and MMP-9, and accelerating the secretion of tissue inhibitor of metalloproteinase (TIMP)-1 and TIMP-2 from cancer cells.
Prognostic value of tissue inhibitor of metalloproteinase-2 expression in patients with non-small cell lung cancer: a systematic review and meta-analysis.
Zhu et al., Shanghai, China. In Plos One, 2014
BACKGROUND AND OBJECTIVES: Tissue inhibitor of metalloproteinase-2 (TIMP-2) is a small secretory glycoprotein with anti-matrix metalloproteinase activity.
Metalloproteinases and Their Tissue Inhibitors in Comparison between Different Chronic Pneumopathies in the Horse.
Gehlen et al., Berlin, Germany. In Mediators Inflamm, 2014
Zymography and equine MMP and TIMP assays were used to detect MMP-2, MMP-8, MMP-9 as well as TIMP-1, and TIMP-2 in BALF supernatant.
Molecular mechanisms of tissue inhibitor of metalloproteinase 2 in the tumor microenvironment.
Bourboulia et al., Syracuse, United States. In Mol Cell Ther, 2013
One TIMP member in particular, TIMP-2, has many distinct properties and functions, that occur independent of MMP inhibition, including the inhibition of tumor growth and reduction of angiogenesis through decreased endothelial cell proliferation and migration.
miR-200c is aberrantly expressed in leiomyomas in an ethnic-dependent manner and targets ZEBs, VEGFA, TIMP2, and FBLN5.
Chegini et al., Gainesville, United States. In Endocr Relat Cancer, 2012
Altered expression of miR-200c may have a significant impact on the outcome of leiomyomas growth, maintenance of their mesenchymal and fibrotic characteristics, and possibly their associated symptoms.
NUR77 inhibits the expression of TIMP2 and increases the migration and invasion of HTR-8/SVneo cells induced by CYR61.
Hu et al., Nanjing, China. In Placenta, 2012
cysteine-rich angiogenic inducer 61 may promote trophoblast cell migration and invasion through upregulation of NUR77 protein leading to the increase of matrix metalloproteinase 2(MMP2) release and the downregulation of tissue inhibitor of MMP2 expression
TIMP2 deficient mice develop accelerated osteoarthritis via promotion of angiogenesis upon destabilization of the medial meniscus.
Xiao et al., Changsha, China. In Biochem Biophys Res Commun, 2012
these findings suggest that reduction of TIMP2 levels and increased angiogenesis are possible primary events in osteoarthritis progression.
[Expression of metalloproteinase MMP-9 and tissue inhibitor of metalloproteinase TIMP-2 in placenta of pregnant women with intrauterine growth restriction].
Karowicz-Bilińska et al., Poland. In Ginekol Pol, 2012
The greatest intensity of the reaction and the villous TIMP-2 expression was characteristic of the group with untreated Intrauterine growth restriction.
The role of matrix metalloproteinases (MMPs) and their inhibitors (TIMPs) in the development of esophageal cancer.
Szmitkowski et al., Białystok, Poland. In Folia Histochem Cytobiol, 2011
The the roles of TIMP-2 in Esophageal cancer (EC) development, tumor progression and formation of metastases have been most extensively characterized and best recognized.
Three immunomarker support vector machines-based prognostic classifiers for stage IB non-small-cell lung cancer.
Rong et al., Guangzhou, China. In J Clin Oncol, 2009
The SVM2 model integrates age, cancer cell type, and 19 markers, including BCL2, caspase-9, CD34MVD, low-molecular-weight cytokeratin, high-molecular-weight cytokeratin, cyclo-oxygenase-2, EMA, HER2, matrix metalloproteinases (MMP) -2, MMP-9, p16, p21ras, p21WAF1, p27kip1, p53, TIMP-1, TIMP-2, vascular endothelial growth factor (VEGF), and beta-catenin.
TIMP-2 mediated inhibition of angiogenesis: an MMP-independent mechanism.
Stetler-Stevenson et al., Bethesda, United States. In Cell, 2003
TIMP-2 mediated inhibition of angiogenesis is an MMP-independent mechanism.
Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in human pancreatic adenocarcinomas: clinicopathologic and prognostic significance of matrilysin expression.
Imai et al., Sapporo, Japan. In J Clin Oncol, 2001
PATIENTS AND METHODS: Using immunohistochemistry, we analyzed 70 pancreatic ductal adenocarcinoma tissues for expression of MMP-1, MMP-2, MMP-3, MMP-7 (matrilysin), MMP-9, MT1-MMP, TIMP-1, and TIMP-2.
Phase I and pharmacologic study of the specific matrix metalloproteinase inhibitor BAY 12-9566 on a protracted oral daily dosing schedule in patients with solid malignancies.
Eckhardt et al., United States. In J Clin Oncol, 2000
The study also sought to determine the principal toxicities of BAY 12-9566, whether plasma BAY 12-9566 steady state concentrations (C(ss)) of biologic relevance could be sustained for prolonged periods, and whether BAY 12-9566 affected plasma concentrations of MMP-2, MMP-9, and tissue inhibitor of MMP-2 (TIMP-2).
Expression and prognostic significance of metalloproteinases and their tissue inhibitors in patients with small-cell lung cancer.
Shepherd et al., Toronto, Canada. In J Clin Oncol, 1999
Positive IHC staining was evident for MMP-1 and -9 in 60% to 70% of tumor cells, and for MMP-11, -13, and -14 and TIMP-2 and -3 in 70% to 100% of tumor cells.
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