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ADAM metallopeptidase domain 9

This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. The protein encoded by this gene interacts with SH3 domain-containing proteins, binds mitotic arrest deficient 2 beta protein, and is also involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. Several alternatively spliced transcript variants have been identified for this gene. [provided by RefSeq, Jul 2010] (from NCBI)
Top mentioned proteins: metalloprotease, ADAM10, TACE, CAN, V1a
Papers on ADAM9
Estrogen induced the expression of ADAM9 through estrogen receptor α but not estrogen receptor β in cultured human neuronal cells.
Cong et al., Jinan, China. In Gene, Mar 2016
PURPOSE OF THE STUDY: To investigate the induction of 'a disintegrin and metalloprotease' 9 (ADAM9) by which estrogen receptor (ER) subtypes and estrogen regulation of expression in cultured human neuronal cells.
Association of MicroRNAs and YRNAs with Platelet Function.
Mayr et al., London, United Kingdom. In Circ Res, Jan 2016
MiR-126 directly and indirectly affects ADAM9 and P2Y12 receptor expression.
MiR-33a suppresses breast cancer cell proliferation and metastasis by targeting ADAM9 and ROS1.
Luo et al., Xiamen, China. In Protein Cell, Dec 2015
Combining bioinformatics prediction and biochemical analyses, we showed that ADAM9 and ROS1 are direct downstream targets of miR-33a.
Disruption of phactr-1 pathway triggers pro-inflammatory and pro-atherogenic factors: New insights in atherosclerosis development.
Lepelletier et al., Villejuif, France. In Biochimie, Nov 2015
Moreover, the decrease of phactr-1 expression induced several factors implicated in atherosclerotic events such as oxidized low-density lipoprotein receptors (CD36, Clusterin, Cadherin-13), pro-inflammatory proteins including Thrombin, Thrombin receptor 1 (PAR-1), A Disintegrin And Metalloprotease domain-9/-17 (ADAM-9/-17), Trombospondin-2 and Galectin-3.
Novel retinopathy in related Gordon setters: a clinical, behavioral, electrophysiological, and genetic investigation.
Ofri et al., Davis, United States. In Vet Ophthalmol, Oct 2015
Mutations that cause achromatopsia (in CNGB3) and cone-rod dystrophies (in ADAM9 and IQCB1) were not detected in any dog tested, although five reference dogs were carriers of the mutation in C2orf71 that causes rod-cone degeneration 4 (rcd4) in Gordon setters and in polski owczarek nizinny dogs.
MicroRNA-126 Overexpression Inhibits Proliferation and Invasion in Osteosarcoma Cells.
He et al., Linyi, China. In Technol Cancer Res Treat, Sep 2015
Cells overexpressing microRNA-126 exhibited reduced ADAM9 expression levels compared to other 2 groups (all P < .05),
ADAM-family metalloproteinases in lung inflammation: potential therapeutic targets.
Ludwig et al., Aachen, Germany. In Am J Physiol Lung Cell Mol Physiol, Mar 2015
ADAM8, ADAM9, ADAM15, and ADAM33 are upregulated during acute or chronic lung inflammation, and recent functional or genetic analyses have linked them to disease development.
MiR-126 regulated breast cancer cell invasion by targeting ADAM9.
Li et al., Zhengzhou, China. In Int J Clin Exp Pathol, 2014
Herein, we demonstrated that miR-126 play a suppressor role in human breast cancer cells invasion through the direct repression of a disintegrin and metalloprotease 9 (ADAM9).
ADAM9 enhances CDCP1 protein expression by suppressing miR-218 for lung tumor metastasis.
Sher et al., Taiwan. In Sci Rep, 2014
We previously demonstrated that ADAM9 enhanced the expression of the pro-migratory protein CDCP1 to promote lung metastasis; however, the regulatory process remains unknown.
miR-126 in human cancers: clinical roles and current perspectives.
Lam et al., Gold Coast, Australia. In Exp Mol Pathol, 2014
In addition, miR-126 can alter a multitude of cellular mechanisms in cancer pathogenesis via suppressing gene translation of numerous validated targets such as PI3K, KRAS, EGFL7, CRK, ADAM9, HOXA9, IRS-1, SOX-2, SLC7A5 and VEGF.
ADAM22 as a prognostic and therapeutic drug target in the treatment of endocrine-resistant breast cancer.
Young et al., Dublin, Ireland. In Vitam Horm, 2012
A number of ADAM proteins have been implicated in the occurrence of breast cancer, including ADAM 9, ADAM12, ADAM15, ADAM17, ADAM22, and ADAM28.
α-Cleavage of cellular prion protein.
Kong et al., Cleveland, United States. In Prion, 2012
The effect of ADAM10, ADAM17, and ADAM9 on N1 secretion clearly indicates their involvement in the α-cleavage of PrP (C) , but there has been no report of direct PrP (C) α-cleavage activity with any of the three ADAMs in a purified protein form.
MT1-MMP inactivates ADAM9 to regulate FGFR2 signaling and calvarial osteogenesis.
Zhou et al., Shenzhen, China. In Dev Cell, 2012
The data revealed a regulatory paradigm for FGRF2 signaling and identified MT1-MMP as a critical negative modulator of ADAM9 activity to maintain FGFR2 signaling in calvarial osteogenesis.
LPS activates ADAM9 dependent shedding of ACE from endothelial cells.
Murphy et al., Cambridge, United Kingdom. In Biochem Biophys Res Commun, 2012
Transient transfection of ADAM9 and ACE cDNAs into HEK293 cells demonstrated that ADAM9 requires both membrane anchorage and its catalytic domain to shed ACE.
MiR-126 acts as a tumor suppressor in pancreatic cancer cells via the regulation of ADAM9.
Shimosegawa et al., Tokyo, Japan. In Mol Cancer Res, 2012
The miR-126/ADAM9 axis plays essential role in the inhibition of invasive growth of pancreatic cancer cells.
ADAM9 inhibition increases membrane activity of ADAM10 and controls α-secretase processing of amyloid precursor protein.
Bartsch et al., Apex, United States. In J Biol Chem, 2011
ADAM10 activity is regulated by inhibition of ADAM9, and this regulation may be used to control shedding of amyloid precursor protein by enhancing alpha-secretase activity, a key regulatory step in the etiology of Alzheimer disease
The disintegrin-like and cysteine-rich domains of ADAM-9 mediate interactions between melanoma cells and fibroblasts.
Mauch et al., Köln, Germany. In J Biol Chem, 2011
ADAM-9 expression plays an important role in mediating cell-cell contacts between fibroblasts and melanoma cells and that these interactions contribute to proteolytic activities required during invasion of melanoma cells.
ADAM9 as a potential target molecule in cancer.
Peduto, Paris, France. In Curr Pharm Des, 2008
ADAM9 is consistently overexpressed in various human cancers, and plays a role in tumorigenesis in mouse models.
Genomic and transcriptional aberrations linked to breast cancer pathophysiologies.
Gray et al., San Francisco, United States. In Cancer Cell, 2006
Nine of these (FGFR1, IKBKB, ERBB2, PROCC, ADAM9, FNTA, ACACA, PNMT, and NR1D1) are considered druggable.
ADAM10 is a principal 'sheddase' of the low-affinity immunoglobulin E receptor CD23.
Blobel et al., New York City, United States. In Nat Immunol, 2006
Here we used loss-of-function and gain-of-function experiments with cells lacking or overexpressing candidate CD23-releasing enzymes (ADAM8, ADAM9, ADAM10, ADAM12, ADAM15, ADAM17, ADAM19 and ADAM33), ADAM-knockout mice and a selective inhibitor to identify ADAM10 as the main CD23-releasing enzyme in vivo.
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