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FXYD domain containing ion transport regulator 3

Mat-8, FXYD3
This gene belongs to a small family of FXYD-domain containing regulators of Na+/K+ ATPases which share a 35-amino acid signature sequence domain, beginning with the sequence PFXYD, and containing 7 invariant and 6 highly conserved amino acids. This gene encodes a cell membrane protein that may regulate the function of ion-pumps and ion-channels. This gene may also play a role in tumor progression. Alternative splicing results in multiple transcript variants encoding distinct isoforms.[provided by RefSeq, Oct 2008] (from NCBI)
Top mentioned proteins: ATPase, Phospholamban, CAN, HAD, ACID
Papers on Mat-8
Silencing overexpression of FXYD3 protein in breast cancer cells amplifies effects of doxorubicin and γ-radiation on Na(+)/K(+)-ATPase and cell survival.
Rasmussen et al., Sydney, Australia. In Breast Cancer Res Treat, Feb 2016
UNASSIGNED: FXYD3, also known as mammary tumor protein 8, is overexpressed in several common cancers, including in many breast cancers.
FXYD1 negatively regulates Na(+)/K(+)-ATPase activity in lung alveolar epithelial cells.
Morty et al., Gießen, Germany. In Respir Physiol Neurobiol, Jan 2016
We describe here increased expression of FXYD1, FXYD3 and FXYD5, three regulatory subunits of the Na(+)/K(+)-ATPase, in the lungs of ARDS patients.
External validation of FXYD3 and KRT20 as predictive biomarkers for the presence of micrometastasis in muscle invasive bladder cancer lymph nodes.
López-Guerrero et al., Valencia, Spain. In Actas Urol Esp, Oct 2015
INTRODUCTION: Recent studies have proposed that FXYD3 and KRT20 mRNA quantified by quantitative reverse transcription polymerase chain reaction (qRT-PCR) in paraffin could be biomarkers to detect lymph nodes with micrometastases that avoid detection by conventional analysis with hematoxylin-eosin (HE).
MicroRNA-143 is a putative predictive factor for the response to fluoropyrimidine-based chemotherapy in patients with metastatic colorectal cancer.
Nagtegaal et al., Nijmegen, Netherlands. In Oncotarget, Oct 2015
Furthermore, FXYD3, an ion transport regulator and a putative target of miR-143, also showed an association with PFS.
Estrogen and tamoxifen up-regulate FXYD3 on breast cancer cells: assessing the differential roles of ER α and ZEB1.
Aronica et al., Buffalo, United States. In Springerplus, 2014
Increased expression of the FXYD3 family of proteins has been associated with lung, colorectal, bladder and pancreatic cancers, and recent evidence suggests that elevated FXYD3 may promote tumor cell proliferation in breast cancer as well.
Expression and clinical significance of FXYD3 in endometrial cancer.
Sun et al., Shijiazhuang, China. In Oncol Lett, 2014
FXYD3 expression is upregulated in numerous cancer cell types.
FXYD6 is a new biomarker of cholangiocarcinoma.
Yan et al., Suzhou, China. In Oncol Lett, 2014
Members of the FXYD domain-containing ion transport regulator protein family, including FXYD3 and FXYD5, play an important role in the pathogenesis of numerous tumors.
Histone code of genes induced by co-treatment with a glucocorticoid hormone agonist and a p44/42 MAPK inhibitor in human small intestinal Caco-2 cells.
Goda et al., Shizuoka, Japan. In Biochim Biophys Acta, 2014
RESULTS: Co-treatment of Caco-2 cells with Dex and PD enhanced several genes related to intestinal differentiation and functions such as SCNN1A, FXYD3, LCT and LOX.
Oxidative inhibition of the vascular Na+-K+ pump via NADPH oxidase-dependent β1-subunit glutathionylation: implications for angiotensin II-induced vascular dysfunction.
Figtree et al., Sydney, Australia. In Free Radic Biol Med, 2013
Ang II-induced oxidative inhibition of Na(+)-K(+) ATPase and decrease in K(+)-induced relaxation were reversed by preincubation of VSMCs and rings with recombinant FXYD3 protein that is known to facilitate deglutathionylation of β1-subunit.
Gluco-incretins regulate beta-cell glucose competence by epigenetic silencing of Fxyd3 expression.
Thorens et al., Lausanne, Switzerland. In Plos One, 2013
RESULTS: Fxyd3 was the most up-regulated gene in glucose incompetent islets from dKO mice.
Gene expression profiling of intrahepatic cholangiocarcinoma.
Petmitrb et al., Bangkok, Thailand. In Asian Pac J Cancer Prev, 2012
For validation of the microarray results, 7 up-regulated genes (FXYD3, GPRC5A, CEACAM5, MUC13, EPCAM, TMC5, and EHF) and 3 down- regulated genes (CPS1, TAT, and ITIH1) were selected for confirmation using quantitative RT-PCR, resulting in 100% agreement.
Translocation of Pseudomonas aeruginosa from the intestinal tract is mediated by the binding of ExoS to an Na,K-ATPase regulator, FXYD3.
Gotoh et al., Kyoto, Japan. In Infect Immun, 2010
ExoS facilitates P. aeruginosa penetration through the intestinal epithelial barrier by binding to FXYD3 and thereby impairing the defense function of tight junctions against bacterial penetration.
Down-regulation of FXYD3 expression in human lung cancers: its mechanism and potential role in carcinogenesis.
Kitamura et al., Yokohama, Japan. In Am J Pathol, 2009
inactivation of FXYD3 through a gene mutation or unknown mechanism could be one cause of the atypical shapes of cancer cells and play a potential role in the progression of lung cancer.
Expression and significance of FXYD-3 protein in gastric adenocarcinoma.
Sun et al., Shijiazhuang, China. In Dis Markers, 2009
Up-regulated expression of FXYD-3 protein may be involved in tumourgenesis and invasion of gastric adenocarcinoma.
Expression of FXYD3 protein in relation to biological and clinicopathological variables in colorectal cancers.
Sun et al., Linköping, Sweden. In Chemotherapy, 2008
FXYD3 expression is related to several biological variables including ras, p53, legumain and PCNA, and may be involved in the development of the relatively early stages of colorectal cancers
FXYD3 expression in gliomas and its clinicopathological significance.
Sun et al., Shijiazhuang, China. In Oncol Res, 2008
Upregulation of FXYD3 is associated with glioma.
[FXYD proteins: novel regulators of Na,K-ATPase].
Geering et al., Lausanne, Switzerland. In Med Sci (paris), 2006
Recent evidence suggests that 6 out of 7 FXYD proteins, FXYD1 (phospholemman), FXYD2 (gamma subunit of Na,K-ATPase), FXYD3 (Mat-8), FXYD4 (CHIF), FXYD5 (Ric) and FXYD7 associate with Na,K-ATPase and modulate its transport properties e.g. its Na+ and/or its K+ affinity in a distinct way.
FXYD proteins: new regulators of Na-K-ATPase.
Geering, Lausanne, Switzerland. In Am J Physiol Renal Physiol, 2006
Recent experimental evidence suggests that at least five of the seven members of this family, FXYD1 (phospholemman), FXYD2 (gamma-subunit of Na-K-ATPase), FXYD3 (Mat-8), FXYD4 (CHIF), and FXYD7, are auxiliary subunits of Na-K-ATPase and regulate Na-K-ATPase activity in a tissue- and isoform-specific way.
Function of FXYD proteins, regulators of Na, K-ATPase.
Geering, Lausanne, Switzerland. In J Bioenerg Biomembr, 2005
FXYD3 expressed in stomach, colon, and numerous tumors also modulates the transport properties of Na, K-ATPase but it has a lower specificity of association than other FXYD proteins and an unusual membrane topology.
Structures of P-type transporting ATPases and chromosomal locations of their genes.
Sato et al., Suita, Japan. In Cell Struct Funct, 1998
Similar small polypeptides (phospholemman, Mat-8 and CHIF), which induce Cl- and K+ currents, have been found.
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