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Purinergic receptor P2X, ligand-gated ion channel, 6

P2X6, P2X6 receptor, P2XM
The protein encoded by this gene belongs to the family of P2X receptors, which are ATP-gated ion channels and mediate rapid and selective permeability to cations. This gene is predominantly expressed in skeletal muscle, and regulated by p53. The encoded protein is associated with VE-cadherin at the adherens junctions of human umbilical vein endothelial cells. Alternative splicing results in multiple transcript variants. A related pseudogene, which is also located on chromosome 22, has been identified. [provided by RefSeq, Apr 2009] (from NCBI)
Top mentioned proteins: P2X4, P2X2, P2X3, P2X7, P2X5
Papers on P2X6
Cardiomyogenesis of embryonic stem cells upon purinergic receptor activation by ADP and ATP.
Wartenberg et al., Jena, Germany. In Purinergic Signal, Dec 2015
Real-time RT-PCR analysis of purinergic receptor expression demonstrated presence of P2X1, P2X4, P2X6, P2X7, P2Y1, P2Y2, P2Y4, and P2Y6 on differentiating ES cells.
Differential expression of ATP-gated P2X receptors in DRG between chronic neuropathic pain and visceralgia rat models.
Li et al., Wuhan, China. In Purinergic Signal, Dec 2015
We found that except P2X2 and P2X3, the expression levels of P2X1 and P2X5 receptors increased in neuropathic pain while those expression levels of P2X4, P2X6, and P2X7 receptors increased in visceral pain.
Effects of ATP and NGF on Proliferation and Migration of Neural Precursor Cells.
Ulrich et al., São Paulo, Brazil. In Neurochem Res, Sep 2015
Gene expression of P2X2-7 and P2Y1,2,4,6,12,14 receptors was confirmed in undifferentiated and neural-differentiated neurospheres, with an up-regulation of P2X2 and P2X6 subtypes, together with a down-regulation of P2X4, P2X7 and P2Y subtypes upon induction to differentiation.
Phenotypes of ATP-activated current associated with their genotypes of P2X1-6 subunits in neurons innervating tooth-pulp.
Li et al., Wuhan, China. In Biochem Biophys Res Commun, Apr 2015
Cells responsive to ATP with the type F current mainly showed positive staining for P2X3 and P2X5, but negative staining for P2X2; cells responsive to ATP with the type I current showed positive staining for P2X1-3 and P2X5, but negative staining for P2X4; and cells responsive to ATP with the type S current showed positive staining for P2X1-5, but negative staining for P2X6.
Pharmacological and molecular characterization of functional P2 receptors in rat embryonic cardiomyocytes.
Burnstock et al., London, United Kingdom. In Purinergic Signal, Mar 2015
P2X1 and a low level of P2X5 receptor messenger RNA (mRNA) were also expressed at E18. Immunofluorescence data indicated that only P2X2 and P2X4 receptor proteins were expressed in E14 cardiomyocytes while protein for all the P2X receptor subtypes was expressed in E18, except for P2X3 and P2X6.
P2X receptors and inflammation.
Di Virgilio, Ferrara, Italy. In Curr Med Chem, 2014
While this is justified to a certain extent for P2X1, P2X2, P2X3, P2X5 and P2X6, which still await identification of a convincing role in the pathophysiology of immune cells, it is clearly not any more the case for P2X4 and even more so for P2X7, a molecule that has achieved the status of an essential, nonredundant, immunomodulatory receptor.
Age-related nuclear translocation of P2X6 subunit modifies splicing activity interacting with splicing factor 3A1.
Miras-Portugal et al., Madrid, Spain. In Plos One, 2014
In this work we report, for the first time, the accumulation of the P2X6 subunit inside the nucleus of hippocampal neurons in an age-dependent way.
Involvement of the left-flipper-to-dorsal-fin interface of the zebrafish P2X4 receptor in ATP binding and structural rearrangement.
Li et al., Guangzhou, China. In Neurosci Lett, 2014
However, insertion of the same sequence frame into a homologous position of the rat P2X6 receptor did not rescue channel function, suggesting that these residues are necessary but not sufficient for achieving the correct ATP-induced conformation.
P2X4 receptor regulation of transient receptor potential melastatin type 6 (TRPM6) Mg2+ channels.
Hoenderop et al., Nijmegen, Netherlands. In Pflugers Arch, 2014
Using RT-qPCR on a mouse tissue panel, P2x4 and P2x6 were shown to be expressed in the epithelium of the colon and of the kidney, two major sites of Mg(2+) reabsorption.
Identification of P2X2/P2X4/P2X6 heterotrimeric receptors using atomic force microscopy (AFM) imaging.
Edwardson et al., Cambridge, United Kingdom. In Febs Lett, 2014
Seven P2X purinergic receptor subunits have been identified: P2X1-P2X7.
The activation of P2Y2 receptors increases MCF-7 breast cancer cells migration through the MEK-ERK1/2 signalling pathway.
Roger et al., Tours, France. In Carcinogenesis, 2014
MCF-7 cells expressed messenger RNA for all known P2Y receptors and for P2X2, P2X4, P2X5, P2X6 and P2X7 receptors.
ATP binding site mutagenesis reveals different subunit stoichiometry of functional P2X2/3 and P2X2/6 receptors.
Illes et al., Aachen, Germany. In J Biol Chem, 2012
one subunit of P2X2 and two subunits of P2X3 form P2X2/3 heteromeric receptors, whereas two subunits of P2X2 and one subunit of P2X6 constitute P2X2/6 receptors
Spatiotemporal and anatomical analyses of P2X receptor-mediated neuronal and glial processing of sensory signals in the rat dorsal horn.
Toyama et al., Tokyo, Japan. In Pain, 2011
The P2X6 receptor subunit is widely expressed in neuropils in the whole gray matter except for the dorsal superficial layer of the dorsal horn.
Directed differentiation of neural progenitors into neurons is accompanied by altered expression of P2X purinergic receptors.
Ulrich et al., São Paulo, Brazil. In J Mol Neurosci, 2011
Results suggest a direct relationship between purinergic P2X2/6 receptor expression and induction of neuronal differentiation in mitogen-free cultured rat neurospheres.
Expression of P2X6 receptors in the enteric nervous system of the rat gastrointestinal tract.
Xiang et al., Shanghai, China. In Histochem Cell Biol, 2010
The P2X(6) receptors are mainly expressed on intrinsic sensory neurons and that ATP, via P2X(6) receptors probably in heteromeric combination with P2X(2) receptors, may be involved in regulating the physiological functions of these neurons.
P2X receptors are expressed on neurons containing luteinizing hormone-releasing hormone in the mouse hypothalamus.
Xiang et al., Shanghai, China. In Neurosci Lett, 2009
This study provides the first evidence that P2X8 receptors are expressed on LHRH-containing neurons.
Go it alone no more--P2X7 joins the society of heteromeric ATP-gated receptor channels.
Dubyak, Cleveland, United States. In Mol Pharmacol, 2007
Current genetic, biochemical, and/or physiological evidence indicates that the extended family of functional P2X receptors includes six homomeric channels composed of P2X1, P2X2, P2X3, P2X4, P2X5, or P2X7 subunits and six heteromeric channels that involve subunit pairings of P2X1/P2X2, P2X1/P2X4, P2X1/P2X5, P2X2/P2X3, P2X2/P2X6, or P2X4/P2X6.
P2X receptors in sensory neurones.
Burnstock, London, United Kingdom. In Br J Anaesth, 2000
P2X4 and/or P2X6 receptors in the CNS also seem to be involved in pain pathways.
Pharmacology of cloned P2X receptors.
Surprenant et al., Sheffield, United Kingdom. In Annu Rev Pharmacol Toxicol, 1999
Six homomeric (P2X1, P2X2, P2X3, P2X4, P2X5, P2X7) and three heteromeric (P2X2/P2X3, P2X4/P2X6, P2X1/P2X5) P2X receptor channels have been characterized in heterologous expression systems.
Functional and molecular diversity of purinergic ion channel receptors.
North et al., Sheffield, United Kingdom. In Ann N Y Acad Sci, 1999
P2X6 receptors do not express readily, and P2X7 receptors correspond closely in their properties to P2Z.
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