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Purinergic receptor P2X, ligand-gated ion channel, 5

The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the neighboring downstream gene, TAX1BP3 (Tax1 binding protein 3). [provided by RefSeq, Mar 2011] (from NCBI)
Top mentioned proteins: P2X4, P2X2, P2X7, P2X3, P2X6
Papers on P2X5
TNP-ATP is Beneficial for Treatment of Neonatal Hypoxia-Induced Hypomyelination and Cognitive Decline.
Li et al., Kunming, China. In Neurosci Bull, Feb 2016
Interestingly, much of the hypoxia-induced brain damage was ameliorated by treatment with the ATP analogue 2',3'-0-(2,4,6-trinitrophenyl)-adenosine 5'-triphosphate (TNP-ATP; blocks all ionotropic P2X1-7 receptors), whereas treatment with pyridoxalphosphate-6-azophenyl-2',4'-disulphonic acid (PPADS; inhibits P2X1-3 and P2X5-7 receptors) was less neuroprotective.
Altered purinergic receptor-Ca(2+) signaling associated with hypoxia-induced epithelial-mesenchymal transition in breast cancer cells.
Monteith et al., Brisbane, Australia. In Mol Oncol, Jan 2016
P2X4, P2X5, P2X7, P2Y1 and P2Y11 mRNAs decreased with hypoxia, whereas P2Y6 mRNA increased.
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.
Purinergic Signalling in the Reproductive System.
Gorodeski, Cleveland, United States. In Auton Neurosci, Sep 2015
Analysis of functional expression of purinoceptors suggests that P2Y2 receptors are involved in the regulation of luminal fluid secretion in vivo; P2X1 and P2X2 in the regulation of smooth muscle cell contraction of blood vessels and tubular organs; P2X2 in the regulation of sperm cell maturation; P2X3 in activation of sensory nerve fibers involved in reflex activities and pain; P2X4 in the regulation of tight junctional resistance and epithelial transport in female reproductive tract epithelia, and in the regulation of luminal acidification in the epididymis, vas deferens and probably the vagina and ectocervix; P2Y1 and P2Y2 in the regulation of cell proliferation; P2X5 and P2X7A in the regulation of epithelial cell terminal differentiation and apoptosis; and A1 receptors in the regulation of sperm cell capacitation.
[The Relationship Study between Expressions of P2X5 Receptor and Deficiency-cold Syndrome/Deficiency-heat Syndrome at Various Ambient Temperatures].
Hou et al., In Zhongguo Zhong Xi Yi Jie He Za Zhi, May 2015
OBJECTIVE: To detect the expression of the peripheral blood P2X5 receptor at various ambient temperatures, and to explore its relationship with deficiency-cold syndrome and deficiency-heat syndrome.
Identification and characterization of a selective allosteric antagonist of human P2X4 receptor channels.
Séguéla et al., Montréal, Canada. In Mol Pharmacol, Apr 2015
BX430 is highly selective, having virtually no functional impact on all other P2X subtypes, namely, P2X1-P2X3, P2X5, and P2X7, at 10-100 times its IC50.
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.
P2X2 and P2X5 Receptors Mediate Bladder Hyperesthesia in ICC in Female Overactive Bladder.
Li et al., Chongqing, China. In Cell Biochem Biophys, Feb 2015
UNASSIGNED: This study was set to explore the role of P2X2 and P2X5 as the important molecules in sensory afferent of bladder in female overactive bladder (OAB) patients with the bladder hyperesthesia.
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.
Purinergic signalling in the musculoskeletal system.
Orriss et al., London, United Kingdom. In Purinergic Signal, 2013
For example, sequential expression of P2X5, P2Y1 and P2X2 receptors occurs during muscle regeneration in the mdx model of muscular dystrophy.
Purinergic signalling in the lower urinary tract.
Burnstock, London, United Kingdom. In Acta Physiol (oxf), 2013
Treatment of prostate and bladder cancer with ATP is effective against the primary tumours in animal models and human cell lines, via P2X5 and P2X7 receptors, and also improves the systemic symptoms associated with advanced malignancy.
Post-translational regulation of P2X receptor channels: modulation by phospholipids.
Séguéla et al., Vancouver, Canada. In Front Cell Neurosci, 2012
All functional mammalian P2X subtypes tested, with the notable exception of P2X5, have been shown to be positively modulated by PIPn, i.e., homomeric P2X1, P2X2, P2X3, P2X4, and P2X7, as well as heteromeric P2X1/5 and P2X2/3 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 P2X5 receptor subunit is located in neuronal somata.
Sensing muscle ischemia: coincident detection of acid and ATP via interplay of two ion channels.
McCleskey et al., Portland, United States. In Neuron, 2010
Purinergic receptor P2X5 binds to adenosine triphosphate (ATP) to form a molecular complex with ASIC3 (acid-sensing ion channel number 3) to detect muscle ischemia.
Genetic and functional analysis of human P2X5 reveals a distinct pattern of exon 10 polymorphism with predominant expression of the nonfunctional receptor isoform.
Whiteside et al., Princeton, United States. In Mol Pharmacol, 2010
findings indicate that most humans express only a nonfunctional isoform of P2X5, which is in stark contrast to what is seen in other vertebrate species in which P2X5 has been studied, from which only the full-length isoform is known
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 P2X5 receptors are expressed on LHRH-containing neurons.
Myeloid leukemic progenitor cells can be specifically targeted by minor histocompatibility antigen LRH-1-reactive cytotoxic T cells.
Dolstra et al., Nijmegen, Netherlands. In Blood, 2009
These findings provide a rationale for use of LRH-1 as immunotherapeutic target antigen to treat residual or persisting myeloid malignancies after allogeneic stem cell transplantation
Molecular physiology of P2X receptors.
North, Sheffield, United Kingdom. In Physiol Rev, 2002
Homomeric P2X1, P2X2, P2X3, P2X4, P2X5, and P2X7 channels and heteromeric P2X2/3 and P2X1/5 channels have been most fully characterized following heterologous expression.
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.
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