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Journal articles on the topic 'P2X2-receptors'

Author: Grafiati
Published: 4 June 2021
Last updated: 2 February 2022

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1

Rodriguez, Larry, Catherine Yi, Cameron Chu, et al. "Cross-Talk between P2X and NMDA Receptors." International Journal of Molecular Sciences 21, no. 19 (2020): 7187. http://dx.doi.org/10.3390/ijms21197187.

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Purinergic P2X receptors (P2X) are ATP-gated ion channels widely expressed in the CNS. While the direct contribution of P2X to synaptic transmission is uncertain, P2X reportedly affect N-methyl-D-aspartate receptor (NMDAR) activity, which has given rise to competing theories on the role of P2X in the modulation of synapses. However, P2X have also been shown to participate in receptor cross-talk: an interaction where one receptor (e.g., P2X2) directly influences the activity of another (e.g., nicotinic, 5-HT3 or GABA receptors). In this study, we tested for interactions between P2X2 or P2X4 and
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2

Chen, Chu, Margarett S. Parker, Anthony P. Barnes, Prescott Deininger, and Richard P. Bobbin. "Functional Expression of Three P2X2 Receptor Splice Variants From Guinea Pig Cochlea." Journal of Neurophysiology 83, no. 3 (2000): 1502–9. http://dx.doi.org/10.1152/jn.2000.83.3.1502.

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ATP has been suggested to act as a neurotransmitter or a neuromodulator in the cochlea. The responses to ATP in different cell types of the cochlea vary in terms of the rate of desensitization and magnitude, suggesting that there may be different subtypes of P2X receptors distributed in the cochlea. Recently three ionotropic P2X2 receptor splice variants, P2X2–1, P2X2–2, and P2X2–3, were isolated and sequenced from a guinea pig cochlear cDNA library. To test the hypothesis that these different splice variants could be expressed as functional homomeric receptors, the three P2X2 receptor variant
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3

Studeny, Simon, Ali Torabi, and Margaret A. Vizzard. "P2X2 and P2X3 receptor expression in postnatal and adult rat urinary bladder and lumbosacral spinal cord." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 289, no. 4 (2005): R1155—R1168. http://dx.doi.org/10.1152/ajpregu.00234.2005.

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P2X receptors mediate the effects of ATP in micturition and nociception. During postnatal maturation, a spinobulbospinal reflex and voluntary voiding replace primitive voiding reflexes. This may involve changes in neuroactive compounds and receptors in bladder reflex pathways. We examined P2X2 and P2X3 receptors in bladder and spinal cord from postnatal (P0–P36, indicating number of days) and adult Wistar rats. Western blot of whole bladders for P2X2 and P2X3 expression was performed. Immunostaining for P2X2 and P2X3 receptors in urothelium and detrusor smooth muscle whole mounts and spinal co
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4

Thériault, Olivier, Hugo Poulin, George R. Thomas, Albert D. Friesen, Waleed A. Al-Shaqha, and Mohamed Chahine. "Pyridoxal-5′-phosphate (MC-1), a vitamin B6 derivative, inhibits expressed P2X receptors." Canadian Journal of Physiology and Pharmacology 92, no. 3 (2014): 189–96. http://dx.doi.org/10.1139/cjpp-2013-0404.

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P2X receptors are cation-permeable ligand-gated ion channels that open in response to the binding of ATP. These receptors are present in many excitable cells, including neurons, striated muscle cells, epithelial cells, and leukocytes. They mediate fast excitatory neurotransmission in the central and peripheral nervous systems and are thought to be involved in neuropathic pain, inflammation, and cell damage following ischemia–reperfusion injuries. P2X receptors are thus a target for the development of new therapeutics to treat chronic pain and inflammation. In this study, we characterized the i
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5

McCord, Jennifer L., Hirotsugu Tsuchimochi, and Marc P. Kaufman. "P2X2/3 and P2X3 receptors contribute to the metaboreceptor component of the exercise pressor reflex." Journal of Applied Physiology 109, no. 5 (2010): 1416–23. http://dx.doi.org/10.1152/japplphysiol.00774.2010.

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The exercise pressor reflex is due to activation of thin fiber afferents within contracting muscle. These afferents are in part stimulated by ATP activation of purinergic 2X (P2X) receptors during contraction. Which of the P2X receptors contribute to the reflex is unknown; however, P2X2/3 and P2X3 receptor subtypes are good candidates because they are located on thin fiber afferents and are involved in sensory neurotransmission. To determine if P2X2/3 and P2X3 receptors evoke the metabolic component of the exercise pressor reflex, we examined the effect of two P2X2/3 and P2X3 antagonists, A-31
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6

Fong, Zhihui, Caoimhín S. Griffin, Roddy J. Large, Mark A. Hollywood, Keith D. Thornbury, and Gerard P. Sergeant. "Regulation of P2X1 receptors by modulators of the cAMP effectors PKA and EPAC." Proceedings of the National Academy of Sciences 118, no. 37 (2021): e2108094118. http://dx.doi.org/10.1073/pnas.2108094118.

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P2X1 receptors are adenosine triphosphate (ATP)-gated cation channels that are functionally important for male fertility, bladder contraction, and platelet aggregation. The activity of P2X1 receptors is modulated by lipids and intracellular messengers such as cAMP, which can stimulate protein kinase A (PKA). Exchange protein activated by cAMP (EPAC) is another cAMP effector; however, its effect on P2X1 receptors has not yet been determined. Here, we demonstrate that P2X1 currents, recorded from human embryonic kidney (HEK) cells transiently transfected with P2X1 cDNA, were inhibited by the hig
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7

Stoop, Ron, Annmarie Surprenant, and R. Alan North. "Different Sensitivities to pH of ATP-Induced Currents at Four Cloned P2X Receptors." Journal of Neurophysiology 78, no. 4 (1997): 1837–40. http://dx.doi.org/10.1152/jn.1997.78.4.1837.

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Stoop, Ron, Annmarie Surprenant, and R. Alan North. Different sensitivities to pH of ATP-induced currents at four cloned P2X receptors. J. Neurophysiol. 78: 1837–1840, 1997. The effect of changing extracellular pH was studied on the currents induced by ATP or αβ-methylene-ATP in HEK293 cells transfected with different P2X receptor subunits. In cells expressing P2X1, P2X3, or P2X4 receptors, the effect of ATP was decreased by acidification. In cells expressing P2X2 receptors, acidification increased the ATP-induced current; this effect was also seen in cells expressing heteromeric P2X2 and P2X3
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8

He, L., J. Chen, B. Dinger, L. Stensaas, and S. Fidone. "Effect of chronic hypoxia on purinergic synaptic transmission in rat carotid body." Journal of Applied Physiology 100, no. 1 (2006): 157–62. http://dx.doi.org/10.1152/japplphysiol.00859.2005.

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Recent studies indicate that chemoafferent nerve fiber excitation in the rat carotid body is mediated by acetylcholine and ATP, acting at nicotinic cholinergic receptors and P2X2 purinoceptors, respectively. We previously demonstrated that, after a 10- to 14-day exposure to chronic hypoxia (CH), the nicotinic cholinergic receptor blocker mecamylamine no longer inhibits rat carotid sinus nerve (CSN) activity evoked by an acute hypoxic challenge. The present experiments examined the effects of CH (9–16 days at 380 Torr) on the expression of P2X2 purinoceptors in carotid body and chemoafferent ne
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9

Zhuang, Jianguo, Xiuping Gao, Wan Wei, Amir Pelleg, and Fadi Xu. "Intralaryngeal application of ATP evokes apneic response mainly via acting on P2X3 (P2X2/3) receptors of the superior laryngeal nerve in postnatal rats." Journal of Applied Physiology 131, no. 3 (2021): 986–96. http://dx.doi.org/10.1152/japplphysiol.00091.2021.

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Aerosolized ATP induces cough and bronchoconstriction via activating P2X3 and P2X2/3 receptors (P2X3R and P2X2/3R) localized on vagal pulmonary sensory fibers. The superior laryngeal nerve (SLN), particularly SLN C-fibers (SLCFs), is involved in generating apnea, hypertension, and bradycardia. This study demonstrates for the first time that either ATP or α,β-mATP applied onto the laryngeal mucosa elicit these cardiorespiratory responses predominately through the activation of P2X3R-P2X2/3R localized on SLCFs.
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10

Skorinkin, Andrei, Andrea Nistri, and Rashid Giniatullin. "Bimodal Action of Protons on ATP Currents of Rat PC12 Cells." Journal of General Physiology 122, no. 1 (2003): 33–44. http://dx.doi.org/10.1085/jgp.200308825.

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The mode of action of extracellular protons on ATP-gated P2X2 receptors remains controversial as either enhancement or depression of ATP-mediated currents has been reported. By investigating, at different pH, the electrophysiological effect of ATP on P2X2 receptors and complementing it with receptor modelling, the present study suggests a unified mechanism for both potentiation and inactivation of ATP receptors by protons. Our experiments on patch-clamped PC12 cells showed that, on the same cell, mild acidification potentiated currents induced by low ATP concentrations (<0.1 mM) and att
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11

Gomes, Dayane A., Zhilin Song, Wanida Stevens, and Celia D. Sladek. "Sustained stimulation of vasopressin and oxytocin release by ATP and phenylephrine requires recruitment of desensitization-resistant P2X purinergic receptors." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 297, no. 4 (2009): R940—R949. http://dx.doi.org/10.1152/ajpregu.00358.2009.

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Coexposure of hypothalamo-neurohypophyseal system explants to ATP and phenylephrine [PE; an α1-adrenergic receptor (α1-AR) agonist] induces an extended elevation in vasopressin and oxytocin (VP/OT) release. New evidence is presented that this extended response is mediated by recruitment of desensitization-resistant ionotropic purinergic receptor subtypes (P2X-Rs): 1) Antagonists of the P2X2/3 and P2X7-Rs truncated the sustained VP/OT release induced by ATP+PE but did not alter the transient response to ATP alone. 2) The P2X2/3 and P2X7-R antagonists did not alter either ATP or ATP+PE-induced i
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12

Xiong, Keming, Robert W. Peoples, Jennifer P. Montgomery, et al. "Differential Modulation by Copper and Zinc of P2X2and P2X4 Receptor Function." Journal of Neurophysiology 81, no. 5 (1999): 2088–94. http://dx.doi.org/10.1152/jn.1999.81.5.2088.

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Differential Modulation by Copper and Zinc of P2X2 and P2X4 Receptor Function. The modulation by Cu2+ and Zn2+ of P2X2 and P2X4 receptors expressed in Xenopus oocytes was studied with the two-electrode, voltage-clamp technique. In oocytes expressing P2X2 receptors, both Cu2+ and Zn2+, in the concentration range 1–130 μM, reversibly potentiated current activated by submaximal concentrations of ATP. The Cu2+ and Zn2+ concentrations that produced 50% of maximal potentiation (EC50) of current activated by 50 μM ATP were 16.3 ± 0.9 (SE) μM and 19.6 ± 1.5 μM, respectively. Cu2+ and Zn2+potentiation
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13

Chiang, Bing-Juin, Chun-Hou Liao, Su-Han Mao, and Chiang-Ting Chien. "Adipose-Derived Stem Cells and Their Derived Microvesicles Ameliorate Detrusor Overactivity Secondary to Bilateral Partial Iliac Arterial Occlusion-Induced Bladder Ischemia." International Journal of Molecular Sciences 22, no. 13 (2021): 7000. http://dx.doi.org/10.3390/ijms22137000.

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(1) Background: We established a new bladder ischemia rat model through bilateral partial iliac arterial occlusion (BPAO) and investigated the therapeutic effect of adipose-derived stem cells (ADSCs) and ADSC-derived microvesicles (MVs); (2) Methods: The study included four groups: (1) sham, (2) BPAO, (3) BPAO + ADSCs, and (4) BPAO + ADSC-derived MVs. Female Wistar rats with BPAO were injected with ADSCs or ADSC-derived MVs through the femoral artery. Doppler flowmetry and real-time laser speckle contrast imaging were performed to quantify blood flow in the common iliac arteries and bladder mi
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14

Decker, Dima A., and James J. Galligan. "Cross-inhibition between nicotinic acetylcholine receptors and P2X receptors in myenteric neurons and HEK-293 cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 296, no. 6 (2009): G1267—G1276. http://dx.doi.org/10.1152/ajpgi.00048.2009.

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The enteric nervous system (ENS) controls gut function. P2X receptors and nicotinic acetylcholine receptors (nAChRs) are ligand-gated cation channels that mediate fast synaptic excitation in the ENS. Close molecular coupling in enteric neuronal membranes contributes to a mutually inhibitory interaction between these receptors; this effect is called cross-inhibition. We studied the molecular mechanisms responsible for cross-inhibition. Whole cell patch-clamp techniques were used to measure P2X- and nAChR-mediated currents in cultured enteric neurons and HEK-293 cells. In cultured myenteric neur
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15

Pelleg, Amir, Fadi Xu, Jianguo Zhuang, Bradley Undem, and Geoffrey Burnstock. "DT-0111: a novel drug-candidate for the treatment of COPD and chronic cough." Therapeutic Advances in Respiratory Disease 13 (January 2019): 175346661987796. http://dx.doi.org/10.1177/1753466619877960.

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Background: Extracellular adenosine 5′-triphosphate (ATP) plays important mechanistic roles in pulmonary disorders in general and chronic obstructive pulmonary disease (COPD) and cough in particular. The effects of ATP in the lungs are mediated to a large extent by P2X2/3 receptors (P2X2/3R) localized on vagal sensory nerve terminals (both C and Aδ fibers). The activation of these receptors by ATP triggers a pulmonary-pulmonary central reflex, which results in bronchoconstriction and cough, and is also proinflammatory due to the release of neuropeptides from these nerve terminals via the axon
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16

Villalobos, Carlos, Sara R. Alonso-Torre, Lucía Núñez, and Javier García-Sancho. "Functional ATP receptors in rat anterior pituitary cells." American Journal of Physiology-Cell Physiology 273, no. 6 (1997): C1963—C1971. http://dx.doi.org/10.1152/ajpcell.1997.273.6.c1963.

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The effects of ATP and other nucleotides on the cytosolic Ca2+ concentration ([Ca2+]i) of single immunocytochemically typed anterior pituitary (AP) cells have been studied. ATP increased [Ca2+]iin a large percentage (60–88%) of all five AP cell types: lactotropes, somatotropes, corticotropes, gonadotropes, and thyrotropes. Additivity experiments suggest the presence of at least two different receptors, one accepting both ATP and UTP (U receptor), producing Ca2+ release from the intracellular stores, and the other preferring ATP (A receptor), producing Ca2+ (and Mn2+) entry. The characteristics
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17

Xu, Wenming, Ke Wang, Yan Chen, et al. "Sperm gamma-aminobutyric acid type A receptor delta subunit (GABRD) and its interaction with purinergic P2X2 receptors in progesterone-induced acrosome reaction and male fertility." Reproduction, Fertility and Development 29, no. 10 (2017): 2060. http://dx.doi.org/10.1071/rd16294.

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The mechanism underlying the non-genomic action of progesterone in sperm functions and related Ca2+ mobilisation remains elusive. Herein we report the expression of gamma-aminobutyric acid type A receptor delta subunit (GABRD) in human and rodent sperm and its involvement in mediating the progesterone-induced acrosome reaction. GABRD was localised in the sperm head/neck region. A δ(392–422)-specific inhibitory peptide against GABRD blocked the progesterone-induced acrosome reaction and the associated increase in intracellular Ca2+. Similarly, an inhibitory effect against both progesterone-indu
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18

Kreindler, James L., Marta Troyanovskaya, and Phillip A. Wackym. "Ligand-Gated Purinergic Receptors are Differentially Expressed in the Adult Rat Vestibular Periphery." Annals of Otology, Rhinology & Laryngology 110, no. 3 (2001): 277–82. http://dx.doi.org/10.1177/000348940111000314.

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To further characterize the pattern of expression of the ligand-gated purinergic P2X receptors in the peripheral vestibular system, we conducted reverse transcription—polymerase chain reaction amplification of P2X1 and P2X2 messenger RNA extracted from adult rat vestibular ganglia (Scarpa's ganglia) and vestibular end organs. Transcripts encoding P2X1 were found in both Scarpa's ganglia and the end organs, but transcripts encoding P2X2 were found only in the vestibular end organs. These results support previous electrophysiological data, and they provide a more complete understanding of the sp
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19

Spelta, Valeria, Abdelaziz Mekhalfia, Dominik Rejman, Mark Thompson, G. Michael Blackburn, and R. Alan North. "ATP analogues with modified phosphate chains and their selectivity for rat P2X2 and P2X2/3 receptors." British Journal of Pharmacology 140, no. 6 (2003): 1027–34. http://dx.doi.org/10.1038/sj.bjp.0705531.

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20

Hausmann, Ralf, Mandy Bodnar, Ronja Woltersdorf, et al. "ATP Binding Site Mutagenesis Reveals Different Subunit Stoichiometry of Functional P2X2/3 and P2X2/6 Receptors." Journal of Biological Chemistry 287, no. 17 (2012): 13930–43. http://dx.doi.org/10.1074/jbc.m112.345207.

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21

Burgard, Edward C., Wende Niforatos, Tim van Biesen, et al. "P2X Receptor–Mediated Ionic Currents in Dorsal Root Ganglion Neurons." Journal of Neurophysiology 82, no. 3 (1999): 1590–98. http://dx.doi.org/10.1152/jn.1999.82.3.1590.

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Nociceptive neurons in the dorsal root ganglia (DRG) are activated by extracellular ATP, implicating P2X receptors as potential mediators of painful stimuli. However, the P2X receptor subtype(s) underlying this activity remain in question. Using electrophysiological techniques, the effects of P2X receptor agonists and antagonists were examined on acutely dissociated adult rat lumbar DRG neurons. Putative P2X-expressing nociceptors were identified by labeling neurons with the lectin IB4. These neurons could be grouped into three categories based on response kinetics to extracellularly applied A
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22

Schmidt, Axel, Sylvia Joussen, Ralf Hausmann, Stefan Gründer, and Dominik Wiemuth. "Bile acids are potent inhibitors of rat P2X2 receptors." Purinergic Signalling 15, no. 2 (2019): 213–21. http://dx.doi.org/10.1007/s11302-019-09657-2.

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23

Allsopp, Rebecca C., Louise K. Farmer, Alistair G. Fryatt, and Richard J. Evans. "P2X Receptor Chimeras Highlight Roles of the Amino Terminus to Partial Agonist Efficacy, the Carboxyl Terminus to Recovery from Desensitization, and Independent Regulation of Channel Transitions." Journal of Biological Chemistry 288, no. 29 (2013): 21412–21. http://dx.doi.org/10.1074/jbc.m113.464651.

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P2X receptor subtypes can be distinguished by their sensitivity to ATP analogues and selective antagonists. We have used chimeras between human P2X1 and P2X2 receptors to address the contribution of the extracellular ligand binding loop, transmembrane segments (TM1 and TM2), and intracellular amino and carboxyl termini to the action of partial agonists (higher potency and efficacy of BzATP and Ap5A at P2X1 receptors) and antagonists. Sensitivity to the antagonists NF449, suramin, and PPADS was conferred by the nature of the extracellular loop (e.g. nanomolar for NF449 at P2X1 and P2X2-1EXT and
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24

Chen, Lin, Changlong Leng, Qin Ru, Qi Xiong, Mei Zhou, and Yuxiang Wu. "Retrograde Labeling of Different Distribution Features of DRG P2X2 and P2X3 Receptors in a Neuropathic Pain Rat Model." BioMed Research International 2020 (July 23, 2020): 1–15. http://dx.doi.org/10.1155/2020/9861459.

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The distributions of P2X subtypes during peripheral neuropathic pain conditions and their differential roles are not fully understood. To explore these characteristics, the lumbosacral dorsal root ganglion (DRG) in the chronic constriction injury (CCI) sciatic nerve rat model was studied. Retrograde trace labeling combined with immunofluorescence technology was applied to analyze the distribution of neuropathic nociceptive P2X1-6 receptors. Our results suggest that Fluoro-Gold (FG) retrograde trace labeling is an efficient method for studying lumbosacral DRG neurons in the CCI rat model, espec
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25

Punthambaker, Sukanya, Jacob A. Blum, and Richard I. Hume. "High Potency Zinc Modulation of Human P2X2 Receptors and Low Potency Zinc Modulation of Rat P2X2 Receptors Share a Common Molecular Mechanism." Journal of Biological Chemistry 287, no. 26 (2012): 22099–111. http://dx.doi.org/10.1074/jbc.m112.369157.

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26

Ishii, Toshiyuki, Kohei Homma, Asuka Mano, et al. "Novel channel-mediated choline transport in cholinergic neurons of the mouse retina." Journal of Neurophysiology 118, no. 4 (2017): 1952–61. http://dx.doi.org/10.1152/jn.00506.2016.

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Choline uptake into the presynaptic terminal of cholinergic neurons is mediated by the high-affinity choline transporter and is essential for acetylcholine synthesis. In a previous study, we reported that P2X2 purinoceptors are selectively expressed in OFF-cholinergic amacrine cells of the mouse retina. Under specific conditions, P2X2 purinoceptors acquire permeability to large cations, such as N-methyl-d-glucamine, and therefore potentially could act as a noncanonical pathway for choline entry into neurons. We tested this hypothesis in OFF-cholinergic amacrine cells of the mouse retina. ATP-i
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27

Samways, Damien S. K., and Terrance M. Egan. "Acidic Amino Acids Impart Enhanced Ca2+ Permeability and Flux in Two Members of the ATP-gated P2X Receptor Family." Journal of General Physiology 129, no. 3 (2007): 245–56. http://dx.doi.org/10.1085/jgp.200609677.

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P2X receptors are ATP-gated cation channels expressed in nerve, muscle, bone, glands, and the immune system. The seven family members display variable Ca2+ permeabilities that are amongst the highest of all ligand-gated channels (Egan and Khakh, 2004). We previously reported that polar residues regulate the Ca2+ permeability of the P2X2 receptor (Migita et al., 2001). Here, we test the hypothesis that the formal charge of acidic amino acids underlies the higher fractional Ca2+ currents (Pf%) of the rat and human P2X1 and P2X4 subtypes. We used patch-clamp photometry to measure the Pf% of HEK-2
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28

Cheung, Kwok-Kuen, and Geoffrey Burnstock. "Localization of P2X3 receptors and coexpression with P2X2 receptors during rat embryonic neurogenesis." Journal of Comparative Neurology 443, no. 4 (2002): 368–82. http://dx.doi.org/10.1002/cne.10123.

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29

Moffatt, Luciano, and Richard I. Hume. "Responses of Rat P2X2 Receptors to Ultrashort Pulses of ATP Provide Insights into ATP Binding and Channel Gating." Journal of General Physiology 130, no. 2 (2007): 183–201. http://dx.doi.org/10.1085/jgp.200709779.

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To gain insight into the way that P2X2 receptors localized at synapses might function, we explored the properties of outside-out patches containing many of these channels as ATP was very rapidly applied and removed. Using a new method to calibrate the speed of exchange of solution over intact patches, we were able to reliably produce applications of ATP lasting <200 μs. For all concentrations of ATP, there was a delay of at least 80 μs between the time when ATP arrived at the receptor and the first detectable flow of inward current. In response to 200-μs pulses of ATP, the time constant
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30

North, R. Alan. "Molecular Physiology of P2X Receptors." Physiological Reviews 82, no. 4 (2002): 1013–67. http://dx.doi.org/10.1152/physrev.00015.2002.

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P2X receptors are membrane ion channels that open in response to the binding of extracellular ATP. Seven genes in vertebrates encode P2X receptor subunits, which are 40–50% identical in amino acid sequence. Each subunit has two transmembrane domains, separated by an extracellular domain (∼280 amino acids). Channels form as multimers of several subunits. Homomeric P2X1, P2X2, P2X3, P2X4, P2X5, and P2X7channels and heteromeric P2X2/3and P2X1/5channels have been most fully characterized following heterologous expression. Some agonists (e.g., αβ-methylene ATP) and antagonists [e.g., 2′,3′- O-(2,4,
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31

Clyne, J. D., T. C. Brown, and R. I. Hume. "Expression level dependent changes in the properties of P2X2 receptors." Neuropharmacology 44, no. 3 (2003): 403–12. http://dx.doi.org/10.1016/s0028-3908(02)00406-9.

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32

Kowalski, Maria, Ralf Hausmann, Julia Schmid, et al. "Flexible subunit stoichiometry of functional human P2X2/3 heteromeric receptors." Neuropharmacology 99 (December 2015): 115–30. http://dx.doi.org/10.1016/j.neuropharm.2015.07.008.

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33

Chaumont, S., V. Compan, E. Toulme, et al. "Regulation of P2X2 Receptors by the Neuronal Calcium Sensor VILIP1." Science Signaling 1, no. 41 (2008): ra8. http://dx.doi.org/10.1126/scisignal.1162329.

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34

Tittle, R. K., and R. I. Hume. "Opposite Effects of Zinc on Human and Rat P2X2 Receptors." Journal of Neuroscience 28, no. 44 (2008): 11131–40. http://dx.doi.org/10.1523/jneurosci.2763-08.2008.

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35

Spelta, Valeria, Lin-Hua Jiang, Annmarie Surprenant, and R. Alan North. "Kinetics of antagonist actions at rat P2X2/3 heteromeric receptors." British Journal of Pharmacology 135, no. 6 (2002): 1524–30. http://dx.doi.org/10.1038/sj.bjp.0704591.

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36

Shcherbatko, Anatoly, Davide Foletti, Kris Poulsen, et al. "Modulation of P2X3 and P2X2/3 Receptors by Monoclonal Antibodies." Journal of Biological Chemistry 291, no. 23 (2016): 12254–70. http://dx.doi.org/10.1074/jbc.m116.722330.

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37

Gasparri, Federica, Jesper Wengel, Thomas Grutter, and Stephan A. Pless. "Molecular determinants for agonist recognition and discrimination in P2X2 receptors." Journal of General Physiology 151, no. 7 (2019): 898–911. http://dx.doi.org/10.1085/jgp.201912347.

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P2X receptors (P2XRs) are trimeric ligand-gated ion channels that open a cation-selective pore in response to ATP binding. P2XRs contribute to synaptic transmission and are involved in pain and inflammation, thus representing valuable drug targets. Recent crystal structures have confirmed the findings of previous studies with regards to the amino acid chains involved in ligand recognition, but they have also suggested that backbone carbonyl atoms contribute to ATP recognition and discrimination. Here we use a combination of site-directed mutagenesis, amide-to-ester substitutions, and a range o
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Costantin, James L., Timothy Strassmaier, Giustina M. Rotordam, et al. "Kinetic and Pharmacological Properties of P2X3 and P2X2/3 Receptors." Biophysical Journal 118, no. 3 (2020): 118a—119a. http://dx.doi.org/10.1016/j.bpj.2019.11.787.

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Antonio, LS, AP Stewart, XJ Xu, WA Varanda, RD Murrell-Lagnado, and JM Edwardson. "P2X4 receptors interact with both P2X2 and P2X7 receptors in the form of homotrimers." British Journal of Pharmacology 163, no. 5 (2011): 1069–77. http://dx.doi.org/10.1111/j.1476-5381.2011.01303.x.

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Ruan, Huai-Zhen, Lori A. Birder, William C. de Groat, et al. "Localization of P2X and P2Y Receptors in Dorsal Root Ganglia of the Cat." Journal of Histochemistry & Cytochemistry 53, no. 10 (2005): 1273–82. http://dx.doi.org/10.1369/jhc.4a6556.2005.

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The distribution of P2X and P2Y receptor subtypes in upper lumbosacral cat dorsal root ganglia (DRG) has been investigated using immunohistochemistry. Intensity of immunoreactivity for six P2X receptors (P2X5 receptors were immuno-negative) and the three P2Y receptors examined in cat DRG was in the order of P2Y2 = P2Y4>P2X3>P2X2 = P2X7>P2X6>P2X1 = P2X4>P2Y1. P2X3, P2Y2, and P2Y4 receptor polyclonal antibodies stained 33.8%, 35.3%, and 47.6% of DRG neurons, respectively. Most P2Y2, P2X1, P2X3, P2X4, and P2X6 receptor staining was detected in small- and medium-diameter neurons. Ho
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41

George, Benjamin, Kenton J. Swartz, and Mufeng Li. "Hearing loss mutations alter the functional properties of human P2X2 receptor channels through distinct mechanisms." Proceedings of the National Academy of Sciences 116, no. 45 (2019): 22862–71. http://dx.doi.org/10.1073/pnas.1912156116.

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Activation of P2X2 receptor channels by extracellular ATP is thought to play important roles in cochlear adaptation to elevated sound levels and protection from overstimulation. Each subunit of a trimeric P2X2 receptor is composed of intracellular N and C termini, a large extracellular domain containing the ATP binding site and 2 transmembrane helices (TM1 and TM2) that form a cation permeable pore. Whole-exome sequencing and linkage analysis have identified 3 hP2X2 receptor mutations (V60L, D273Y, and G353R) that cause dominantly inherited progressive sensorineural hearing loss (DFNA41). Avai
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Punthambaker, Sukanya, and Richard I. Hume. "Potent and long-lasting inhibition of human P2X2 receptors by copper." Neuropharmacology 77 (February 2014): 167–76. http://dx.doi.org/10.1016/j.neuropharm.2013.09.001.

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43

Staikopoulos, V., B. J. Sessle, J. B. Furness, and E. A. Jennings. "Localization of P2X2 and P2X3 receptors in rat trigeminal ganglion neurons." Neuroscience 144, no. 1 (2007): 208–16. http://dx.doi.org/10.1016/j.neuroscience.2006.09.035.

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Stelmashenko, Olga, Ulyana Lalo, Yue Yang, Laricia Bragg, R. Alan North, and Vincent Compan. "Activation of Trimeric P2X2 Receptors by Fewer than Three ATP Molecules." Molecular Pharmacology 82, no. 4 (2012): 760–66. http://dx.doi.org/10.1124/mol.112.080903.

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Bongartz, Eva-Verena, Jürgen Rettinger, and Ralf Hausmann. "Aminoglycoside block of P2X2 receptors heterologously expressed in Xenopus laevis oocytes." Purinergic Signalling 6, no. 4 (2010): 393–403. http://dx.doi.org/10.1007/s11302-010-9204-9.

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Gasparri, Federica, Jesper Wengel, Thomas Grutter, and Stephan Pless. "Effects of Ligand Conformations and Hetero-Liganded States on P2X2 Receptors." Biophysical Journal 112, no. 3 (2017): 421a. http://dx.doi.org/10.1016/j.bpj.2016.11.2250.

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Hu, Bo, Chen Yu Chiang, James W. Hu, Jonathan O. Dostrovsky, and Barry J. Sessle. "P2X Receptors in Trigeminal Subnucleus Caudalis Modulate Central Sensitization in Trigeminal Subnucleus Oralis." Journal of Neurophysiology 88, no. 4 (2002): 1614–24. http://dx.doi.org/10.1152/jn.2002.88.4.1614.

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This study investigated the role of trigeminal subnucleus caudalis (Vc) P2X receptors in the mediation of central sensitization induced in nociceptive neurons in subnucleus oralis (Vo) by mustard oil (MO) application to the tooth pulp in anesthetized rats. MO application produced a long-lasting central sensitization reflected in neuroplastic changes (i.e., increases in neuronal mechanoreceptive field size and responses to innocuous and noxious mechanical stimuli) in Vo nociceptive neurons. Twenty minutes after MO application, the intrathecal (i.t.) administration to the rostral Vc of the selec
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Kwong, Kevin, Marian Kollarik, Christina Nassenstein, Fei Ru, and Bradley J. Undem. "P2X2 receptors differentiate placodal vs. neural crest C-fiber phenotypes innervating guinea pig lungs and esophagus." American Journal of Physiology-Lung Cellular and Molecular Physiology 295, no. 5 (2008): L858—L865. http://dx.doi.org/10.1152/ajplung.90360.2008.

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The lungs and esophagus are innervated by sensory neurons with somata in the nodose, jugular, and dorsal root ganglion. These sensory ganglia are derived from embryonic placode (nodose) and neural crest tissues (jugular and dorsal root ganglia; DRG). We addressed the hypothesis that the neuron's embryonic origin (e.g., placode vs. neural crest) plays a greater role in determining particular aspects of its phenotype than the environment in which it innervates (e.g., lungs vs. esophagus). This hypothesis was tested using a combination of extracellular and patch-clamp electrophysiology and single
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Tsuzuki, Kenzo, Ariel Ase, Philippe Séguéla, et al. "TNP-ATP-Resistant P2X Ionic Current on the Central Terminals and Somata of Rat Primary Sensory Neurons." Journal of Neurophysiology 89, no. 6 (2003): 3235–42. http://dx.doi.org/10.1152/jn.01171.2002.

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P2X receptors have been suggested to be expressed on the central terminals of Aδ-afferent fibers innervating dorsal horn lamina V and play a role in modulating sensory synaptic transmission. These P2X receptors have been widely thought to be P2X2+3 receptors. However, we have recently found that P2X receptor-mediated modulation of sensory transmission in lamina V is not inhibited by trinitrophenyl-adenosine triphosphate (TNP-ATP), a potent antagonist of P2X1, P2X3 homomers, and P2X2+3 heteromers. To provide direct evidence for the presence of TNP-ATP-resistant P2X receptors on primary afferent
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Florenzano, F., M. T. Viscomi, F. Cavaliere, C. Volonté, and M. Molinari. "Cerebellar lesion up-regulates P2X1 and P2X2 purinergic receptors in precerebellar nuclei." Neuroscience 115, no. 2 (2002): 425–34. http://dx.doi.org/10.1016/s0306-4522(02)00397-4.

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