Academic literature on the topic 'P2X2-receptors'

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Journal articles on the topic "P2X2-receptors"

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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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "P2X2-receptors"

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Lindner, Anna. "Untersuchung der Interaktion der Untereinheiten im humanen P2X2- und P2X2/3-Rezeptor durch Cystein-substituierte Aminosäuren." Doctoral thesis, Universitätsbibliothek Leipzig, 2015. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-189913.

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P2X-Rezeptoren treten aufgrund ihrer Präsenz in verschiedensten Organsystemen des menschlichen Körpers zunehmend in den Mittelpunkt zahlreicher Forschungsansätze. Besonderes Interesse gilt dabei u.a. den P2X2/3-Rezeptoren, da in ihnen ein neuer Angriffspunkt für die Entwicklung von Schmerztherapeutika gesehen wird. Trotz enormer Fortschritte in diesem Bereich, bleiben die Vorgänge und strukturellen Gegebenheiten, die zur Öffnung der Ionenkanäle führen, weiterhin spekulativ. In der vorliegenden Arbeit wurden mithilfe einer Mutagenese einzelne Aminosäuren des hP2X2-Rezeptors, welche sich in geri
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Wang, Haihong. "Amino acid residues constituting the agonist binding site of the human P2X3 receptor and subunit stoichiometry of heteromeric P2X2/3 and P2X2/6 receptors." Doctoral thesis, Universitätsbibliothek Leipzig, 2013. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-112913.

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Homotrimeric P2X3 and heteromeric P2X2/3 receptors are present in sensory ganglia and participate in pain perception. In order to develop pharmacological antagonists for these receptors, it is important to clarify which amino acid (AA) residues constitute the agonist binding pouch as well as to learn the stoichiometry of the receptor subunits forming a heteromeric receptor. We expressed the homomeric human (h)P2X3 receptor or its mutants in HEK293 cells and measured the ATP-induced responses by the whole-cell patch-clamp method. For the binding-site mutants, all conserved and some non-conserve
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Wang, Haihong [Verfasser], Peter [Akademischer Betreuer] Illes, Wolfgang [Gutachter] Nörenberg, and Andreas [Gutachter] Reichenbach. "Amino acid residues constituting the agonist binding site of the human P2X3 receptor and subunit stoichiometry of heteromeric P2X2/3 and P2X2/6 receptors / Haihong Wang ; Gutachter: Wolfgang Nörenberg, Andreas Reichenbach ; Betreuer: Peter Illes." Leipzig : Universitätsbibliothek Leipzig, 2013. http://d-nb.info/1238366546/34.

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Majumder, Paromita. "Análise dos receptores P2X2 e P2X4 durante a diferenciação neuronal." Universidade de São Paulo, 2007. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-05102007-145008/.

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Durante o desenvolvimento do sistema nervoso, as oscilações da concentração de cálcio intracelular livre resultam na proliferação celular, migração e diferenciação neuronal. Nesta tese foram investigadas a participação dos receptores ionotrópicos purinérgicos dos tipos P2X2 e P2X4 seletivos ao influxo de cálcio durante a diferenciação neuronal in vitro das células de carcinoma embrionário murino P19. Identificamos o padrão diferencial de expressão de receptores purinérgicos nas células indiferenciadas e neurônios P19. O receptor P2X4 é expresso durante toda a diferenciação neuronal e o
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Wang, Haihong. "Amino acid residues constituting the agonist binding site of the human P2X3 receptor and subunit stoichiometry of heteromeric P2X2/3 and P2X2/6 receptors." Doctoral thesis, 2012. https://ul.qucosa.de/id/qucosa%3A11905.

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Homotrimeric P2X3 and heteromeric P2X2/3 receptors are present in sensory ganglia and participate in pain perception. In order to develop pharmacological antagonists for these receptors, it is important to clarify which amino acid (AA) residues constitute the agonist binding pouch as well as to learn the stoichiometry of the receptor subunits forming a heteromeric receptor. We expressed the homomeric human (h)P2X3 receptor or its mutants in HEK293 cells and measured the ATP-induced responses by the whole-cell patch-clamp method. For the binding-site mutants, all conserved and some non-conserve
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Chow, Yu-wen, and 周郁雯. "Investigating the structure-function relationship of P2X2 receptors with the aid of site-directed mutagenesis and electrophysiological characterizations." Thesis, 1997. http://ndltd.ncl.edu.tw/handle/96485288398260249877.

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碩士<br>長庚醫學暨工程學院<br>基礎醫學研究所<br>85<br>Adenosine-5'-triphosphate (ATP) 除了在細胞內扮演著能量來源的 角色外, 近年來被認為在中樞和周圍神經系統中也扮演著神經傳導物質 (neurotransmitter) 的生理功能. ATP 的作用是經由活化 P2X 受體而興 奮神經元及收縮血管或內臟器官的平滑肌. 最近利用分子生物學的方法, 已有七種 P2X 受體的亞型(subtypes) 被發現. 根據 hydropathy analysis 推測其分子構造, 包含了 兩段 transmembrane domains (M1 and M2), 一段 extracellular loop 與兩段 intracellular domains (N- and C-terminal regions). P2X 受體與各種已知的受體離子通道 (ligand-gated channels) 有明顯的不同, 且在胺基酸序列上, P2X 受體 和其它受體離子通到也不具相似性 (h
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Conference papers on the topic "P2X2-receptors"

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Finger, Thomas, and Brigit High. "Absence of P2X2 purinergic receptors in human taste bud innervation." In ERS International Congress 2020 abstracts. European Respiratory Society, 2020. http://dx.doi.org/10.1183/13993003.congress-2020.2575.

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