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Journal articles on the topic 'P2X7'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Coutinho-Silva, Robson, Lynn Stahl, Kwok-Kuen Cheung, et al. "P2X and P2Y purinergic receptors on human intestinal epithelial carcinoma cells: effects of extracellular nucleotides on apoptosis and cell proliferation." American Journal of Physiology-Gastrointestinal and Liver Physiology 288, no. 5 (2005): G1024—G1035. http://dx.doi.org/10.1152/ajpgi.00211.2004.

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Extracellular nucleotides interact with purinergic receptors, which regulate ion transport in a variety of epithelia. With the use of two different human epithelial carcinoma cell lines (HCT8 and Caco-2), we have shown by RT-PCR that the cells express mRNA for P2X1, P2X3, P2X4, P2X5, P2X6, P2X7, P2Y1, P2Y2, P2Y4, P2Y6, P2Y11, and P2Y12 receptors. Protein expression for P2Y1 and P2Y2 receptors was also demonstrated immunohistochemically, and P2X receptor subtype protein was present in the following decreasing order: P2X4 > P2X7 > P2X1 > P2X3 > P2X6 > P2X5 >> P2X2. The funct

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2

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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3

Birder, L. A., H. Z. Ruan, B. Chopra, et al. "Alterations in P2X and P2Y purinergic receptor expression in urinary bladder from normal cats and cats with interstitial cystitis." American Journal of Physiology-Renal Physiology 287, no. 5 (2004): F1084—F1091. http://dx.doi.org/10.1152/ajprenal.00118.2004.

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Purinergic mechanisms appear to be involved in motor as well as sensory functions in the urinary bladder. ATP released from efferent nerves excites bladder smooth muscle, whereas ATP released from urothelial cells can activate afferent nerves and urothelial cells. In the present study, we used immunohistochemical techniques to examine the distribution of purinoceptors in the urothelium, smooth muscle, and nerves of the normal cat urinary bladder as well as possible changes in the expression of these receptors in cats with a chronic painful bladder condition termed feline interstitial cystitis

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4

Lee, B. M., H. Jo, G. Park, et al. "Extracellular ATP Induces Calcium Signaling in Odontoblasts." Journal of Dental Research 96, no. 2 (2016): 200–207. http://dx.doi.org/10.1177/0022034516671308.

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Odontoblasts form dentin at the outermost surface of tooth pulp. An increasing level of evidence in recent years, along with their locational advantage, implicates odontoblasts as a secondary role as sensory or immune cells. Extracellular adenosine triphosphate (ATP) is a well-characterized signaling molecule in the neuronal and immune systems, and its potential involvement in interodontoblast communications was recently demonstrated. In an effort to elaborate the ATP-mediated signaling pathway in odontoblasts, the current study performed single-cell reverse transcription polymerase chain reac

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5

Baines, Abigail, Katie Parkinson, Joan A. Sim, Laricia Bragg, Christopher R. L. Thompson, and R. Alan North. "Functional Properties of Five Dictyostelium discoideum P2X Receptors." Journal of Biological Chemistry 288, no. 29 (2013): 20992–1000. http://dx.doi.org/10.1074/jbc.m112.445346.

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The Dictyostelium discoideum genome encodes five proteins that share weak sequence similarity with vertebrate P2X receptors. Unlike vertebrate P2X receptors, these proteins are not expressed on the surface of cells, but populate the tubules and bladders of the contractile vacuole. In this study, we expressed humanized cDNAs of P2XA, P2XB, P2XC, P2XD, and P2XE in human embryonic kidney cells and altered the ionic and proton environment in an attempt to reflect the situation in amoeba. Recording of whole-cell membrane currents showed that four receptors operated as ATP-gated channels (P2XA, P2XB

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6

Ruan, Huai Zhen, Lori A. Birder, Zhenghua Xiang, et al. "Expression of P2X and P2Y receptors in the intramural parasympathetic ganglia of the cat urinary bladder." American Journal of Physiology-Renal Physiology 290, no. 5 (2006): F1143—F1152. http://dx.doi.org/10.1152/ajprenal.00333.2005.

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The distribution and function of P2X and P2Y receptor subtypes were investigated on intact or cultured intramural ganglia of the cat urinary bladder by immunocytochemistry and calcium-imaging techniques, respectively. Neurons were labeled by all seven P2X receptor subtype antibodies and antibodies for P2Y2, P2Y4, P2Y6, and P2Y12 receptor subtypes with a staining intensity of immunoreactivity in the following order: P2X3=P2Y2=P2Y4=P2Y6=P2Y12>P2X1=P2X2=P2X4>P2X5=P2X6=P2X7. P2Y1 receptor antibodies labeled glial cells, but not neurons. P2X3 and P2Y4 polyclonal antibodies labeled ∼95 and 40%

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7

Roberts, V. H. J., S. L. Greenwood, A. C. Elliott, C. P. Sibley, and L. H. Waters. "Purinergic receptors in human placenta: evidence for functionally active P2X4, P2X7, P2Y2, and P2Y6." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 290, no. 5 (2006): R1374—R1386. http://dx.doi.org/10.1152/ajpregu.00612.2005.

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Appropriate regulation of ion transport by the human placental syncytiotrophoblast is important for fetal growth throughout pregnancy. In nonplacental tissues, ion transport can be modulated by extracellular nucleotides that raise intracellular calcium ([Ca2+]i) via activation of purinergic receptors. We tested the hypothesis that purinergic receptors are expressed by human placental cytotrophoblast cells and that their activation by extracellular nucleotides modulates ion (K+) efflux and [Ca2+]i. P2X/P2Y receptor agonists 5-bromouridine 5′-triphosphate (5-BrUTP), ADP, ATP, 2′,3′- O-(4-benzoyl

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8

Nakamura, Ei'Ichiro, Yasuhito Uezono, Ken'Ichiro Narusawa, et al. "ATP activates DNA synthesis by acting on P2X receptors in human osteoblast-like MG-63 cells." American Journal of Physiology-Cell Physiology 279, no. 2 (2000): C510—C519. http://dx.doi.org/10.1152/ajpcell.2000.279.2.c510.

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In human osteoblast-like MG-63 cells, extracellular ATP increased [3H]thymidine incorporation and cell proliferation and synergistically enhanced platelet-derived growth factor- or insulin-like growth factor I-induced [3H]thymidine incorporation. ATP-induced [3H]thymidine incorporation was mimicked by the nonhydrolyzable ATP analogs adenosine 5′- O-(3-thiotriphosphate) and adenosine 5′-adenylylimidodiphosphate and was inhibited by the P2 purinoceptor antagonist suramin, suggesting involvement of P2 purinoceptors. The P2Y receptor agonist UTP and UDP and a P2Y receptor antagonist reactive blue

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9

Ramirez, Angelina N., and Diana L. Kunze. "P2X purinergic receptor channel expression and function in bovine aortic endothelium." American Journal of Physiology-Heart and Circulatory Physiology 282, no. 6 (2002): H2106—H2116. http://dx.doi.org/10.1152/ajpheart.00892.2001.

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We examined bovine aortic endothelial cells (BAECs) for the functional expression of P2X receptors, the ATP-gated cation channels. We identified the P2X subtypes present in BAECs using RT-PCR. mRNA was present for only three of seven family members: P2X4, P2X5, and P2X7. We then characterized agonist-activated currents in whole cell and outside-out patch recordings using 2-methyl-thio-ATP (MeSATP) as a P2X4 and P2X5 receptor agonist and 2′,3′- O-(4-benzoylbenzoyl)ATP (BzATP) as a P2X7 receptor agonist. MeSATP (10–20 μM) produced current with characteristics of P2X4 receptors. The current was a

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10

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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11

Rivera, Ian, Shali Zhang, B. Scott Fuller, et al. "P2 receptor regulation of [Ca2+]i in cultured mouse mesangial cells." American Journal of Physiology-Renal Physiology 292, no. 5 (2007): F1380—F1389. http://dx.doi.org/10.1152/ajprenal.00349.2006.

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Experiments were performed to establish the pharmacological profile of purinoceptors and to identify the signal transduction pathways responsible for increases in intracellular calcium concentration ([Ca2+]i) for cultured mouse mesangial cells. Mouse mesangial cells were loaded with fura 2 and examined using fluorescent spectrophotometry. Basal [Ca2+]i averaged 102 ± 2 nM ( n = 346). One hundred micromolar concentrations of ATP, ADP, 2′,3′-(benzoyl-4-benzoyl)-ATP (BzATP), ATP-γ-S, and UTP in normal Ca2+ medium evoked peak increases in [Ca2+]i of 866 ± 111, 236 ± 18, 316 ± 26, 427 ± 37, and 808

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12

Trang, Mira, Günther Schmalzing, Christa E. Müller, and Fritz Markwardt. "Dissection of P2X4 and P2X7 Receptor Current Components in BV-2 Microglia." International Journal of Molecular Sciences 21, no. 22 (2020): 8489. http://dx.doi.org/10.3390/ijms21228489.

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Microglia cells represent the immune system of the central nervous system. They become activated by ATP released from damaged and inflamed tissue via purinergic receptors. Ionotropic purinergic P2X4 and P2X7 receptors have been shown to be involved in neurological inflammation and pain sensation. Whether the two receptors assemble exclusively as homotrimers or also as heterotrimers is still a matter of debate. We investigated the expression of P2X receptors in BV-2 microglia cells applying the whole-cell voltage-clamp technique. We dissected P2X4 and P2X7 receptor-mediated current components b

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13

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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14

Layhadi, Janice A., and Samuel J. Fountain. "ATP-Evoked Intracellular Ca2+ Responses in M-CSF Differentiated Human Monocyte-Derived Macrophage are Mediated by P2X4 and P2Y11 Receptor Activation." International Journal of Molecular Sciences 20, no. 20 (2019): 5113. http://dx.doi.org/10.3390/ijms20205113.

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Tissues differentially secrete multiple colony stimulating factors under conditions of homeostasis and inflammation, orientating recruited circulating monocytes to differentiate to macrophage with differing functional phenotypes. Here, we investigated ATP-evoked intracellular Ca2+ responses in human macrophage differentiated with macrophage colony-stimulating factor (M-CSF). Extracellular ATP evoked (EC50 13.3 ± 1.4 μM) robust biphasic intracellular Ca2+ responses that showed a dependency on both metabotropic (P2Y) and ionotropic (P2X) receptors. qRT-PCR and immunocytochemistry revealed the ex

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15

Gui, Yu, ZengYong Wang, XiaoRui Sun, et al. "Uridine adenosine tetraphosphate induces contraction of airway smooth muscle." American Journal of Physiology-Lung Cellular and Molecular Physiology 301, no. 5 (2011): L789—L794. http://dx.doi.org/10.1152/ajplung.00203.2011.

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Contraction of airway smooth muscle (ASM) plays an important role in the regulation of air flow and is potentially involved in the pathophysiology of certain respiratory diseases. Extracellular nucleotides regulate ASM contraction via purinergic receptors, but the signaling mechanisms involved are not fully understood. Uridine adenosine tetraphosphate (Up4A) contains both pyrimidine and purine moieties, which are known to potentially activate P2X and P2Y receptors. Both P2X and P2Y receptors have been identified in the lung, including airway epithelial cells and ASM. We report here a study of

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16

Bujko, Kamila, Mateusz Adamiak, Arjun Thapa, Magdalena Kucia, Janina Ratajczak, and Mariusz Z. Ratajczak. "Novel Evidence That Extracellular Adenosine Triphosphate (ATP), As a Purinergic Signaling Mediator, Activates Mobilization By Engaging a P2X4 Ligand-Gated Cation Channel Receptor Expressed on the Surface of Hematopoietic and Innate Immunity Cells." Blood 134, Supplement_1 (2019): 4472. http://dx.doi.org/10.1182/blood-2019-125858.

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Background . Adenosine triphosphate (ATP) is an important nucleotide involved in intracellular energy transfer, but it is also released from activated cells into the extracellular space as a crucial component of the purinergic signaling network. Purinergic signaling is an ancient form of extracellular signaling that is mediated by ATP and other extracellular nucleotides (EXNs). Purinergic receptors for EXNs are expressed on the surface of all cells in the body; are represented by several families of P1, P2X, and P2Y receptors; and are among the most abundant receptors in living organisms. Of a

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17

Yamamoto, Kimiko, Risa Korenaga, Akira Kamiya, Zhi Qi, Masahiro Sokabe, and Joji Ando. "P2X4 receptors mediate ATP-induced calcium influx in human vascular endothelial cells." American Journal of Physiology-Heart and Circulatory Physiology 279, no. 1 (2000): H285—H292. http://dx.doi.org/10.1152/ajpheart.2000.279.1.h285.

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ATP induces Ca2+ influx across the cell membrane and activates release from intracellular Ca2+ pools in vascular endothelial cells (ECs). Ca2+ signaling leads to the modification of a variety of EC functions, including the production of vasoactive substances such as nitric oxide and prostacyclin. However, the molecular mechanisms for ATP-induced Ca2+ influx in ECs have not been thoroughly clarified. Here we demonstrate evidence that a P2X4receptor for an ATP-gated cation channel is predominantly expressed in human ECs and is involved in the ATP-induced Ca2+ influx. Northern blot analysis disti

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18

Challa, Siva Reddy, Hunter Levingston, Casimir A. Fornal, et al. "Temporal mRNA Expression of Purinergic P2 Receptors in the Brain Following Cerebral Ischemia and Reperfusion: Similarities and Distinct Variations Between Rats and Mice." International Journal of Molecular Sciences 26, no. 6 (2025): 2379. https://doi.org/10.3390/ijms26062379.

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Purinergic P2 receptors are crucial in energy utilization and cellular signaling, making them key targets for stroke therapies. This study examines the temporal mRNA expression of all P2 receptors in rats and mice. Both species exhibited a common subset of P2X and P2Y receptors with elevated expression following cerebral ischemia and reperfusion (I/R), highlighting conserved mechanisms across these species. The receptors with upregulated expression in both species were P2X3, P2X4, P2X7, P2Y2, and P2Y6. While these similarities were observed, notable differences in receptor expression emerged b

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Pippel, Anja, Michaela Stolz, Ronja Woltersdorf, Achim Kless, Günther Schmalzing, and Fritz Markwardt. "Localization of the gate and selectivity filter of the full-length P2X7 receptor." Proceedings of the National Academy of Sciences 114, no. 11 (2017): E2156—E2165. http://dx.doi.org/10.1073/pnas.1610414114.

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The P2X7 receptor (P2X7R) belongs to the P2X family of ATP-gated cation channels. P2X7Rs are expressed in epithelial cells, leukocytes, and microglia, and they play important roles in immunological and inflammatory processes. P2X7Rs are obligate homotrimers, with each subunit having two transmembrane helices, TM1 and TM2. Structural and functional data regarding the P2X2 and P2X4 receptors indicate that the central trihelical TM2 bundle forms the intrinsic transmembrane channel of P2X receptors. Here, we studied the accessibility of single cysteines substituted along the pre-TM2 and TM2 helix

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20

Mutini, Carmela, Simonetta Falzoni, Davide Ferrari, et al. "Mouse Dendritic Cells Express the P2X7 Purinergic Receptor: Characterization and Possible Participation in Antigen Presentation." Journal of Immunology 163, no. 4 (1999): 1958–65. http://dx.doi.org/10.4049/jimmunol.163.4.1958.

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Abstract Immune cells express P2 purinoceptors of the P2Y and P2X subtypes. In the present work, we show that three dendritic cell (DC) lines, D2SC/1, CB1, and FSDC, representative of immature DCs, express the P2X7 (formerly P2Z) receptor, as judged from RT-PCR amplification, reactivity to a specific antiserum, and pharmacological and functional evidence. Receptor expression is higher in FSDC cells, a cell line that is functionally more mature than D2SC/1 and CB1. From the wild-type DC population, we selected cell clones lacking the P2X7R (P2X7less). We also used a P2XR blocker, oxidized ATP,

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21

Cardoso, Andréia Machado, Maria Luiza Mukai Franciosi, and Adriana Wagner. "What is new in Purinergic Signaling and Cervical Cancer?" Cancer Research and Cellular Therapeutics 5, no. 2 (2021): 01–03. http://dx.doi.org/10.31579/2640-1053/084.

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Since our publication “Purinergic Signaling and Tumor Microenvironment in Cervical Cancer” [1], in early 2020, there has been a significant change in purinergic signaling research. The Coronavirus disease 2019 (COVID-19) significantly impacted the prevention, diagnosis, and treatment of cervical cancer [2]. In that previous review, we had addressed the possibilities of purinergic signaling in the tumor microenvironment of this type of cancer [1]. The conclusions were: the extracellular medium of cervical cancer is rich in adenosine triphosphate (ATP) and adenosine [3, 4, 5]; ATP is a pro-infla

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22

Li, Wanzhen, Shengyuan Wang, Tongyangzi Zhang, Yiqing Zhu, Li Yu, and Xianghuai Xu. "Activation of Adenosine Triphosphate-Gated Purinergic 2 Receptor Channels by Transient Receptor Potential Vanilloid Subtype 4 in Cough Hypersensitivity." Biomolecules 15, no. 2 (2025): 285. https://doi.org/10.3390/biom15020285.

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Background: Transient receptor potential vanilloid subtype 4 (TRPV4) is a Ca2+-permeable non-selective cation channel that is involved in the development of cough hypersensitivity. Purinergic 2 receptors (P2X) belong to a class of adenosine triphosphate (ATP)-gated non-selective cation channels that also play an important role in cough hypersensitivity. Nevertheless, little is known about the interaction between them for cough hypersensitivity. The present study was designed to clarify the roles of TRPV4 and ATP-P2X receptors in cough hypersensitivity, and to explore the possible involvement o

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23

Arkhipov, Sergey N., D’Anna L. Potter, Aron M. Geurts, and Tengis S. Pavlov. "Knockout of P2rx7 purinergic receptor attenuates cyst growth in a rat model of ARPKD." American Journal of Physiology-Renal Physiology 317, no. 6 (2019): F1649—F1655. http://dx.doi.org/10.1152/ajprenal.00395.2019.

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The severity of polycystic kidney diseases (PKD) depends on the counterbalancing of genetic predisposition and environmental factors exerting permissive or protective influence on cyst development. One poorly characterized phenomenon in the cystic epithelium is abnormal purinergic signaling. Earlier experimental studies revealed the high importance of the ionotropic P2X receptors (particularly, P2X7) in the pathophysiology of the cyst wall. To study mechanisms of P2X7 involvement in cyst growth and aspects of targeting these receptors in PKD treatment we performed a CRISPR/SpCas9-mediated glob

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24

Inoue, Hiroyuki, Hidetaka Kuroda, Wataru Ofusa, et al. "Functional Coupling between the P2X7 Receptor and Pannexin-1 Channel in Rat Trigeminal Ganglion Neurons." International Journal of Molecular Sciences 22, no. 11 (2021): 5978. http://dx.doi.org/10.3390/ijms22115978.

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The ionotropic P2X receptor, P2X7, is believed to regulate and/or generate nociceptive pain, and pain in several neuropathological diseases. Although there is a known relationship between P2X7 receptor activity and pain sensing, its detailed functional properties in trigeminal ganglion (TG) neurons remains unclear. We examined the electrophysiological and pharmacological characteristics of the P2X7 receptor and its functional coupling with other P2X receptors and pannexin-1 (PANX1) channels in primary cultured rat TG neurons, using whole-cell patch-clamp recordings. Application of ATP and Bz-A

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25

Iegorova, O., and O. Maximyuk. "P2X RECEPTORS AS A NOVEL PROMINENT PHARMACOLOGICAL TARGET FOR VARIOUS CNS DISORDERS [." Fiziolohichnyĭ zhurnal 70, no. 3 (2024): 79–87. http://dx.doi.org/10.15407/fz70.03.079.

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Purinergic P2X receptors, particularly P2X7 and P2X4, are pivotal in brain functioning and pathology, affecting various central nervous system diseases. This review delves into P2X receptors’ roles in various pathologies, including ischemia, epilepsy, COVID-19, some neurodegenerative and psychiatric disorders. P2X7’s involvement in neuroinflammatory processes through the activation of the NLRP3 inflammasome highlights its significant role in corresponding pathologies and their treatment, as seen in studies using selective receptor antagonists like JNJ-55308942. Similarly, P2X4 receptor, which

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Marques, Rita D., Pauline I. A. de Bruijn, Mads V. Sorensen, Markus Bleich, Helle A. Praetorius, and Jens Leipziger. "Basolateral P2X receptors mediate inhibition of NaCl transport in mouse medullary thick ascending limb (mTAL)." American Journal of Physiology-Renal Physiology 302, no. 4 (2012): F487—F494. http://dx.doi.org/10.1152/ajprenal.00570.2011.

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Extracellular nucleotides regulate epithelial transport via luminal and basolateral P2 receptors. Renal epithelia express multiple P2 receptors, which mediate significant inhibition of solute absorption. Recently, we identified several P2 receptors in the medullary thick ascending limb (mTAL) including luminal and basolateral P2Y2 receptors (Jensen ME, Odgaard E, Christensen MH, Praetorius HA, Leipziger J. J Am Soc Nephrol 18: 2062–2070, 2007). In addition, we found evidence for a basolateral P2X receptor. Here, we investigate the effect of basolateral ATP on NaCl absorption in isolated, perfu

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27

Adamiak, Mateusz, Arjun Thapa, Kamila Bujko, et al. "A Novel Underappreciated Role for the Extracellular Adenosine Triphosphate (ATP)-P2X4 Purinergic Receptor Axis in the Homing and Engraftment of HSPCs." Blood 136, Supplement 1 (2020): 32. http://dx.doi.org/10.1182/blood-2020-137123.

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Background. Adenosine triphosphate (ATP) is an important nucleotide involved in intracellular energy transfer, but when released from activated cells into the extracellular space as extracellular ATP (eATP) it becomes a crucial mediator of the purinergic signaling network. Purinergic receptors for extracellular nucleotides (EXNs), expressed on the surface of all cells in the body, are represented by the P1, P2X, and P2Y receptor families, which are among the most abundant receptors in living organisms. Of all these receptors, the P2X receptor family is most highly specific for eATP signaling a

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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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Woehrle, Tobias, Linda Yip, Abdallah Elkhal, et al. "Pannexin-1 hemichannel–mediated ATP release together with P2X1 and P2X4 receptors regulate T-cell activation at the immune synapse." Blood 116, no. 18 (2010): 3475–84. http://dx.doi.org/10.1182/blood-2010-04-277707.

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Abstract Engagement of T cells with antigen-presenting cells requires T-cell receptor (TCR) stimulation at the immune synapse. We previously reported that TCR stimulation induces the release of cellular adenosine-5′-triphosphate (ATP) that regulates T-cell activation. Here we tested the roles of pannexin-1 hemichannels, which have been implicated in ATP release, and of various P2X receptors, which serve as ATP-gated Ca2+ channels, in events that control T-cell activation. TCR stimulation results in the translocation of P2X1 and P2X4 receptors and pannexin-1 hemichannels to the immune synapse,

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Ziberi, Sihana, Mariachiara Zuccarini, Marzia Carluccio, et al. "Upregulation of Epithelial-To-Mesenchymal Transition Markers and P2X7 Receptors Is Associated to Increased Invasiveness Caused by P2X7 Receptor Stimulation in Human Glioblastoma Stem Cells." Cells 9, no. 1 (2019): 85. http://dx.doi.org/10.3390/cells9010085.

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Glioblastoma (GBM) stem cells (GSCs), which contribute to GBM unfavorable prognosis, show high expression levels of ATP/P2X7 receptors (P2X7R). Here, we reported that cells exposure to 2’(3’)-O-(4-benzoylbenzoyl)-ATP (BzATP), a P2X7R agonist, up-regulated the expression of markers associated to epithelial-to-mesenchymal transition (EMT), a process likely contributing to GSC malignancy, and increased GSC migration/invasiveness like the known EMT inducer, Transforming Growth Factor β1 (TGFβ1). These effects were coupled to phosphorylation of SMAD2, a downstream effector in the TGFβ pathway, sugg

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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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Salcman, Barbora, Rajia Bahri, Peter W. West, Chiara Tontini, Karen Affleck, and Silvia Bulfone-Paus. "P2X7 Receptor-Induced Human Mast Cell Degranulation Is Enhanced by Interleukin 33." International Journal of Molecular Sciences 25, no. 3 (2024): 1730. http://dx.doi.org/10.3390/ijms25031730.

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MCs are tissue-resident immune cells that strategically reside in barrier organs and respond effectively to a wide range of stimuli, such as IL-33, a mediator released upon epithelial damage. Adenosine triphosphate (ATP) accumulates at sites of tissue injury and is known to modulate MC activities. This study investigated how an inflammatory tissue environment rich in IL-33 modulates the ATP-mediated activation of MCs. Human primary MCs primed with IL-33 displayed a strongly increased response to ATP but not ADP. This resulted in increased degranulation, IL-8 release, and pERK1/2 signalling. Su

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De Salis, Sophie K. F., Lanxin Li, Zheng Chen, et al. "Alternatively Spliced Isoforms of the P2X7 Receptor: Structure, Function and Disease Associations." International Journal of Molecular Sciences 23, no. 15 (2022): 8174. http://dx.doi.org/10.3390/ijms23158174.

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The P2X7 receptor (P2X7R) is an ATP-gated membrane ion channel that is expressed by multiple cell types. Following activation by extracellular ATP, the P2X7R mediates a broad range of cellular responses including cytokine and chemokine release, cell survival and differentiation, the activation of transcription factors, and apoptosis. The P2X7R is made up of three P2X7 subunits that contain specific domains essential for the receptor’s varied functions. Alternative splicing produces P2X7 isoforms that exclude one or more of these domains and assemble in combinations that alter P2X7R function. T

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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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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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Liu, Cuiling, Simon Mather, Yu Huang, Christopher J. Garland, and Xiaoqiang Yao. "Extracellular ATP facilitates flow-induced vasodilatation in rat small mesenteric arteries." American Journal of Physiology-Heart and Circulatory Physiology 286, no. 5 (2004): H1688—H1695. http://dx.doi.org/10.1152/ajpheart.00576.2003.

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ATP can be released from endothelial cells, and this release is increased by intraluminal flow in blood vessels. In the present study, the effect of extracellular ATP (1 μM) on flow-induced vasodilatation was investigated in isolated and pressurized rat small mesenteric arteries. In the absence of extracellular ATP, only 46% of arteries developed dilatation in response to flow, and this response was both transient and unstable. In marked contrast, with ATP present, all vessels developed a prolonged and stable dilatation in response to flow. Even in the vessels that failed to respond to flow in

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Panupinthu, Nattapon, Joseph T. Rogers, Lin Zhao, et al. "P2X7 receptors on osteoblasts couple to production of lysophosphatidic acid: a signaling axis promoting osteogenesis." Journal of Cell Biology 181, no. 5 (2008): 859–71. http://dx.doi.org/10.1083/jcb.200708037.

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Nucleotides are released from cells in response to mechanical stimuli and signal in an autocrine/paracrine manner through cell surface P2 receptors. P2rx7−/− mice exhibit diminished appositional growth of long bones and impaired responses to mechanical loading. We find that calvarial sutures are wider in P2rx7−/− mice. Functional P2X7 receptors are expressed on osteoblasts in situ and in vitro. Activation of P2X7 receptors by exogenous nucleotides stimulates expression of osteoblast markers and enhances mineralization in cultures of rat calvarial cells. Moreover, osteogenesis is suppressed in

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Mikolajewicz, Nicholas, Delaney Smith, Svetlana V. Komarova, and Anmar Khadra. "High-affinity P2Y2 and low-affinity P2X7 receptor interaction modulates ATP-mediated calcium signaling in murine osteoblasts." PLOS Computational Biology 17, no. 6 (2021): e1008872. http://dx.doi.org/10.1371/journal.pcbi.1008872.

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The P2 purinergic receptor family implicated in many physiological processes, including neurotransmission, mechanical adaptation and inflammation, consists of ATP-gated non-specific cation channels P2XRs and G-protein coupled receptors P2YRs. Different cells, including bone forming osteoblasts, express multiple P2 receptors; however, how P2X and P2Y receptors interact in generating cellular responses to various doses of [ATP] remains poorly understood. Using primary bone marrow and compact bone derived osteoblasts and BMP2-expressing C2C12 osteoblastic cells, we demonstrated conserved features

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Spildrejorde, Mari, Rachael Bartlett, Leanne Stokes, et al. "R270C polymorphism leads to loss of function of the canine P2X7 receptor." Physiological Genomics 46, no. 14 (2014): 512–22. http://dx.doi.org/10.1152/physiolgenomics.00195.2013.

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The relative function of the P2X7 receptor, an ATP-gated ion channel, varies between humans due to polymorphisms in the P2RX7 gene. This study aimed to assess the functional impact of P2X7 variation in a random sample of the canine population. Blood and genomic DNA were obtained from 69 dogs selected as representatives of a cross section of different breeds. P2X7 function was determined by flow cytometric measurements of dye uptake and patch-clamp measurements of inward currents. P2X7 expression was determined by immunoblotting and immunocytochemistry. Sequencing was used to identify P2RX7 gen

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Hasko, George, Balazs Csoka, Zoltan Németh, Gabor Törö, Marco Idzko, and Andreas Zech. "ATP protects against sepsis through macrophage P2X7 purinergic receptors by enhancing bacterial killing (INC2P.407)." Journal of Immunology 194, no. 1_Supplement (2015): 55.1. http://dx.doi.org/10.4049/jimmunol.194.supp.55.1.

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Abstract Extracellular ATP binds to and signals through P2X7 receptors (P2X7R)s to modulate immune function in both inflammasome-dependent and independent manners. We show here using P2X7-/- mice as well as pharmacological receptor and channel ligands that ATP release through connexin/pannexin channels and subsequent P2X7R activation are crucial for the control of mortality, bacterial dissemination and inflammation following sepsis induced by cecal ligation and puncture. Our results with P2X7-/- bone-marrow chimeras, adoptive transfer of macrophages, and myeloid-specific P2X7-/- mice indicate

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Dal Ben, Diego, Michela Buccioni, Catia Lambertucci, et al. "Radioligands Targeting the Purinergic P2X Receptors." Cells 14, no. 13 (2025): 984. https://doi.org/10.3390/cells14130984.

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Purinergic P2X receptors have a wide distribution within the body and modulate a number of physiological processes, being also involved in the development and progression of inflammation-, neuroinflammation-, neurodegeneration-, and cancer-related diseases. Radioligands that can detect specific P2X receptor subtypes and reveal their level of expression are of key importance for the development of novel P2X modulators, for the depiction of the involvement of these proteins in physio-pathological processes, and for the availability of novel diagnostic tools to be used for imaging experiments in

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Agrawal, Ankita, and Alison Gartland. "P2X7 receptors: role in bone cell formation and function." Journal of Molecular Endocrinology 54, no. 2 (2015): R75—R88. http://dx.doi.org/10.1530/jme-14-0226.

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The role of the P2X7 receptor (P2X7R) is being explored with intensive interest in the context of normal bone physiology, bone-related diseases and, to an extent, bone cancer. In this review, we cover the current understanding of P2X7R regulation of bone cell formation, function and survival. We will discuss how the P2X7R drives lineage commitment of undifferentiated bone cell progenitors, the vital role of P2X7R activation in bone mineralisation and its relatively unexplored role in osteocyte function. We also review how P2X7R activation is imperative for osteoclast formation and its role in

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LIGHT, ALAN R., YING WU, RONALD W. HUGHEN, and PETER B. GUTHRIE. "Purinergic receptors activating rapid intracellular Ca2+ increases in microglia." Neuron Glia Biology 2, no. 2 (2005): 125–38. http://dx.doi.org/10.1017/s1740925x05000323.

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We provide both molecular and pharmacological evidence that the metabotropic, purinergic, P2Y6, P2Y12 and P2Y13 receptors and the ionotropic P2X4 receptor contribute strongly to the rapid calcium response caused by ATP and its analogues in mouse microglia. Real-time PCR demonstrates that the most prevalent P2 receptor in microglia is P2Y6 followed, in order, by P2X4, P2Y12, and P2X7 = P2Y13. Only very small quantities of mRNA for P2Y1, P2Y2, P2Y4, P2Y14, P2X3 and P2X5 were found. Dose-response curves of the rapid calcium response gave a potency order of: 2MeSADP>ADP=UDP=IDP=UTP>ATP>Bz

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Pacheco, Paulo Anastácio Furtado, Daniel Tadeu Gomes Gonzaga, Natalia Lidmar von Ranke, et al. "Synthesis, Biological Evaluation and Molecular Modeling Studies of Naphthoquinone Sulfonamides and Sulfonate Ester Derivatives as P2X7 Inhibitors." Molecules 28, no. 2 (2023): 590. http://dx.doi.org/10.3390/molecules28020590.

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ATP acts in the extracellular environment as an important signal, activating a family of receptors called purinergic receptors. In recent years, interest in the potential therapeutics of purinergic components, including agonists and antagonists of receptors, has increased. Currently, many observations have indicated that ATP acts as an important mediator of inflammatory responses and, when found in high concentrations in the extracellular space, is related to the activation of the P2X7 purinergic receptor. In this sense, the search for new inhibitors for this receptor has attracted a great dea

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Salvestrini, Valentina, Stefania Orecchioni, Francesca Reggiani, et al. "P2X7 Receptor Activation By ATP As Target of Novel Therapies in Acute Myeloid Leukemia." Blood 126, no. 23 (2015): 3684. http://dx.doi.org/10.1182/blood.v126.23.3684.3684.

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Abstract ATP is the key energy molecule as well as an ubiquitous extracellular messenger. Depending on its dose and the engaged purinergic P2 receptor (P2R) subtype, ATP can trigger many different cell responses, including proliferation and cell death. Recent studies have shown that high ATP level exhibits direct cytotoxicity on many tumor cell types. Among the receptors engaged by ATP, P2X7 is the most consistently expressed by tumor cells and its overexpression is related to tumor growth and progression. The P2X7 is an ATP-gated ion channel that, upon sustained stimulation with millimolar AT

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Høyer, Eva Risborg, Melisa Demir, Lasse Kristoffer Bak, Niklas Rye Jørgensen, and Ankita Agrawal. "Expression of the Purinergic P2X7 Receptor in Murine MOPC315.BM Myeloma Cells." Receptors 2, no. 3 (2023): 191–203. http://dx.doi.org/10.3390/receptors2030013.

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The adenosine-5’ triphosphate (ATP)-gated, ion channel, P2X receptor superfamily has seven members expressed by many cancer types. Subtype 7 (P2X7 receptor) is expressed consistently at levels higher than in comparatively healthy tissues. Moreover, transcript variant heterogeneity is associated with drug resistance. We have previously described the role of the P2X7 receptor in myeloma, a rare blood disease that uniquely presents with aggressive bone destruction. In this study, we used known agonists of the P2X7 receptor to induce calcium influx and YO-PRO-1 uptake in murine MOPC315.BM myeloma

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Estrada, Juan A., Guillaume P. Ducrocq, Joyce S. Kim, and Marc P. Kaufman. "Intrathecal injection of brilliant blue G, a P2X7 antagonist, attenuates the exercise pressor reflex in rats." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 319, no. 2 (2020): R223—R232. http://dx.doi.org/10.1152/ajpregu.00093.2020.

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Purinergic 2X (P2X) receptors on the endings of group III and IV afferents play a role in evoking the exercise pressor reflex. Particular attention has been paid to P2X3 receptors because their blockade in the periphery attenuated this reflex. In contrast, nothing is known about the role played by P2X receptors in the spinal cord in evoking the exercise pressor reflex in rats. P2X7 receptors, in particular, may be especially important in this regard because they are found in abundance on spinal glial cells and may communicate with neurons to effect reflexes controlling cardiovascular function.

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Faccinetto, Celine, Christelle Lecut, Roland Greimers, Vincent Bours, and Cecile Oury. "New Role for ATP P2X1 Receptors in the Control of Neutrophil Apoptosis and Respiratory Burst Activity." Blood 108, no. 11 (2006): 1647. http://dx.doi.org/10.1182/blood.v108.11.1647.1647.

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Abstract P2X receptors are membrane non-selective cation channels that open in response to the binding of extracellular ATP. Seven genes encode P2X receptor subunits (P2X1–7) in vertebrates. Channels form homo- or hetero-multimers of several subunits that are highly permeable to Ca2+. P2X receptors are widely distributed. In recent years, increasing attention has been paid to extracellular ATP as a candidate danger signal locally released at the inception of inflammation. One of the most striking features of ATP is its ability to promote P2X7 receptor-mediated massive release of mature IL-1β f

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Harris, T. H., M. R. Wallace, H. Huang, H. Li, and L. M. Shaddox. "Associations of P2RX7 Functional Diplotypes with Localized Aggressive Periodontitis." JDR Clinical & Translational Research 4, no. 4 (2019): 342–51. http://dx.doi.org/10.1177/2380084419863789.

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Aim: The purpose of this study was to test for the role of the P2X7 receptor in localized aggressive periodontitis (LAP). Methods: Peripheral blood was obtained from 95 subjects with LAP and 76 healthy unrelated controls (HUCs). Three P2RX7 single-nucleotide polymorphisms (rs1718119, rs2230911, and rs3751143) were genotyped from these subjects, and their peripheral blood samples were stimulated with lipopolysaccharide (LPS) from Escherichia coli and tested for inflammatory markers. The 3 P2RX7 single-nucleotide polymorphisms were in found to be in perfect linkage disequilibrium, and a total of

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Huang, Andrew Chih Wei, Hsi-Chien Shih, and Bai Chuang Shyu. "The P2X7 Hypothesis of Central Post-Stroke Pain." International Journal of Molecular Sciences 25, no. 12 (2024): 6577. http://dx.doi.org/10.3390/ijms25126577.

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The present study examined how P2X7 receptor knockout (KO) modulates central post-stroke pain (CPSP) induced by lesions of the ventrobasal complex (VBC) of the thalamus in behaviors, molecular levels, and electrical recording tests. Following the experimental procedure, the wild-type and P2X7 receptor KO mice were injected with 10 mU/0.2 μL type IV collagenase in the VBC of the thalamus to induce an animal model of stroke-like thalamic hemorrhage. Behavioral data showed that the CPSP group induced thermal and mechanical pain. The P2X7 receptor KO group showed reduced thermal and mechanical pai

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