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Special Issue "Purinergic P2 Receptors: Structure and Function"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 30 April 2020.

Special Issue Editor

Dr. Hana Zemkova
E-Mail Website
Guest Editor
Institute of Physiology, Czech Academy of Sciences, Videnska 1083, 142 20 Prague 4, Czech Republic
Interests: secretion of hormones and neurotransmitters; ion channels; ATP release; P2X receptors; molecular structure

Special Issue Information

Dear Colleagues,

ATP (adenosine-5´-triphosphate) is a multifunctional intracellular molecule that serves as an energy source in all living cells. Much less is known about its role as an extracellular messenger or neurotransmitter. Extracellular ATP and its metabolic products acts on its plasma membrane receptors termed purinergic receptors, composed of two families: the ion-conducting P2X receptor channels and G protein-coupled P2Y receptors. By mediating depolarization, Ca2+ influx, and Ca2+ mobilization from intracellular stores, the extracellular nucleotide/P2 receptor system has numerous functions in excitable and nonexcitable cells. P2X and P2Y receptors have been documented in many physiological and pathological processes including inflammation, pain, and cancer and are potential therapeutic targets for treatment of these pathologies. This perspective is closely related to understanding the molecular physiology of these receptors that might be activated simultaneously if expressed in the same cell.

This issue aims to present the contemporary research on structural insights into the function of P2X and P2Y receptors, and their physiology and pharmacology. It may include original articles covering experimental reports on some particular receptor, technical development or novel screening technologies, as well as review papers relating to the subjects.

Dr. Hana Zemkova
Guest Editor

Manuscript Submission Information

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Keywords

  • Extracellular ATP
  • Purinergic signaling
  • P2X receptor
  • P2Y receptor
  • ATP release
  • Molecular structure
  • Molecular pathway

Published Papers (3 papers)

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Research

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Open AccessArticle
Increased Purinergic Responses Dependent on P2Y2 Receptors in Hepatocytes from CCl4-Treated Fibrotic Mice
Int. J. Mol. Sci. 2020, 21(7), 2305; https://doi.org/10.3390/ijms21072305 (registering DOI) - 26 Mar 2020
Abstract
Inflammatory and wound healing responses take place during liver damage, primarily in the parenchymal tissue. It is known that cellular injury elicits an activation of the purinergic signaling, mainly by the P2X7 receptor; however, the role of P2Y receptors in the onset of [...] Read more.
Inflammatory and wound healing responses take place during liver damage, primarily in the parenchymal tissue. It is known that cellular injury elicits an activation of the purinergic signaling, mainly by the P2X7 receptor; however, the role of P2Y receptors in the onset of liver pathology such as fibrosis has not been explored. Hence, we used mice treated with the hepatotoxin CCl4 to implement a reversible model of liver fibrosis to evaluate the expression and function of the P2Y2 receptor (P2Y2R). Fibrotic livers showed an enhanced expression of P2Y2R that eliminated its zonal distribution. Hepatocytes from CCl4-treated mice showed an exacerbated ERK-phosphorylated response to the P2Y2R-specific agonist, UTP. Cell proliferation was also enhanced in the fibrotic livers. Hepatic transcriptional analysis by microarrays, upon CCl4 administration, showed that P2Y2 activation regulated diverse pathways, revealing complex action mechanisms. In conclusion, our data indicate that P2Y2R activation is involved in the onset of the fibrotic damage associated with the reversible phase of the hepatic damage promoted by CCl4. Full article
(This article belongs to the Special Issue Purinergic P2 Receptors: Structure and Function)
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Open AccessArticle
Interaction between Calcium Chelators and the Activity of P2X7 Receptors in Mouse Motor Synapses
Int. J. Mol. Sci. 2020, 21(6), 2034; https://doi.org/10.3390/ijms21062034 - 16 Mar 2020
Abstract
The ability of P2X7 receptors to potentiate rhythmically evoked acetylcholine (ACh) release through Ca2+ entry via P2X7 receptors and via L-type voltage-dependent Ca2+ channels (VDCCs) was compared by loading Ca2+ chelators into motor nerve terminals. Neuromuscular preparations of the diaphragms [...] Read more.
The ability of P2X7 receptors to potentiate rhythmically evoked acetylcholine (ACh) release through Ca2+ entry via P2X7 receptors and via L-type voltage-dependent Ca2+ channels (VDCCs) was compared by loading Ca2+ chelators into motor nerve terminals. Neuromuscular preparations of the diaphragms of wild-type (WT) mice and pannexin-1 knockout (Panx1−/−) mice, in which ACh release is potentiated by the disinhibition of the L-type VDCCs upon the activation of P2X7 receptors, were used. Miniature end-plate potentials (MEPPs) and evoked end-plate potentials (EPPs) were recorded when the motor terminals were loaded with slow or fast Ca2+ chelators (EGTA-AM or BAPTA-AM, respectively, 50 μM). In WT and Panx1−/− mice, EGTA-AM did not change either spontaneous or evoked ACh release, while BAPTA-AM inhibited synaptic transmission by suppressing the quantal content of EPPs throughout the course of the short rhythmic train (50 Hz, 1 s). In the motor synapses of either WT or Panx1−/− mice in the presence of BAPTA-AM, the activation of P2X7 receptors by BzATP (30 μM) returned the EPP quantal content to the control level. In the neuromuscular junctions (NMJs) of Panx1−/− mice, EGTA-AM completely prevented the BzATP-induced increase in EPP quantal content. After Panx1−/− NMJs were treated with BAPTA-AM, BzATP lost its ability to enhance the EPP quantal content to above the control level. Nitrendipine (1 μM), an inhibitor of L-type VDCCs, was unable to prevent this BzATP-induced enhancement of EPP quantal content to the control level. We propose that the activation of P2X7 receptors may provide additional Ca2+ entry into motor nerve terminals, which, independent of the modulation of L-type VDCC activity, can partially reduce the buffering capacity of Ca2+ chelators, thereby providing sufficient Ca2+ signals for ACh secretion at the control level. However, the activity of both Ca2+ chelators was sufficient to eliminate Ca2+ entry via L-type VDCCs activated by P2X7 receptors and increase the EPP quantal content in the NMJs of Panx1−/− mice to above the control level. Full article
(This article belongs to the Special Issue Purinergic P2 Receptors: Structure and Function)
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Review

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Open AccessReview
Guanosine-Based Nucleotides, the Sons of a Lesser God in the Purinergic Signal Scenario of Excitable Tissues
Int. J. Mol. Sci. 2020, 21(5), 1591; https://doi.org/10.3390/ijms21051591 - 26 Feb 2020
Abstract
Purines are nitrogen compounds consisting mainly of a nitrogen base of adenine (ABP) or guanine (GBP) and their derivatives: nucleosides (nitrogen bases plus ribose) and nucleotides (nitrogen bases plus ribose and phosphate). These compounds are very common in nature, especially in a phosphorylated [...] Read more.
Purines are nitrogen compounds consisting mainly of a nitrogen base of adenine (ABP) or guanine (GBP) and their derivatives: nucleosides (nitrogen bases plus ribose) and nucleotides (nitrogen bases plus ribose and phosphate). These compounds are very common in nature, especially in a phosphorylated form. There is increasing evidence that purines are involved in the development of different organs such as the heart, skeletal muscle and brain. When brain development is complete, some purinergic mechanisms may be silenced, but may be reactivated in the adult brain/muscle, suggesting a role for purines in regeneration and self-repair. Thus, it is possible that guanosine-5′-triphosphate (GTP) also acts as regulator during the adult phase. However, regarding GBP, no specific receptor has been cloned for GTP or its metabolites, although specific binding sites with distinct GTP affinity characteristics have been found in both muscle and neural cell lines. Finally, even if the cross regulation mechanisms between the two different purines (ABP and GBP) are still largely unknown, it is now possible to hypothesize the existence of specific signal paths for guanosine-based nucleotides that are capable of modulating the intensity and duration of the intracellular signal, particularly in excitable tissues such as brain and muscle. Full article
(This article belongs to the Special Issue Purinergic P2 Receptors: Structure and Function)
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