High impact information on P2rx4

• Furthermore, P2rx4(-/-) mice have higher blood pressure and excrete smaller amounts of NO products in their urine than do wild-type mice [1].
• P2rx4(-/-) mice do not have normal endothelial cell responses to flow, such as influx of Ca(2+) and subsequent production of the potent vasodilator nitric oxide (NO) [1].
• INTRODUCTION: Osteoclasts express functional P2X4 and P2X7 receptors, which are ATP-gated cation channels [2].
• Preincubation with a low concentration of ATP, the natural agonist of the P2X4 receptor, also protected the motor neurons against a subsequent excitotoxic stimulation, while high concentrations of ATP were toxic [3].
• Preincubation with both P2X4 modulators did not influence the number or Ca2+ permeability of the AMPA receptors and addition during kainate stimulation alone had no effect [3].

Biological context of P2rx4

• In the presence of the P2X4 receptor-selective allosteric enhancer ivermectin (3 microM), the 2-meSATP-stimulated current increased significantly in both WT and TG ventricular cells, consistent with an important role of P2X4 receptors in mediating the ATP current not only in TG but also WT myocytes [4].
• Use of the polymerase chain reaction coupled with reverse transcription showed that mouse clonal early proximal tubule (S1) cell line (NF-5) and outer medullary collecting tubule (OMCT) cells expressed mRNA for P2X4, P2Y1 and P2Y2 purinoceptors [5].
• Here we report the generation of a P2X4 receptor knock-out mouse and show that long-term potentiation (LTP) at Schaffer collateral synapses is reduced relative to that in wild-type mice [6].

Anatomical context of P2rx4

• These results suggest that in undifferentiated PC12 cells ATP mainly acts on a P2X receptor, possibly the P2X4 subtype [7].
• When expressed in Xenopus laevis oocytes, mP2X4 produces a rapid inward current in response to ATP with an EC50 of 1.68+/-0.2 microM, consistent with the affinity of the rat and human P2X4 receptors for ATP [8].
• Membrane currents under voltage clamp were determined in myocytes from both wild-type (WT) and P2X4 receptor-overexpressing transgenic (TG) mice [4].
• The objective of the present study was to characterize the electrophysiologic actions of P2X4 receptors in cardiac myocytes and to determine whether they are involved in mediating the effect of extracellular ATP [4].
• Significant expression of P2X4 and P2X7 proteins was immunodetected in dystrophic myoblasts [9].

Associations of P2rx4 with chemical compounds

• The P2X antagonist suramin was only able to block partially the 2-meSATP-stimulated current in WT cells, implying that both P2X4 receptor and another yet-to-be-identified P2X receptor mediate this current [4].

Physical interactions of P2rx4

• Homotrimers of P2X7 were able to co-immunoprecipitate with P2X4, suggesting that an interaction occurs between rather than within receptor complexes [10].

Analytical, diagnostic and therapeutic context of P2rx4

• Molecular cloning, functional characterization and possible cooperativity between the murine P2X4 and P2X4a receptors [8].

References