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Data found that P2RX4, which is abundantly expressed in vascular endothelial cells, is required for ischemic tolerance following middle artery occlusion in mice, and demonstrate a novel mechanism whereby vascular endothelial cells are involved in ischemic tolerance.
P2RX4-signaling contributes to allergen induces airway inflammation pathogenesis by regulating dendritic cell mediated Th2 cell priming via modulating IL-1ss secretion.
Study demonstrates that microglia-derived ATP differentially modulates synaptic transmission and short-term plasticity at hippocampal mossy fibre synapses by acting, respectively, on presynaptic P2X4 receptors and on adenosine A1 receptors after conversion of extracellular ATP to adenosine.
These data support that P2X7 (show P2RX7 Proteins) and P2X4 receptor activation has a protective effect during severe Escherichia coli infection.
This study provides a molecular mechanism for lysosomal ATP transport mediated by SLC17A9 and also suggests a regulatory mechanism of lysosomal P2X4 by SLC17A9
IRF5 (show IRF5 Proteins) expression in microglia is regulated by IRF8 (show IRF8 Proteins). IRF5 (show IRF5 Proteins) directly upregulates P2rX4 expression on microglia in peripheral nerve injury, and may play a role in neuropathic pain.
Specific localization of the P2X4 receptor subunit was evaluated in mouse, rat and cat retinae using fluorescence immunohistochemistry and pre-embedding immuno-electron microscopy
P2X4 receptors contribute to ethanol intake and indicate that there is a complex interaction between P2X4 receptors and ethanol.
Loss of P2X4 expression is associated with exaggerated renal fibrosis following unilateral ureteric obstruction.
There is a protective role for endogenous cardiac myocyte P2X4R in heart failure. It is demonstrated in a physical interaction between the myocyte receptor and eNOS (show NOS3 Proteins).
Our study nominates rare genetic variants in P2RX4 and P2RX7 (show P2RX7 Proteins) as major genetic contributors to disease, further supporting a role for these purinergic receptors in MS and the disruption of transmembrane cation channels leading to impairment of phagocytosis as the pathological mechanisms of disease
the intersubunit physical couplings among the DF and two lower body domains fostered by the LF domain at the open state act as an integrated structural element that is stringently required for the channel gating of P2X4 receptors.
These findings provide new insights in understanding the contribution of the salt bridge between Asp (show ASIP Proteins)-85 and Arg-309 and its structurally coupled beta2,3-sheet to the function of P2X4 receptors.
The results suggest a role of PrP(C (show PRNP Proteins)) in proteostasis, dysfunctions of which may be involved in the pathogenesis of neurodegenerative diseases such as TSE and Alzheimer's Disease.
Fndings support role for P2X7 (show P2RX7 Proteins) and P2X4 coupled to induction of inflammatory molecules in modulating high glucose and palmitate-induced endothelial cell activation and dysfunction.
These data suggest that vascular smooth muscle cells from human gastro-omental arteries express P2X1 (show P2RX1 Proteins) and P2X4 receptor subunits
This study demonstrates a major physiological finding that the shear-induced effects on endothelial KLF2 (show KLF2 Proteins) axis are in part dependent on ATP release and P2X4, a previously unidentified mechanism.
Using pHluorin, P2X4 was found to be expressed on the plasma membrane and within subcellular compartments in hippocampus.
It appears to mediate the cells' response to extracellular ATP. Although Ca2thorn influx via P2X1 receptor is necessary for alpha-synuclein accumulation.
P2X4 and calmodulin form a complex at endolysosomal membrane where P2X4 activation recruits calmodulin to promote fusion and vacuolation in a Ca(2 (show CA2 Proteins)+)-dependent fashion.
The renal epithelial Na channel is stimulated by P2Xreceptor activation; the stimulation is dependent on increases in intracellular Ca(2 (show CA2 Proteins)) and phosphatidylinositol 3-kinase activation.
A point mutation in ectodomain-transmembrane 2 of P2X4 receptor significantly reduces ethanol's inhibitory effects.
ATP-recognition of P2X4 receptors
a property that is essential for purinergic sensory signaling. Apo (show C9orf3 Proteins) and ATP-bound X-ray structures of the detergent-solubilized zebrafish P2X4 receptor provide a blueprint for receptor mechanisms
crystal structure of the zebrafish P2X4 receptor in complex with ATP and a new structure of the apo (show C9orf3 Proteins) receptor
Cloning and characterization of zebrafish P2X4 and P2X5 (show P2RX5 Proteins).
Comparison of the acid-sensing ion channel (show ACCN2 Proteins) structure with the ATP-gated P2X(4) receptor reveals similarity in pore architecture and aqueous vestibules
The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel with high calcium permeability. The main pharmacological distinction between the members of the purinoceptor family is the relative sensitivity to the antagonists suramin and PPADS. The product of this gene has the lowest sensitivity for these antagonists. Multiple alternatively spliced transcript variants, some protein-coding and some not protein-coding, have been found for this gene.
purinergic receptor P2X4
, purinergic receptor P2X, ligand-gated ion channel, 4
, p2X purinoceptor 4-like
, ATP receptor
, P2X purinoceptor 4
, ionotropic purinergic receptor
, ATP-gated cation channel protein
, P2X receptor, subunit 4
, purinoceptor P2X4
, P2X4 purinoceptor
, ATP-gated ion channel subunit P2X4