Comparison of mRNA Expression of P2X Receptor Subtypes in Different Arterial Tissues of Rats

Li, Lingzhi; Yue, Li-hui; Zhang, Zhimin; Zhao, Jing; Ren, Lei-Ming; Wang, Hongjie; Li, Lü

doi:10.1007/s10528-020-09968-9

Cited by 3 publications

(1 citation statement)

References 21 publications

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“…When ATP binds to a P2X receptor, it causes cytomembrane depolarization and the subsequent elevation of the intracellular calcium concentration, either by direct Ca 2+ permeation or by the activation of voltage-gated Ca 2+ channels, which triggers a range of signaling cascades, resulting in both short- and long-term cellular events ( 7 ). P2X receptors are widely expressed in a number of tissues and cells ( 8 ). However, P2X7R differs from the other P2XRs to a certain degree.…”

Section: Introductionmentioning

confidence: 99%

Potential mechanisms of osteoprotegerin-induced damage to osteoclast adhesion structures via P2X7R-mediated MAPK signaling

Shi

Zhao

et al. 2022

Int J Mol Med

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Osteoprotegerin (OPG) is a negative regulator of osteoclast formation by competing with receptor activator of the nuclear factor-κB (NF-κB) ligand (RANKL) for RANK. OPG is not only a soluble decoy receptor for RANKL, but is also considered as a direct effector of osteoclast functions. However, the mechanismsresponsible for OPG-induced changes to osteoclast bone resorption functionsremain unknown. P2X7R is involved in the process of multinucleation and cell fusion. Therefore, in the present study, mitogen-activated protein kinase (MAPK) inhibitors and the RNA interference of purinergic receptor P2X7 (P2X7R) were usedtoexamine the effects of P2X7R-mediated MAPK signaling on changes to osteoclast adhesion structure induced by OPG; for this purpose, western blot analysis and immunofluorescence staining were performed. The results revealed that OPG inhibited osteoclast adhesion-related protein expression, disrupted adhesion protein distribution, and destroyed osteoclast filopodia and lamellipodia structures. The inhibitors partially restored osteoclast adhesion structure, including protein expression, distribution and cell morphology. The absence of P2X7R markedly inhibited osteoclast formation, and subsequent OPG treatment accelerated the damage to adhesion structures. However, P2X7R activation significantly recosvered the phosphorylation of paxillin, vinculin, phosphorylated protein tyrosine kinase 2 and SRc proto-oncogene, non-receptor tyrosine kinase induced by OPG, and their distribution was uniform at the osteoclast periphery. P2X7R silencing suppressed the phosphorylation of MAPK. On the whole, the findings of the present study highlighta key role of P2X7R/MAPK signaling in osteoclast adhesion, and provide a novel therapeutic target for bone disease.

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Section: Introductionmentioning

confidence: 99%

Potential mechanisms of osteoprotegerin-induced damage to osteoclast adhesion structures via P2X7R-mediated MAPK signaling

Shi

Zhao

et al. 2022

Int J Mol Med

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Purinergic regulation of pulmonary vascular tone

Alveal,

Méndez,

García

et al. 2024

Purinergic Signalling

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Ionotropic P2X4 and P2X7 receptors in the regulation of ion transport across rat colon

Ballout

Claßen

Richter

et al. 2022

British J Pharmacology

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Background and purpose: ATP plays an important role as an extracellular messenger acting via different types of purinoceptors. Whereas most of the actions of ATP at intestinal epithelia are thought to be mediated by metabotropic P2Y receptors, the role of ionotropic P2X receptors remains unclear. Consequently, we investigated the role of P2X4 and P2X7 receptors on ion transport across rat colonic epithelia by using BzATP, a potent agonist at P2X7 (and weak agonist at P2X4).Experimental approach: Ussing chamber and Ca 2+ imaging experiments were performed on rat colonic epithelia, combined with P2X receptor expression studies.Key results: Ussing chamber experiments revealed that serosal BzATP induced a neuronally mediated increase in short-circuit current caused by Cl À secretion. In contrast, the effect of mucosal BzATP was smaller, insensitive to tetrodotoxin and Cl À -independent. When epithelia were basolaterally depolarized to measure currents across the apical membrane, BzATP stimulated a cation current consistent with the activation of apical nonselective cation channels. Experiments with isolated colonic crypts revealed a BzATP-induced increase in the cytosolic Ca 2+ concentration. Sensitivity to antagonists indicates stimulation of P2X4 and P2X7 receptors by serosal BzATP and of P2X7 receptors by mucosal BzATP. A similar pattern was observed with native ATP, which induced larger transepithelial currents in comparison to BzATP. RT-PCR and immunohistochemistry experiments confirmed the expression of P2X4 and P2X7 receptors in the colon localized in the epithelium and in submucosal ganglia. Conclusions and implications: Epithelial and neuronal ionotropic P2X receptors are involved in the regulation of intestinal ion transport.

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Comparison of mRNA Expression of P2X Receptor Subtypes in Different Arterial Tissues of Rats

Cited by 3 publications

References 21 publications

Potential mechanisms of osteoprotegerin-induced damage to osteoclast adhesion structures via P2X7R-mediated MAPK signaling

Potential mechanisms of osteoprotegerin-induced damage to osteoclast adhesion structures via P2X7R-mediated MAPK signaling

Purinergic regulation of pulmonary vascular tone

Ionotropic P2X4 and P2X7 receptors in the regulation of ion transport across rat colon

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