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Blockade of the P2X7 receptor reduces cyst formation via ERK (show MAPK1 Proteins)-dependent pathways in a zebrafish model of polycystic kidney disease.
The results indicate that P2X7 receptors may play a significant role in contributing to the unwanted activation of mast cells in chronic inflammatory conditions where extracellular ATP levels are elevated
In vitro and in vivo results provide support for the involvement of an oxidative stress through P2X7 receptor activation and mitochondrial dysfunction in the pathophysiology of oxaliplatin-induced neuronal injury and likely to painful neuropathy.
Eight Single nucleotide polymorphisms loci, including rs1653624, rs10160951, rs1718119, rs7958316, rs16950860, rs208294, rs17525809 and rs2230912, were screened and detected, and rs1653624, rs7958316 and rs17525809 were associated with gout arthritis. P2X7R function associated single nucleotide polymorphisms may be related to gouty arthritis.
The loss-of-function SNP rs2230911 in P2X7, that negatively affect NLRP3 (show NLRP3 Proteins)-inflammasome activation, confers susceptibility toward active pulmonary tuberculosis in Brazilian Amazon cohort.
this review discusses P2X7R structure and its contribution to inflammation and host defense
P2X7R expression was correlated with enhanced tumor grade and metastasis in colorectal carcinoma patients.
Our present study shows that loss of function of the P2X7 receptor in mice induces retinal changes representing characteristics of early age-related macular degeneration.
Single nucleotide polymorphism in P2X7R gene is associated with pulmonary non-tuberculous mycobacterial disease.
Our results reveal that P2RX7 rs2230911 may be associated with primary gout risk in a Chinese Han male population and allele G may be a susceptibility factor for primary gout.
Together, this body of research suggests that P2X7R may constitute an important therapeutic target for a variety of neurological disorders.
For the inflammasome-dependent IL-1beta (show IL1B Proteins) release, bovine monocytes require ATP in addition to a primary stimulus. This IL-1beta (show IL1B Proteins) release depends on potassium efflux, but, in contrast to human and murine monocytes, does not require calcium influx or generation of reaction oxygen and is independent of the P2X7 receptor.
we show that P2X7 activation prolongs and potentiates Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling in osteoblasts
Our data indicate that P2X7 exerts a role in limiting the early edema formation, possibly by modulating glial responses, and supports later microglia activation after transient middle cerebral artery occlusion
Extracellular ATP reduces the replication of VSV, Newcastle disease virus, murine leukemia virus and HSV in vivo and in vitro through the P2X7 receptor; ATP increases IFN-beta (show IFNB1 Proteins) expression. Mechanistically, ATP facilitates IFN-beta (show IFNB1 Proteins) secretion through P38 (show CRK Proteins)/JNK (show MAPK8 Proteins)/ATF-2 (show ATF2 Proteins) signaling pathways, which are crucial in promoting antiviral immunity.
P2X7R activation induces the production of proinflammatory cytokines, including IL-1beta (show IL1B Proteins) and IL-18 (show IL18 Proteins), by inducing the oligomerization of the multiprotein complex NLRP3 (show NLRP3 Proteins)-type inflammasome.
there are several potential mechanisms for the antidepressant phenotype of P2rx7-/- mice, such as the absence of P2rx7-mediated glutamate (show GRIN1 Proteins) release, elevated basal BDNF (show BDNF Proteins) production, enhanced neurogenesis and increased 5-HT (show DDC Proteins) bioavailability in the hippocampus.
This study provides a new insight into malaria immunology by showing the importance of P2X7 receptor in controlling the fine-tuning between Th1 (show HAND1 Proteins) and Tfh cell differentiation during P. chabaudi infection
Critical Role for P2X7 Receptor-Induced VCAM-1 (show VCAM1 Proteins) Shedding and Neutrophil Infiltration during Acute Lung Injury
These data support that P2X7 and P2X4 (show P2RX4 Proteins) receptor activation has a protective effect during severe Escherichia coli infection.
The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel and is responsible for ATP-dependent lysis of macrophages through the formation of membrane pores permeable to large molecules. Activation of this nuclear receptor by ATP in the cytoplasm may be a mechanism by which cellular activity can be coupled to changes in gene expression. Multiple alternatively spliced variants have been identified, most of which fit nonsense-mediated decay (NMD) criteria.
P2X purinoceptor 7
, purinergic receptor P2X, ligand-gated ion channel, 7
, p2X purinoceptor 7-like
, ATP receptor
, P2X7 receptor
, P2Z receptor
, purinergic receptor P2X7 variant A
, P2X7 purinoceptor
, purinergic receptor P2X7