P2RX7

Official Full Name

purinergic receptor P2X 7

Organism

Homo sapiens

GeneID

5027

Background

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. [provided by RefSeq, Jul 2010]

Synonyms

P2X7;

Cat.No.	Product Name	Price

Cat.No.	Product Name	Price

Cat.No.	Product Name	Price

Cat.No.	Product Name	Price

Detailed Information

Overview:

ATP and other nucleotides, as well as nucleosides, are important extracellular signaling molecules that operate through complex purine energy signaling networks. The network consists of a number of membrane receptors and ectoenzymes, including P2X7 receptors. The P2X7 receptor is encoded by the P2RX7 gene and belongs to the P2X family of trimer ligand gated cationic channels, in which there are seven different members (p2x1-7). Of the P2X family, the P2X7 monomer subunit is the largest, with a length of 595 amino acids. Each subunit is characterized by relatively short and long amino and carboxyl (C) ends in the cell, and two hydrophobic membranes across segments (transmembrane domain) separated by a long glycosylated extracellular ATP binding domain.

P2RX7 Figure 1. Simplified illustration of extracellular purinergic signaling.
(https://commons. wikimedia. org/wiki/File:Purinergic_signalling. jpg#/media/File:Purinergic_signalling. jpg)

Structure:

P2X7 receptor is a ligand-gated cation channel that opens in response to ATP binding and leads to cell depolarization. The P2X7 receptor requires higher levels of ATP than other P2X receptors. However, the response can be potentiated by reducing the concentration of divalent cations such as calcium or magnesium. Continued binding leads to increased permeability to N-methyl-D-glucamine (NMDG+). P2X7 receptors do not become desensitized readily and continued signaling leads to the aforementioned increased permeability and an increase in current amplitude.

Distributions:

P2X7 is widely distributed in mammals. This receptor was initially thought to be limited to hematopoietic cells, such as macrophages, dendritic cells, monocytes, lymphocytes, and red blood cells as well as osteoclasts, and eosinophils. However, it is now clear that P2X7 exists in cells from other lineages, including osteoblasts, fibroblasts, endothelial cells and epithelial cells. In addition, P2X7 is also present in cells of the central and peripheral nervous systems, including microglia, astrocytes, oligodendrocytes and Schwann cells. In microglia, P2X7 receptors are found mostly on the cell surface.

Diseases associated with P2RX7:

Activation of the P2X7 receptor by ATP leads to recruitment of pannexin pores which allow small molecules such as ATP to leak out of cells. This allows for further activation of purinergic receptors and physiological responses such as spreading cytoplasmic waves of calcium. Furthermore, this could be responsible for ATP-dependent lysis of macrophages by forming membrane pores that are permeable to larger molecules. Microglial P2X7 receptors are thought to be involved in neuropathic pain because blockade or deletion of P2X7 receptors results in decreased responses to pain, as demonstrated in vivo. In addition, P2X7 receptor signaling increases the release of pro-inflammatory molecules such as IL-1β, IL-6, and TNF-α.

References:

Rassendren F, Buell GN, Virginio C, Collo G, North RA, Surprenant A (1997). "The permeabilizing ATP receptor, P2X7. Cloning and expression of a human cDNA." Journal of Biological Chemistry. 272 (9): 5482-6.
Buell GN, Talabot F, Gos A, Lorenz J, Lai E, Morris MA, Antonarakis SE (1999). "Gene structure and chromosomal localization of the human P2X7 receptor." Receptors Channels. 5 (6): 347-54.
Torres GE, Egan TM, Voigt MM (1999). "Hetero-oligomeric assembly of P2X receptor subunits. Specificities exist with regard to possible partners." Journal of Biological Chemistry. 274 (10): 6653-9.
Jindrichova M, Kuzyk P, Li S, Stojilkovic SS, Zemkova H (2012). "Conserved ectodomain cysteines are essential for rat P2X7 receptor trafficking." Purinergic Signalling. 8 (2): 317-25.
Kobayashi K, Takahashi E, Miyagawa Y, Yamanaka H, Noguchi K (2011). "Induction of the P2X7 receptor in spinal microglia in a neuropathic pain model." Neuroscience Letters. 504 (1): 57-61.
Boison D, Chen JF, Fredholm BB (2010). "Adenosine signaling and function in glial cells." Cell Death & Differentiation. 17 (7): 1071-82.
Chessell IP, Hatcher JP, Bountra C, Michel AD, Hughes JP, Green P, Egerton J, Murfin M, Richardson J, Peck WL, Grahames CB, Casula MA, Yiangou Y, Birch R, Anand P, Buell GN (2005). "Disruption of the P2X7 purinoceptor gene abolishes chronic inflammatory and neuropathic pain." Pain. 114 (3): 386-96.
Deuchars J (2001). "Neuronal P2X7 receptors are targeted to presynaptic terminals in the central and peripheral nervous systems." Journal of Neuroscience. 21 (18): 7143-52.

Quick Inquiry

Interested in learning more?

Contact us today for a free consultation with the scientific team and discover how Creative Biogene can be a valuable resource and partner for your organization.

Request a quote today!

Inquiry