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Official Full Name
purinergic receptor P2X, ligand-gated ion channel, 5
The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the neighboring downstream gene, TAX1BP3 (Tax1 binding protein 3).
P2RX5; purinergic receptor P2X, ligand-gated ion channel, 5; P2X purinoceptor 5; P2X5; ATP receptor; ATP receptor subunit; ionotropic ATP receptor P2X5; MGC47755; P2X5R; Purinergic receptor; Purinergic receptor P2X ligand gated ion channel 5; OTTHUMP00000115870; OTTHUMP00000241718; OTTHUMP00000241719; OTTHUMP00000241720; OTTHUMP00000241722; OTTHUMP00000241723; lymphoid-restricted histocompatibility antigen-1; LRH-1; ATP-gated ion channel receptor P2X8; P2X5.1


P2X purine receptor 5 is a protein encoded by the P2RX5 gene. The P2RX5 gene has identified four transcriptional variants that encode different subtypes. P2RX5 has several characteristic motifs in its main structure, but unlike other members of the purine receptor family, P2RX5 has only one transmembrane domain, and P2RX5 is highly expressed in adult rat heart and is less expressed in the central nervous system.

Figure 1. The 3D stracture of P2RX5.

The discovery of the P2RX5:

P2RX5 cDNA was first isolated from the cDNA library constructed from rat abdominal ganglion and heart. P2X receptors are also cloned from chicken embryo skeletal muscles. The only human cDNA reported were deletion of exons 10 (hP2RX5a) or exons 3 and 10 (hP2RX5b). Scientists have identified seven subtypes (P2RX1-P2RX7) that can be combined into homo- and isotrimer molecules. One feature of the current generated PaRX5is its small amplitude, and P2RX5 mRNA is highly expressed during skeletal muscle development compared to the expression of P2X1, P2X2, P2X3, or P2RX4 receptors under similar conditions.

Latest research:

The genotyping of human DNA samples reveals the advantage of the g-bearing allele, which exists only in DNA samples from white Americans, Middle Easterners and Chinese. Samples from African-American donors are polymorphic and the G allele is more frequent. Reverse transcription polymerase chain reaction analysis of lymphocytes revealed a 100% positive correlation between genotype and P2RX5 transcript. Immunoblotting of P2RX1/P2RX5 stably co-expressed cell lines showed full length P2RX5 expression on the cell surface, and exon 10 deletion in the cytoplasm. Pharmacological features based on fluorescence imaging showed increased ligand-dependence of calcium in 1321N1 astrocytoma cells and transient expression of full-length P2RX5, but there was no exon 10 deletion. Similarly, electrophysiological analyses showed that ATP-induced current was stronger when full-length P2RX5 subtypes were expressed without exon 10 deletion. Taken together, our findings suggest that most humans express only one non-functional subtype of P2RX5, a stark contrast to other subtypes of vertebrates that have studied.

In addition, more and more people think that purine receptor signal transduction is an important regulator of inflammation. It is believed that P2RX5 may be an important regulator of inflammatory bone loss. However, the role of P2X5 in periodontitis remains unclear. In a study evaluating P2RX5's role in ligation-induced periodontitis in mice, analysis of alveolar bone after 5 days of ligation showed reduced bone loss in compared with P2RX5-/- and WT control mice. Gene expression analysis of gingival tissue of ligated mice showed that compared with WT mice, the expression levels of P2RX5-/- IL1b, IL6, IL17a and Tnfsf11 were significantly reduced. These results suggest that P2RX5 receptor may regulate bone loss associated with periodontitis and therefore may be a new therapeutic target for this oral disease.


  1. Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U. S. A. 99 (26): 16899–903.
  2. Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9.
  3. North RA (2002). "Molecular physiology of P2X receptors". Physiol. Rev. 82 (4): 1013–67.
  4. Kim, Hyunsoo; Kajikawa, Tetsuhiro; Walsh, Matthew C; Takegahara, Noriko; Jeong, Yun Hee; Hajishengallis, George; Choi, Yongwon ( Aug 2018) “The purinergic receptor P2X5 contributes to bone loss in experimental periodontitis”. News.

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