P2RX3: Difference between revisions

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Latest revision as of 03:26, 27 October 2018

P2X purinoceptor 3 is a protein that in humans is encoded by the P2RX3 gene.^[1]^[2]

The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel and may transduce ATP-evoked nociceptor activation. Mouse studies suggest that this receptor is important for peripheral pain responses, and also participates in pathways controlling urinary bladder volume reflexes, platelet aggregation, macrophage activation, apoptosis and neuronal–glial interactions. It is possible that the development of selective antagonists for this receptor may have a therapeutic potential in pain relief and in the treatment of disorders of urine storage.^[2]

References

↑ Garcia-Guzman M, Stuhmer W, Soto F (Sep 1997). "Molecular characterization and pharmacological properties of the human P2X3 purinoceptor". Brain Res Mol Brain Res. 47 (1–2): 59–66. doi:10.1016/S0169-328X(97)00036-3. PMID 9221902.
↑ ^2.0 ^2.1 "Entrez Gene: P2RX3 purinergic receptor P2X, ligand-gated ion channel, 3".

North RA (2002). "Molecular physiology of P2X receptors". Physiol. Rev. 82 (4): 1013–67. doi:10.1152/physrev.00015.2002. PMID 12270951.
Jarvis MF (2005). "Contributions of P2X3 homomeric and heteromeric channels to acute and chronic pain". Expert Opin. Ther. Targets. 7 (4): 513–22. doi:10.1517/14728222.7.4.513. PMID 12885270.
Kennedy C, Leff P (1995). "Painful connection for ATP". Nature. 377 (6548): 385–6. doi:10.1038/377385a0. PMID 7566110.
Lewis C, Neidhart S, Holy C, et al. (1995). "Coexpression of P2X2 and P2X3 receptor subunits can account for ATP-gated currents in sensory neurons". Nature. 377 (6548): 432–5. doi:10.1038/377432a0. PMID 7566120.
Garcia-Guzman M, Soto F, Gomez-Hernandez JM, et al. (1997). "Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue". Mol. Pharmacol. 51 (1): 109–18. PMID 9016352.
Cook SP, McCleskey EW (2000). "ATP, pain and a full bladder". Nature. 407 (6807): 951–2. doi:10.1038/35039648. PMID 11069162.
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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Renton T, Yiangou Y, Baecker PA, et al. (2003). "Capsaicin receptor VR1 and ATP purinoceptor P2X3 in painful and nonpainful human tooth pulp". Journal of Orofacial Pain. 17 (3): 245–50. PMID 14520770.
Mason HS, Bourke S, Kemp PJ (2005). "Selective modulation of ligand-gated P2X purinoceptor channels by acute hypoxia is mediated by reactive oxygen species". Mol. Pharmacol. 66 (6): 1525–35. doi:10.1124/mol.104.000851. PMID 15331767.
Fabbretti E, Sokolova E, Masten L, et al. (2005). "Identification of negative residues in the P2X3 ATP receptor ectodomain as structural determinants for desensitization and the Ca2+-sensing modulatory sites". J. Biol. Chem. 279 (51): 53109–15. doi:10.1074/jbc.M409772200. PMID 15475563.
Brown DA, Yule DI (2007). "Protein kinase C regulation of P2X3 receptors is unlikely to involve direct receptor phosphorylation". Biochim. Biophys. Acta. 1773 (2): 166–75. doi:10.1016/j.bbamcr.2006.09.020. PMC 1861828. PMID 17052768.

External links

P2RX3+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

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[pmid9221902-1] Garcia-Guzman M, Stuhmer W, Soto F (Sep 1997). "Molecular characterization and pharmacological properties of the human P2X3 purinoceptor". Brain Res Mol Brain Res. 47 (1–2): 59–66. doi:10.1016/S0169-328X(97)00036-3. PMID 9221902.

[entrez-2] 2.0 ^2.1 "Entrez Gene: P2RX3 purinergic receptor P2X, ligand-gated ion channel, 3".

[1]

[2]

@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox_gene}}
-{{PBB_Controls
+'''P2X purinoceptor 3''' is a [[protein]] that in humans is encoded by the ''P2RX3'' [[gene]].<ref name="pmid9221902">{{cite journal |vauthors=Garcia-Guzman M, Stuhmer W, Soto F | title = Molecular characterization and pharmacological properties of the human P2X3 purinoceptor | journal = Brain Res Mol Brain Res | volume = 47 | issue = 1–2 | pages = 59–66 |date=Sep 1997 | pmid = 9221902 | pmc =  | doi =10.1016/S0169-328X(97)00036-3  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: P2RX3 purinergic receptor P2X, ligand-gated ion channel, 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5024| accessdate = }}</ref>
-| update_page = yes
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-}}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{GNF_Protein_box
- | image =
- | image_source =
- | PDB =
- | Name = Purinergic receptor P2X, ligand-gated ion channel, 3
- | HGNCid = 8534
- | Symbol = P2RX3
- | AltSymbols =; MGC129956; P2X3
- | OMIM = 600843
- | ECnumber =
- | Homologene = 1922
- | MGIid = 1097160
- | Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004931 |text = ATP-gated cation channel activity}} {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}}
-  | Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
- | Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 5024
-    | Hs_Ensembl =
-    | Hs_RefseqProtein = XP_001126192
-    | Hs_RefseqmRNA = XM_001126192
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr =
-    | Hs_GenLoc_start =
-    | Hs_GenLoc_end =
-    | Hs_Uniprot =
-    | Mm_EntrezGene = 228139
-    | Mm_Ensembl = ENSMUSG00000027071
-    | Mm_RefseqmRNA = NM_145526
-    | Mm_RefseqProtein = NP_663501
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 2
-    | Mm_GenLoc_start = 84797391
-    | Mm_GenLoc_end = 84836673
-    | Mm_Uniprot = Q3UR32
-  }}
-}}
-{{CMG}}
-'''Purinergic receptor P2X, ligand-gated ion channel, 3''', also known as '''P2RX3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: P2RX3 purinergic receptor P2X, ligand-gated ion channel, 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5024| accessdate = }}</ref>
 <!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
 {{PBB_Summary
 | section_title =
-| summary_text = The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel and may transduce ATP-evoked nociceptor activation. Mouse studies suggest that this receptor is important for peripheral pain responses, and also participates in pathways controlling urinary bladder volume reflexes. It is possible that the development of selective antagonists for this receptor may have a therapeutic potential in pain relief and in the treatment of disorders of urine storage.<ref name="entrez">{{cite web | title = Entrez Gene: P2RX3 purinergic receptor P2X, ligand-gated ion channel, 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5024| accessdate = }}</ref>
+| summary_text = The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel and may transduce ATP-evoked nociceptor activation. Mouse studies suggest that this receptor is important for peripheral pain responses, and also participates in pathways controlling urinary bladder volume reflexes, platelet aggregation, macrophage activation, apoptosis and neuronal–glial interactions. It is possible that the development of selective antagonists for this receptor may have a therapeutic potential in pain relief and in the treatment of disorders of urine storage.<ref name="entrez" />
 }}
 ==See also==
+* [[P2X purinoreceptor]]
 * [[Purinergic receptor]]
+* [[Ligand-gated ion channel]]
+* [[Nociceptor]]
 ==References==
-{{reflist|2}}
+{{reflist}}
 ==Further reading==
@@ Line 68: / Line 21: @@
 {{PBB_Further_reading
 | citations =
-*{{cite journal  | author=North RA |title=Molecular physiology of P2X receptors. |journal=Physiol. Rev. |volume=82 |issue= 4 |pages= 1013-67 |year= 2002 |pmid= 12270951 |doi= 10.1152/physrev.00015.2002 }}
+*{{cite journal  | author=North RA |title=Molecular physiology of P2X receptors |journal=Physiol. Rev. |volume=82 |issue= 4 |pages= 1013–67 |year= 2002 |pmid= 12270951 |doi= 10.1152/physrev.00015.2002 }}
-*{{cite journal  | author=Jarvis MF |title=Contributions of P2X3 homomeric and heteromeric channels to acute and chronic pain. |journal=Expert Opin. Ther. Targets |volume=7 |issue= 4 |pages= 513-22 |year= 2005 |pmid= 12885270 |doi= 10.1517/14728222.7.4.513 }}
+*{{cite journal  | author=Jarvis MF |title=Contributions of P2X3 homomeric and heteromeric channels to acute and chronic pain |journal=Expert Opin. Ther. Targets |volume=7 |issue= 4 |pages= 513–22 |year= 2005 |pmid= 12885270 |doi= 10.1517/14728222.7.4.513 }}
-*{{cite journal  | author=Kennedy C, Leff P |title=Painful connection for ATP. |journal=Nature |volume=377 |issue= 6548 |pages= 385-6 |year= 1995 |pmid= 7566110 |doi= 10.1038/377385a0 }}
+*{{cite journal  |vauthors=Kennedy C, Leff P |title=Painful connection for ATP |journal=Nature |volume=377 |issue= 6548 |pages= 385–6 |year= 1995 |pmid= 7566110 |doi= 10.1038/377385a0 }}
-*{{cite journal  | author=Lewis C, Neidhart S, Holy C, ''et al.'' |title=Coexpression of P2X2 and P2X3 receptor subunits can account for ATP-gated currents in sensory neurons. |journal=Nature |volume=377 |issue= 6548 |pages= 432-5 |year= 1995 |pmid= 7566120 |doi= 10.1038/377432a0 }}
+*{{cite journal  | author=Lewis C |title=Coexpression of P2X2 and P2X3 receptor subunits can account for ATP-gated currents in sensory neurons |journal=Nature |volume=377 |issue= 6548 |pages= 432–5 |year= 1995 |pmid= 7566120 |doi= 10.1038/377432a0  |name-list-format=vanc| author2=Neidhart S  | author3=Holy C  | display-authors=3  | last4=North  | first4=R. A.  | last5=Buell  | first5=G.  | last6=Surprenant  | first6=A. }}
-*{{cite journal  | author=Garcia-Guzman M, Soto F, Gomez-Hernandez JM, ''et al.'' |title=Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue. |journal=Mol. Pharmacol. |volume=51 |issue= 1 |pages= 109-18 |year= 1997 |pmid= 9016352 |doi=  }}
+*{{cite journal  | author=Garcia-Guzman M |title=Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue |journal=Mol. Pharmacol. |volume=51 |issue= 1 |pages= 109–18 |year= 1997 |pmid= 9016352 |doi=  |name-list-format=vanc| author2=Soto F  | author3=Gomez-Hernandez JM  | display-authors=3  | last4=Lund  | first4=PE  | last5=Stühmer  | first5=W  }}
-*{{cite journal  | author=Garcia-Guzman M, Stühmer W, Soto F |title=Molecular characterization and pharmacological properties of the human P2X3 purinoceptor. |journal=Brain Res. Mol. Brain Res. |volume=47 |issue= 1-2 |pages= 59-66 |year= 1997 |pmid= 9221902 |doi=  }}
+*{{cite journal  |vauthors=Cook SP, McCleskey EW |title=ATP, pain and a full bladder |journal=Nature |volume=407 |issue= 6807 |pages= 951–2 |year= 2000 |pmid= 11069162 |doi= 10.1038/35039648 }}
-*{{cite journal  | author=Cook SP, McCleskey EW |title=ATP, pain and a full bladder. |journal=Nature |volume=407 |issue= 6807 |pages= 951-2 |year= 2000 |pmid= 11069162 |doi= 10.1038/35039648 }}
+*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
-*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
+*{{cite journal  | author=Renton T |title=Capsaicin receptor VR1 and ATP purinoceptor P2X3 in painful and nonpainful human tooth pulp |journal=Journal of Orofacial Pain |volume=17 |issue= 3 |pages= 245–50 |year= 2003 |pmid= 14520770 |doi=  |name-list-format=vanc| author2=Yiangou Y  | author3=Baecker PA  | display-authors=3  | last4=Ford  | first4=AP  | last5=Anand  | first5=P  }}
-*{{cite journal  | author=Renton T, Yiangou Y, Baecker PA, ''et al.'' |title=Capsaicin receptor VR1 and ATP purinoceptor P2X3 in painful and nonpainful human tooth pulp. |journal=Journal of orofacial pain |volume=17 |issue= 3 |pages= 245-50 |year= 2003 |pmid= 14520770 |doi=  }}
+*{{cite journal  |vauthors=Mason HS, Bourke S, Kemp PJ |title=Selective modulation of ligand-gated P2X purinoceptor channels by acute hypoxia is mediated by reactive oxygen species |journal=Mol. Pharmacol. |volume=66 |issue= 6 |pages= 1525–35 |year= 2005 |pmid= 15331767 |doi= 10.1124/mol.104.000851 }}
-*{{cite journal  | author=Mason HS, Bourke S, Kemp PJ |title=Selective modulation of ligand-gated P2X purinoceptor channels by acute hypoxia is mediated by reactive oxygen species. |journal=Mol. Pharmacol. |volume=66 |issue= 6 |pages= 1525-35 |year= 2005 |pmid= 15331767 |doi= 10.1124/mol.104.000851 }}
+*{{cite journal  | author=Fabbretti E |title=Identification of negative residues in the P2X3 ATP receptor ectodomain as structural determinants for desensitization and the Ca2+-sensing modulatory sites |journal=J. Biol. Chem. |volume=279 |issue= 51 |pages= 53109–15 |year= 2005 |pmid= 15475563 |doi= 10.1074/jbc.M409772200  |name-list-format=vanc| author2=Sokolova E  | author3=Masten L  | display-authors=3  | last4=d'Arco  | first4=M.  | last5=Fabbro  | first5=A.  | last6=Nistri  | first6=A.  | last7=Giniatullin  | first7=R. }}
-*{{cite journal  | author=Fabbretti E, Sokolova E, Masten L, ''et al.'' |title=Identification of negative residues in the P2X3 ATP receptor ectodomain as structural determinants for desensitization and the Ca2+-sensing modulatory sites. |journal=J. Biol. Chem. |volume=279 |issue= 51 |pages= 53109-15 |year= 2005 |pmid= 15475563 |doi= 10.1074/jbc.M409772200 }}
+*{{cite journal  |vauthors=Brown DA, Yule DI |title=Protein kinase C regulation of P2X3 receptors is unlikely to involve direct receptor phosphorylation |journal=Biochim. Biophys. Acta |volume=1773 |issue= 2 |pages= 166–75 |year= 2007 |pmid= 17052768 |doi= 10.1016/j.bbamcr.2006.09.020  | pmc=1861828 }}
-*{{cite journal  | author=Brown DA, Yule DI |title=Protein kinase C regulation of P2X3 receptors is unlikely to involve direct receptor phosphorylation. |journal=Biochim. Biophys. Acta |volume=1773 |issue= 2 |pages= 166-75 |year= 2007 |pmid= 17052768 |doi= 10.1016/j.bbamcr.2006.09.020 }}
 }}
 {{refend}}
@@ Line 88: / Line 40: @@
 {{NLM content}}
 {{Ligand-gated ion channels}}
+{{Purinergics}}
+<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{PBB_Controls
+| update_page = yes
+| require_manual_inspection = no
+| update_protein_box = yes
+| update_summary = yes
+| update_citations = yes
+}}
 [[Category:Ion channels]]
-{{WH}}
-{{WS}}
+{{membrane-protein-stub}}

P2RX3: Difference between revisions

Latest revision as of 03:26, 27 October 2018

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See also

References

Further reading

External links

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