P2RX1: Difference between revisions
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}})) |
m (Bot: HTTP→HTTPS) |
||
Line 1: | Line 1: | ||
{{Infobox_gene}} | |||
{{ | '''P2X purinoceptor 1''' is a [[protein]] that in humans is encoded by the ''P2RX1'' [[gene]].<ref name="pmid8834001">{{cite journal | vauthors = Valera S, Talabot F, Evans RJ, Gos A, Antonarakis SE, Morris MA, Buell GN | title = Characterization and chromosomal localization of a human P2X receptor from the urinary bladder | journal = Receptors Channels | volume = 3 | issue = 4 | pages = 283–9 |date=Nov 1996 | pmid = 8834001 | pmc = | doi = }}</ref> | ||
}} | |||
{{ | |||
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. --> | <!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. --> | ||
{{PBB_Summary | {{PBB_Summary | ||
| section_title = | | 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 with relatively high calcium permeability. Expressed in smooth muscle and platelets. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle, being responsible, for example, for sympathetic vasoconstriction in small arteries, arterioles and vas deferens. Mouse studies suggest that this receptor is essential for normal male reproductive function. It is possible that the development of selective antagonists for this receptor may provide an effective non-hormonal male contraceptive pill.<ref name="entrez">{{cite web | title = Entrez Gene: P2RX1 purinergic receptor P2X, ligand-gated ion channel, 1| url = | | summary_text = The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel with relatively high calcium permeability. Expressed in smooth muscle and platelets. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle, being responsible, for example, for sympathetic vasoconstriction in small arteries, arterioles and vas deferens. Mouse studies suggest that this receptor is essential for normal male reproductive function. It is possible that the development of selective antagonists for this receptor may provide an effective non-hormonal male contraceptive pill.<ref name="entrez">{{cite web | title = Entrez Gene: P2RX1 purinergic receptor P2X, ligand-gated ion channel, 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5023| accessdate = }}</ref> | ||
}} | }} | ||
Line 63: | Line 12: | ||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
Line 69: | Line 18: | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | author=North RA |title=Molecular physiology of P2X receptors. |journal=Physiol. Rev. |volume=82 |issue= 4 |pages= | *{{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 | | *{{cite journal | vauthors=Longhurst PA, Schwegel T, Folander K, Swanson R |title=The human P2x1 receptor: molecular cloning, tissue distribution, and localization to chromosome 17. |journal=Biochim. Biophys. Acta |volume=1308 |issue= 3 |pages= 185–8 |year= 1996 |pmid= 8809107 |doi= 10.1016/0167-4781(96)00112-1}} | ||
*{{cite journal |vauthors=Clifford EE, Parker K, Humphreys BD, etal |title=The P2X1 receptor, an adenosine triphosphate-gated cation channel, is expressed in human platelets but not in human blood leukocytes. |journal=Blood |volume=91 |issue= 9 |pages= 3172–81 |year= 1998 |pmid= 9558372 |doi= }} | |||
*{{cite journal | *{{cite journal | vauthors=Sun B, Li J, Okahara K, Kambayashi J |title=P2X1 purinoceptor in human platelets. Molecular cloning and functional characterization after heterologous expression. |journal=J. Biol. Chem. |volume=273 |issue= 19 |pages= 11544–7 |year= 1998 |pmid= 9565569 |doi=10.1074/jbc.273.19.11544 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Mulryan K, Gitterman DP, Lewis CJ, etal |title=Reduced vas deferens contraction and male infertility in mice lacking P2X1 receptors. |journal=Nature |volume=403 |issue= 6765 |pages= 86–9 |year= 2000 |pmid= 10638758 |doi= 10.1038/47495 }} | ||
*{{cite journal | *{{cite journal |vauthors=Oury C, Toth-Zsamboki E, Van Geet C, etal |title=A natural dominant negative P2X1 receptor due to deletion of a single amino acid residue. |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 22611–4 |year= 2000 |pmid= 10816552 |doi= 10.1074/jbc.C000305200 }} | ||
*{{cite journal | *{{cite journal | vauthors=Dhulipala PD, Lianos EA, Kotlikoff MI |title=Regulation of human P2X1 promoter activity by beta helix-loop-helix factors in smooth muscle cells. |journal=Gene |volume=269 |issue= 1–2 |pages= 167–75 |year= 2001 |pmid= 11376948 |doi=10.1016/S0378-1119(01)00442-5 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Ennion SJ, Evans RJ |title=Conserved cysteine residues in the extracellular loop of the human P2X(1) receptor form disulfide bonds and are involved in receptor trafficking to the cell surface |journal=Mol. Pharmacol. |volume=61 |issue= 2 |pages= 303–11 |year= 2002 |pmid= 11809854 |doi=10.1124/mol.61.2.303 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Vial C, Rolf MG, Mahaut-Smith MP, Evans RJ |title=A study of P2X1 receptor function in murine megakaryocytes and human platelets reveals synergy with P2Y receptors |journal=Br. J. Pharmacol. |volume=135 |issue= 2 |pages= 363–72 |year= 2002 |pmid= 11815371 |doi= 10.1038/sj.bjp.0704486 | pmc=1573149 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Oury C, Toth-Zsamboki E, Thys C, etal |title=The ATP-gated P2X1 ion channel acts as a positive regulator of platelet responses to collagen |journal=Thromb. Haemost. |volume=86 |issue= 5 |pages= 1264–71 |year= 2003 |pmid= 11816716 |doi= }} | ||
*{{cite journal | *{{cite journal |vauthors=Toth-Zsamboki E, Oury C, Watanabe H, etal |title=The intracellular tyrosine residues of the ATP-gated P2X(1) ion channel are essential for its function |journal=FEBS Lett. |volume=524 |issue= 1–3 |pages= 15–9 |year= 2002 |pmid= 12135734 |doi=10.1016/S0014-5793(02)02987-3 }} | ||
*{{cite journal | *{{cite journal | vauthors=Oury C, Toth-Zsamboki E, Vermylen J, Hoylaerts MF |title=P2X(1)-mediated activation of extracellular signal-regulated kinase 2 contributes to platelet secretion and aggregation induced by collagen |journal=Blood |volume=100 |issue= 7 |pages= 2499–505 |year= 2002 |pmid= 12239162 |doi= 10.1182/blood-2002-03-0812 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Rolf MG, Mahaut-Smith MP |title=Effects of enhanced P2X1 receptor Ca2+ influx on functional responses in human platelets |journal=Thromb. Haemost. |volume=88 |issue= 3 |pages= 495–502 |year= 2003 |pmid= 12353081 |doi= 10.1267/THRO88030495 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 }} | ||
*{{cite journal | *{{cite journal |vauthors=Valdecantos P, Briones R, Moya P, etal |title=Pharmacological identification of P2X1, P2X4 and P2X7 nucleotide receptors in the smooth muscles of human umbilical cord and chorionic blood vessels |journal=Placenta |volume=24 |issue= 1 |pages= 17–26 |year= 2003 |pmid= 12495655 |doi=10.1053/plac.2002.0862 }} | ||
*{{cite journal | *{{cite journal |vauthors=Oury C, Kuijpers MJ, Toth-Zsamboki E, etal |title=Overexpression of the platelet P2X1 ion channel in transgenic mice generates a novel prothrombotic phenotype |journal=Blood |volume=101 |issue= 10 |pages= 3969–76 |year= 2003 |pmid= 12521992 |doi= 10.1182/blood-2002-10-3215 }} | ||
*{{cite journal | *{{cite journal |vauthors=Wang L, Andersson M, Karlsson L, etal |title=Increased mitogenic and decreased contractile P2 receptors in smooth muscle cells by shear stress in human vessels with intact endothelium |journal=Arterioscler. Thromb. Vasc. Biol. |volume=23 |issue= 8 |pages= 1370–6 |year= 2004 |pmid= 12791671 |doi= 10.1161/01.ATV.0000080350.37408.5A }} | ||
*{{cite journal | *{{cite journal |vauthors=Vial C, Pitt SJ, Roberts J, etal |title=Lack of evidence for functional ADP-activated human P2X1 receptors supports a role for ATP during hemostasis and thrombosis |journal=Blood |volume=102 |issue= 10 |pages= 3646–51 |year= 2004 |pmid= 12907444 |doi= 10.1182/blood-2003-06-1963 }} | ||
*{{cite journal | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
Line 96: | Line 44: | ||
{{NLM content}} | {{NLM content}} | ||
{{Ligand-gated ion channels}} | {{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]] | [[Category:Ion channels]] | ||
{{ | {{membrane-protein-stub}} |
Latest revision as of 17:25, 7 September 2017
VALUE_ERROR (nil) | |||||||
---|---|---|---|---|---|---|---|
Identifiers | |||||||
Aliases | |||||||
External IDs | GeneCards: [1] | ||||||
Orthologs | |||||||
Species | Human | Mouse | |||||
Entrez |
|
| |||||
Ensembl |
|
| |||||
UniProt |
|
| |||||
RefSeq (mRNA) |
|
| |||||
RefSeq (protein) |
|
| |||||
Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
|
P2X purinoceptor 1 is a protein that in humans is encoded by the P2RX1 gene.[1]
The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel with relatively high calcium permeability. Expressed in smooth muscle and platelets. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle, being responsible, for example, for sympathetic vasoconstriction in small arteries, arterioles and vas deferens. Mouse studies suggest that this receptor is essential for normal male reproductive function. It is possible that the development of selective antagonists for this receptor may provide an effective non-hormonal male contraceptive pill.[2]
See also
References
- ↑ Valera S, Talabot F, Evans RJ, Gos A, Antonarakis SE, Morris MA, Buell GN (Nov 1996). "Characterization and chromosomal localization of a human P2X receptor from the urinary bladder". Receptors Channels. 3 (4): 283–9. PMID 8834001.
- ↑ "Entrez Gene: P2RX1 purinergic receptor P2X, ligand-gated ion channel, 1".
Further reading
- North RA (2002). "Molecular physiology of P2X receptors". Physiol. Rev. 82 (4): 1013–67. doi:10.1152/physrev.00015.2002. PMID 12270951.
- Longhurst PA, Schwegel T, Folander K, Swanson R (1996). "The human P2x1 receptor: molecular cloning, tissue distribution, and localization to chromosome 17". Biochim. Biophys. Acta. 1308 (3): 185–8. doi:10.1016/0167-4781(96)00112-1. PMID 8809107.
- Clifford EE, Parker K, Humphreys BD, et al. (1998). "The P2X1 receptor, an adenosine triphosphate-gated cation channel, is expressed in human platelets but not in human blood leukocytes". Blood. 91 (9): 3172–81. PMID 9558372.
- Sun B, Li J, Okahara K, Kambayashi J (1998). "P2X1 purinoceptor in human platelets. Molecular cloning and functional characterization after heterologous expression". J. Biol. Chem. 273 (19): 11544–7. doi:10.1074/jbc.273.19.11544. PMID 9565569.
- Mulryan K, Gitterman DP, Lewis CJ, et al. (2000). "Reduced vas deferens contraction and male infertility in mice lacking P2X1 receptors". Nature. 403 (6765): 86–9. doi:10.1038/47495. PMID 10638758.
- Oury C, Toth-Zsamboki E, Van Geet C, et al. (2000). "A natural dominant negative P2X1 receptor due to deletion of a single amino acid residue". J. Biol. Chem. 275 (30): 22611–4. doi:10.1074/jbc.C000305200. PMID 10816552.
- Dhulipala PD, Lianos EA, Kotlikoff MI (2001). "Regulation of human P2X1 promoter activity by beta helix-loop-helix factors in smooth muscle cells". Gene. 269 (1–2): 167–75. doi:10.1016/S0378-1119(01)00442-5. PMID 11376948.
- Ennion SJ, Evans RJ (2002). "Conserved cysteine residues in the extracellular loop of the human P2X(1) receptor form disulfide bonds and are involved in receptor trafficking to the cell surface". Mol. Pharmacol. 61 (2): 303–11. doi:10.1124/mol.61.2.303. PMID 11809854.
- Vial C, Rolf MG, Mahaut-Smith MP, Evans RJ (2002). "A study of P2X1 receptor function in murine megakaryocytes and human platelets reveals synergy with P2Y receptors". Br. J. Pharmacol. 135 (2): 363–72. doi:10.1038/sj.bjp.0704486. PMC 1573149. PMID 11815371.
- Oury C, Toth-Zsamboki E, Thys C, et al. (2003). "The ATP-gated P2X1 ion channel acts as a positive regulator of platelet responses to collagen". Thromb. Haemost. 86 (5): 1264–71. PMID 11816716.
- Toth-Zsamboki E, Oury C, Watanabe H, et al. (2002). "The intracellular tyrosine residues of the ATP-gated P2X(1) ion channel are essential for its function". FEBS Lett. 524 (1–3): 15–9. doi:10.1016/S0014-5793(02)02987-3. PMID 12135734.
- Oury C, Toth-Zsamboki E, Vermylen J, Hoylaerts MF (2002). "P2X(1)-mediated activation of extracellular signal-regulated kinase 2 contributes to platelet secretion and aggregation induced by collagen". Blood. 100 (7): 2499–505. doi:10.1182/blood-2002-03-0812. PMID 12239162.
- Rolf MG, Mahaut-Smith MP (2003). "Effects of enhanced P2X1 receptor Ca2+ influx on functional responses in human platelets". Thromb. Haemost. 88 (3): 495–502. doi:10.1267/THRO88030495. PMID 12353081.
- 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.
- Valdecantos P, Briones R, Moya P, et al. (2003). "Pharmacological identification of P2X1, P2X4 and P2X7 nucleotide receptors in the smooth muscles of human umbilical cord and chorionic blood vessels". Placenta. 24 (1): 17–26. doi:10.1053/plac.2002.0862. PMID 12495655.
- Oury C, Kuijpers MJ, Toth-Zsamboki E, et al. (2003). "Overexpression of the platelet P2X1 ion channel in transgenic mice generates a novel prothrombotic phenotype". Blood. 101 (10): 3969–76. doi:10.1182/blood-2002-10-3215. PMID 12521992.
- Wang L, Andersson M, Karlsson L, et al. (2004). "Increased mitogenic and decreased contractile P2 receptors in smooth muscle cells by shear stress in human vessels with intact endothelium". Arterioscler. Thromb. Vasc. Biol. 23 (8): 1370–6. doi:10.1161/01.ATV.0000080350.37408.5A. PMID 12791671.
- Vial C, Pitt SJ, Roberts J, et al. (2004). "Lack of evidence for functional ADP-activated human P2X1 receptors supports a role for ATP during hemostasis and thrombosis". Blood. 102 (10): 3646–51. doi:10.1182/blood-2003-06-1963. PMID 12907444.
External links
- P2RX1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
Stub icon | This membrane protein–related article is a stub. You can help Wikipedia by expanding it. |