Bombesin-like receptor 3: Difference between revisions
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{{ | The '''bombesin receptor subtype 3''' also known as '''BRS-3''' or '''BB<sub>3</sub>'''<ref name="IUPHAR-DB">{{cite web | url = http://www.iuphar-db.org/GPCR/ReceptorDisplayForward?receptorID=2958 | title = Bombesin Receptors: BB<sub>3</sub> | accessdate = | date = | format = | work = IUPHAR Database of Receptors and Ion Channels | publisher = International Union of Basic and Clinical Pharmacology | pages = | language = | archiveurl = | archivedate = | quote = }}</ref> is a [[protein]] which in humans is encoded by the ''BRS3'' [[gene]].<ref name="pmid8383682">{{cite journal | vauthors = Fathi Z, Corjay MH, Shapira H, Wada E, Benya R, Jensen R, Viallet J, Sausville EA, Battey JF | title = BRS-3: a novel bombesin receptor subtype selectively expressed in testis and lung carcinoma cells | journal = J. Biol. Chem. | volume = 268 | issue = 8 | pages = 5979–84 |date=March 1993 | pmid = 8383682 | doi = | url = http://www.jbc.org/cgi/pmidlookup?view=long&pmid=8383682 | issn = }}</ref><ref name="pmid9262170">{{cite journal | vauthors = Ohki-Hamazaki H, Wada E, Matsui K, Wada K | title = Cloning and expression of the neuromedin B receptor and the third subtype of bombesin receptor genes in the mouse | journal = Brain Res. | volume = 762 | issue = 1-2 | pages = 165–72 |date=July 1997 | pmid = 9262170 | doi = 10.1016/S0006-8993(97)00380-6| url = }}</ref> | ||
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== Function == | |||
Mammalian [[bombesin]]-like peptides are widely distributed in the [[central nervous system]] as well as in the [[gastrointestinal tract]], where they modulate smooth-muscle contraction, exocrine and endocrine processes, metabolism, and behavior. They bind to G protein-coupled receptors on the cell surface to elicit their effects. Bombesin-like peptide receptors include [[gastrin-releasing peptide receptor]], [[neuromedin B receptor]], and bombesin-like receptor-3 (BRS3; this article).<ref name="pmid9262170"/><ref name="entrez">{{cite web | title = Entrez Gene: BRS3 bombesin-like receptor 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=680| accessdate = }}</ref> | |||
< | BB<sub>3</sub> is a [[G protein-coupled receptor]].<ref name="pmid8383682" /> BB<sub>3</sub> only interacts with known naturally occurring bombesin-related peptides with low affinity and therefore, as it has no natural high-affinity ligand, is classified as an [[orphan receptor]].<ref name="pmid8383682" /><ref name="pmid9325344">{{cite journal | vauthors = Mantey SA, Weber HC, Sainz E, Akeson M, Ryan RR, Pradhan TK, Searles RP, Spindel ER, Battey JF, Coy DH, Jensen RT | last-author-amp = yes | title = Discovery of a high affinity radioligand for the human orphan receptor, bombesin receptor subtype 3, which demonstrates that it has a uniquepharmacology compared with other mammalian bombesin receptors. | journal = J. Biol. Chem. | volume = 272 | issue = 41| pages = 26062–26071 | year = 1997 | pmid = 9325344 | doi = 10.1074/jbc.272.41.26062| url = }}</ref><ref name="pmid18055507">{{cite journal | vauthors = Jensen RT, Battey JF, Spindel ER, Benya RV | last-author-amp = yes | title = International Union of Pharmacology: The Bombesin Receptors. Nomenclature, distribution, pharmacology, signaling and functions in normal and diseased states. | journal = Pharmacol. Rev. | volume = 60 | issue = 1| pages = 1–42 | year = 2007 | pmid = 18055507 | doi = 10.1124/pr.107.07108| url = | pmc = 2517428 }}</ref> | ||
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==References== | ==References== | ||
{{reflist| | {{reflist|30em}} | ||
==Further reading== | ==Further reading== | ||
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*{{cite journal | | *{{cite journal | vauthors=Gorbulev V, Akhundova A, Grzeschik KH, Fahrenholz F |title=Organization and chromosomal localization of the gene for the human bombesin receptor subtype expressed in pregnant uterus. |journal=FEBS Lett. |volume=340 |issue= 3 |pages= 260–4 |year= 1994 |pmid= 8131855 |doi=10.1016/0014-5793(94)80150-9 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Fathi Z, Corjay MH, Shapira H |title=BRS-3: a novel bombesin receptor subtype selectively expressed in testis and lung carcinoma cells. |journal=J. Biol. Chem. |volume=268 |issue= 8 |pages= 5979–84 |year= 1993 |pmid= 8383682 |doi= |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Kane MA, Toi-Scott M, Johnson GL |title=Bombesin-like peptide receptors in human bronchial epithelial cells. |journal=Peptides |volume=17 |issue= 1 |pages= 111–8 |year= 1996 |pmid= 8822519 |doi=10.1016/0196-9781(95)02088-8 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Ohki-Hamazaki H, Watase K, Yamamoto K |title=Mice lacking bombesin receptor subtype-3 develop metabolic defects and obesity. |journal=Nature |volume=390 |issue= 6656 |pages= 165–9 |year= 1997 |pmid= 9367152 |doi= 10.1038/36568 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Ryan RR, Weber HC, Hou W |title=Ability of various bombesin receptor agonists and antagonists to alter intracellular signaling of the human orphan receptor BRS-3. |journal=J. Biol. Chem. |volume=273 |issue= 22 |pages= 13613–24 |year= 1998 |pmid= 9593699 |doi=10.1074/jbc.273.22.13613 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Liu J, Lao ZJ, Zhang J |title=Molecular basis of the pharmacological difference between rat and human bombesin receptor subtype-3 (BRS-3). |journal=Biochemistry |volume=41 |issue= 28 |pages= 8954–60 |year= 2002 |pmid= 12102638 |doi=10.1021/bi0202777 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Ross MT, Grafham DV, Coffey AJ |title=The DNA sequence of the human X chromosome. |journal=Nature |volume=434 |issue= 7031 |pages= 325–37 |year= 2005 |pmid= 15772651 |doi= 10.1038/nature03440 | pmc=2665286 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Hou X, Wei L, Harada A, Tatamoto K |title=Activation of bombesin receptor subtype-3 stimulates adhesion of lung cancer cells. |journal=Lung Cancer |volume=54 |issue= 2 |pages= 143–8 |year= 2007 |pmid= 16979789 |doi= 10.1016/j.lungcan.2006.08.005 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Tan YR, Qin XQ, Xiang Y |title=PPARalpha and AP-2alpha regulate bombesin receptor subtype 3 expression in ozone-stressed bronchial epithelial cells. |journal=Biochem. J. |volume=405 |issue= 1 |pages= 131–7 |year= 2007 |pmid= 17355223 |doi= 10.1042/BJ20061754 | pmc=1925247 |display-authors=etal}} | ||
}} | }} | ||
{{refend}} | {{refend}} | ||
==External links== | ==External links== | ||
* | * {{cite web | url = http://www.iuphar-db.org/GPCR/ReceptorDisplayForward?receptorID=2958 | title = Bombesin Receptors: BB<sub>3</sub> | accessdate = | date = | format = | work = IUPHAR Database of Receptors and Ion Channels | publisher = International Union of Basic and Clinical Pharmacology | pages = | language = | archiveurl = | archivedate = | quote = }} | ||
* {{MeshName|bombesin+receptor+subtype+3}} | * {{MeshName|bombesin+receptor+subtype+3}} | ||
* {{UCSC gene info|BRS3}} | |||
{{NLM content}} | |||
{{G protein-coupled receptors}} | {{G protein-coupled receptors}} | ||
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[[Category:G protein coupled receptors]] | [[Category:G protein coupled receptors]] | ||
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The bombesin receptor subtype 3 also known as BRS-3 or BB3[1] is a protein which in humans is encoded by the BRS3 gene.[2][3]
Function
Mammalian bombesin-like peptides are widely distributed in the central nervous system as well as in the gastrointestinal tract, where they modulate smooth-muscle contraction, exocrine and endocrine processes, metabolism, and behavior. They bind to G protein-coupled receptors on the cell surface to elicit their effects. Bombesin-like peptide receptors include gastrin-releasing peptide receptor, neuromedin B receptor, and bombesin-like receptor-3 (BRS3; this article).[3][4]
BB3 is a G protein-coupled receptor.[2] BB3 only interacts with known naturally occurring bombesin-related peptides with low affinity and therefore, as it has no natural high-affinity ligand, is classified as an orphan receptor.[2][5][6]
References
- ↑ "Bombesin Receptors: BB3". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology.
- ↑ 2.0 2.1 2.2 Fathi Z, Corjay MH, Shapira H, Wada E, Benya R, Jensen R, Viallet J, Sausville EA, Battey JF (March 1993). "BRS-3: a novel bombesin receptor subtype selectively expressed in testis and lung carcinoma cells". J. Biol. Chem. 268 (8): 5979–84. PMID 8383682.
- ↑ 3.0 3.1 Ohki-Hamazaki H, Wada E, Matsui K, Wada K (July 1997). "Cloning and expression of the neuromedin B receptor and the third subtype of bombesin receptor genes in the mouse". Brain Res. 762 (1–2): 165–72. doi:10.1016/S0006-8993(97)00380-6. PMID 9262170.
- ↑ "Entrez Gene: BRS3 bombesin-like receptor 3".
- ↑ Mantey SA, Weber HC, Sainz E, Akeson M, Ryan RR, Pradhan TK, Searles RP, Spindel ER, Battey JF, Coy DH & Jensen RT (1997). "Discovery of a high affinity radioligand for the human orphan receptor, bombesin receptor subtype 3, which demonstrates that it has a uniquepharmacology compared with other mammalian bombesin receptors". J. Biol. Chem. 272 (41): 26062–26071. doi:10.1074/jbc.272.41.26062. PMID 9325344.
- ↑ Jensen RT, Battey JF, Spindel ER & Benya RV (2007). "International Union of Pharmacology: The Bombesin Receptors. Nomenclature, distribution, pharmacology, signaling and functions in normal and diseased states". Pharmacol. Rev. 60 (1): 1–42. doi:10.1124/pr.107.07108. PMC 2517428. PMID 18055507.
Further reading
- Gorbulev V, Akhundova A, Grzeschik KH, Fahrenholz F (1994). "Organization and chromosomal localization of the gene for the human bombesin receptor subtype expressed in pregnant uterus". FEBS Lett. 340 (3): 260–4. doi:10.1016/0014-5793(94)80150-9. PMID 8131855.
- Fathi Z, Corjay MH, Shapira H, et al. (1993). "BRS-3: a novel bombesin receptor subtype selectively expressed in testis and lung carcinoma cells". J. Biol. Chem. 268 (8): 5979–84. PMID 8383682.
- Kane MA, Toi-Scott M, Johnson GL, et al. (1996). "Bombesin-like peptide receptors in human bronchial epithelial cells". Peptides. 17 (1): 111–8. doi:10.1016/0196-9781(95)02088-8. PMID 8822519.
- Ohki-Hamazaki H, Watase K, Yamamoto K, et al. (1997). "Mice lacking bombesin receptor subtype-3 develop metabolic defects and obesity". Nature. 390 (6656): 165–9. doi:10.1038/36568. PMID 9367152.
- Ryan RR, Weber HC, Hou W, et al. (1998). "Ability of various bombesin receptor agonists and antagonists to alter intracellular signaling of the human orphan receptor BRS-3". J. Biol. Chem. 273 (22): 13613–24. doi:10.1074/jbc.273.22.13613. PMID 9593699.
- Liu J, Lao ZJ, Zhang J, et al. (2002). "Molecular basis of the pharmacological difference between rat and human bombesin receptor subtype-3 (BRS-3)". Biochemistry. 41 (28): 8954–60. doi:10.1021/bi0202777. PMID 12102638.
- Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome". Nature. 434 (7031): 325–37. doi:10.1038/nature03440. PMC 2665286. PMID 15772651.
- Hou X, Wei L, Harada A, Tatamoto K (2007). "Activation of bombesin receptor subtype-3 stimulates adhesion of lung cancer cells". Lung Cancer. 54 (2): 143–8. doi:10.1016/j.lungcan.2006.08.005. PMID 16979789.
- Tan YR, Qin XQ, Xiang Y, et al. (2007). "PPARalpha and AP-2alpha regulate bombesin receptor subtype 3 expression in ozone-stressed bronchial epithelial cells". Biochem. J. 405 (1): 131–7. doi:10.1042/BJ20061754. PMC 1925247. PMID 17355223.
External links
- "Bombesin Receptors: BB3". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology.
- bombesin+receptor+subtype+3 at the US National Library of Medicine Medical Subject Headings (MeSH)
- Human BRS3 genome location and BRS3 gene details page in the UCSC Genome Browser.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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