Bradykinin receptor B2

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External IDs	GeneCards: [1]
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Species	Human	Mouse
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Bradykinin receptor B₂ is a G-protein coupled receptor for bradykinin, encoded by the BDKRB2 gene in humans.

Mechanism

The B₂ receptor is a G protein-coupled receptor, probably coupled to G_q and G_i. G_q stimulates phospholipase C to increase intracellular free calcium and G_i inhibits adenylate cyclase. Furthermore, the receptor stimulates the mitogen-activated protein kinase pathways. It is ubiquitously and constitutively expressed in healthy tissues.

The B₂ receptor forms a complex with angiotensin converting enzyme (ACE), and this is thought to play a role in cross-talk between the renin-angiotensin system (RAS) and the kinin-kallikrein system (KKS). The heptapeptide angiotensin (1-7) also potentiates bradykinin action on B₂ receptors.

Kallidin also signals through the B₂ receptor. An antagonist for the receptor is Hoe 140 (icatibant).

Function

The 9 amino acid bradykinin peptide elicits many responses including vasodilation, edema, smooth muscle spasm and pain fiber stimulation.

Gene

Alternate start codons result in two isoforms of the protein.

See also

• Bradykinin receptor

External links

• "Bradykinin Receptors: B₂". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology.
• Human BDKRB2 genome location and BDKRB2 gene details page in the UCSC Genome Browser.

Further reading

• Duchêne J, Schanstra J, Cellier E, et al. (2002). "[30 years: Happy birthday, GPCR. The bradykinin B2 receptor: an alternative and antiproliferative pathway]". Néphrologie. 23 (1): 39–41. PMID 11908480.
• Ariza AC, Bobadilla NA, Halhali A (2007). "[Endothelin 1 and angiotensin II in preeeclampsia]". Rev. Invest. Clin. 59 (1): 48–56. PMID 17569300.
• Hess JF, Borkowski JA, Young GS, et al. (1992). "Cloning and pharmacological characterization of a human bradykinin (BK-2) receptor". Biochem. Biophys. Res. Commun. 184 (1): 260–8. doi:10.1016/0006-291X(92)91187-U. PMID 1314587.
• Eggerickx D, Raspe E, Bertrand D, et al. (1992). "Molecular cloning, functional expression and pharmacological characterization of a human bradykinin B2 receptor gene". Biochem. Biophys. Res. Commun. 187 (3): 1306–13. doi:10.1016/0006-291X(92)90445-Q. PMID 1329734.
• Kammerer S, Braun A, Arnold N, Roscher AA (1995). "The human bradykinin B2 receptor gene: full length cDNA, genomic organization and identification of the regulatory region". Biochem. Biophys. Res. Commun. 211 (1): 226–33. doi:10.1006/bbrc.1995.1800. PMID 7779089.
• Braun A, Kammerer S, Böhme E, et al. (1995). "Identification of polymorphic sites of the human bradykinin B2 receptor gene". Biochem. Biophys. Res. Commun. 211 (1): 234–40. doi:10.1006/bbrc.1995.1801. PMID 7779090.
• Ma JX, Wang DZ, Ward DC, et al. (1995). "Structure and chromosomal localization of the gene (BDKRB2) encoding human bradykinin B2 receptor". Genomics. 23 (2): 362–9. doi:10.1006/geno.1994.1512. PMID 7835885.
• Powell SJ, Slynn G, Thomas C, et al. (1993). "Human bradykinin B2 receptor: nucleotide sequence analysis and assignment to chromosome 14". Genomics. 15 (2): 435–8. doi:10.1006/geno.1993.1084. PMID 7916737.
• Menke JG, Borkowski JA, Bierilo KK, et al. (1994). "Expression cloning of a human B1 bradykinin receptor". J. Biol. Chem. 269 (34): 21583–6. PMID 8063797.
• Hess JF, Borkowski JA, Macneil T, et al. (1994). "Differential pharmacology of cloned human and mouse B2 bradykinin receptors". Mol. Pharmacol. 45 (1): 1–8. PMID 8302267.
• McIntyre P, Phillips E, Skidmore E, et al. (1993). "Cloned murine bradykinin receptor exhibits a mixed B1 and B2 pharmacological selectivity". Mol. Pharmacol. 44 (2): 346–55. PMID 8394991.
• AbdAlla S, Godovac-Zimmermann J, Braun A, et al. (1996). "Structure of the bradykinin B2 receptors' amino terminus". Biochemistry. 35 (23): 7514–9. doi:10.1021/bi9601060. PMID 8652530.
• Isami S, Kishikawa H, Araki E, et al. (1996). "Bradykinin enhances GLUT4 translocation through the increase of insulin receptor tyrosine kinase in primary adipocytes: evidence that bradykinin stimulates the insulin signalling pathway". Diabetologia. 39 (4): 412–20. doi:10.1007/BF00400672. PMID 8777990.
• Dalemar LR, Ivy Jong YJ, Wilhelm B, Baenziger NL (1996). "Protein kinases A and C rapidly modulate expression of human lung fibroblast B2 bradykinin receptor affinity forms". Eur. J. Cell Biol. 69 (3): 236–44. PMID 8900488.
• Soskic V, Nyakatura E, Roos M, et al. (1999). "Correlations in palmitoylation and multiple phosphorylation of rat bradykinin B2 receptor in Chinese hamster ovary cells". J. Biol. Chem. 274 (13): 8539–45. doi:10.1074/jbc.274.13.8539. PMID 10085087.
• Cassano G, Susca F, Lippe C, Guanti G (1999). "Two B1 and B2 bradykinin receptor antagonists fail to inhibit the Ca2+ response elicited by bradykinin in human skin fibroblasts". Gen. Pharmacol. 32 (2): 239–44. doi:10.1016/S0306-3623(98)00275-4. PMID 10188626.
• Efremov R, Truong MJ, Darcissac EC, et al. (1999). "Human chemokine receptors CCR5, CCR3 and CCR2B share common polarity motif in the first extracellular loop with other human G-protein coupled receptors implications for HIV-1 coreceptor function". Eur. J. Biochem. 263 (3): 746–56. doi:10.1046/j.1432-1327.1999.00553.x. PMID 10469138.
• Marrero MB, Venema VJ, Ju H, et al. (1999). "Endothelial nitric oxide synthase interactions with G-protein-coupled receptors". Biochem. J. 343 (2): 335–40. doi:10.1042/0264-6021:3430335. PMC 1220558. PMID 10510297.
• Reyes-Cruz G, Vázquez-Prado J, Müller-Esterl W, Vaca L (2000). "Regulation of the human bradykinin B2 receptor expressed in sf21 insect cells: a possible role for tyrosine kinases". J. Cell. Biochem. 76 (4): 658–73. doi:10.1002/(SICI)1097-4644(20000315)76:4<658::AID-JCB14>3.0.CO;2-7. PMID 10653985.
• Golser R, Gorren AC, Leber A, et al. (2000). "Interaction of endothelial and neuronal nitric-oxide synthases with the bradykinin B2 receptor. Binding of an inhibitory peptide to the oxygenase domain blocks uncoupled NADPH oxidation". J. Biol. Chem. 275 (8): 5291–6. doi:10.1074/jbc.275.8.5291. PMID 10681501.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.