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Bradykinin receptor B2
Symbols BDKRB2; B2R; BK-2; BK2; BKR2; BRB2; DKFZp686O088
External IDs OMIM113503 MGI102845 HomoloGene519 IUPHAR: B2 GeneCards: BDKRB2 Gene
RNA expression pattern
PBB GE BDKRB2 205870 at tn.png
More reference expression data
Species Human Mouse
Entrez 624 12062
Ensembl ENSG00000168398 ENSMUSG00000021070
UniProt P30411 P32299
RefSeq (mRNA) NM_000623 NM_009747
RefSeq (protein) NP_000614 NP_033877
Location (UCSC) Chr 14:
95.74 - 95.78 Mb
Chr 12:
105.96 - 105.99 Mb
PubMed search [1] [2]

Bradykinin receptor B2 (B2) is a g-protein coupled receptor for bradykinin, encoded by the BDKRB2 gene in humans.



The B2 receptor is a G protein-coupled receptor, probably coupled to Gq and Gi. Gq stimulates phospholipase C to increase intracellular free calcium and Gi 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 (A1-7) also potentiates bradykinin action on B2 receptors.[1]

Kallidin also signals through the B2 receptor.


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


Alternate start codons result in two isoforms of the protein.[2]

See also


External links

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 Pt 2: 335–40. doi:10.1042/0264-6021:3430335. 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.



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