Bradikininski receptor B2

Из Википедије, слободне енциклопедије
Bradikininski receptor B2
Identifikatori
Simboli BDKRB2; B2R; BK-2; BK2; BKR2; BRB2; DKFZp686O088
Vanjski ID OMIM113503 MGI102845 HomoloGene519 IUPHAR: B2 GeneCards: BDKRB2 Gene
Pregled RNK izražavanja
PBB GE BDKRB2 205870 at tn.png
podaci
Ortolozi
Vrsta Čovek Miš
Entrez 624 12062
Ensembl ENSG00000168398 ENSMUSG00000021070
UniProt P30411 P32299
RefSeq (mRNA) NM_000623 NM_009747
RefSeq (protein) NP_000614 NP_033877
Lokacija (UCSC) Chr 14:
95.74 - 95.78 Mb
Chr 12:
105.96 - 105.99 Mb
PubMed pretraga [1] [2]

Bradikininski receptor B2 je G-protein spregnuti receptor bradikinina. Njega kodira BDKRB2 gen kod čoveka.

Mehanizam[уреди]

B2 receptor je G protein-spregnuti receptor. Pretpostavlja se da je spregnut sa Gq, dok Gi. Gq stimuliše fosfolipazu C i povišava koncentraciju Intracelularnog slobodnog kalcijuma i Gi inhibira adenilat ciklazu. Pored toga, receptor stimuliše puteve mitogenom-aktiviranih proteinskih kinaza. On je široko rasprostranjen i konstitutivno izražen u zdravim tkivima.

B2 receptor formira kompleks sa angiotenzin konvertujućim enzimom (ACE), i stoga se smatra da učestvuje u razmeni informacija između renin-angiotenzinskog sistema (RAS) i kinin-kalikreinskog sistema (KKS). Heptapeptid angiotenzin 1-7 (A1-7) takođe pojačava dejstvo bradikinina na B2 receptore.[1]

Kalidin takođe dejstvuje kroz B2 receptor.

Funkcija[уреди]

Bradikinin je peptid sa 9 aminokiselina koji proizvodi mnogobrojne response kao što su vazodilatacija, edemi i spazam glatkih mišića.

Vidi još[уреди]

Bradikininski receptor

Literatura[уреди]

  1. ^ Fernandes L, Fortes ZB, Nigro D, Tostes RC, Santos RA, Catelli De Carvalho MH (2001). „Potentiation of bradykinin by angiotensin-(1-7) on arterioles of spontaneously hypertensive rats studied in vivo“. Hypertension 37 (2 Part 2): 703–9. PMID 11230360. 

Dodatna literatura[уреди]

  • 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. 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.