Beta-1 adrenergički receptor

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Adrenergički, beta-1, receptor
Identifikatori
SimboliADRB1; ADRB1R; B1AR; BETA1AR; RHR
Vanjski IDOMIM: 109630 MGI: 87937 HomoloGene: 20171 IUPHAR: β1-adrenoceptor GeneCards: ADRB1 Gene
Ontologija gena
Molekularna funkcija • rodopsinu-slična receptorska aktivnost
• receptorska aktivnost
• adrenoceptorska aktivnost
• beta1-adrenergička receptorska aktivnost
• proteinsko vezivanje
Celularna komponenta • membranska frakcija
• ćelijska membrana
• integralno sa ćelijskom membranom
• membrana
• integralno sa membranom
Biološki proces • pozitivna regulacija brzine kontrakcija srca epinefrin-norepinefrinom
• povišenje jačine srčanih kontrakcija epinefrin-norepinefrinom
• dijetom indukovana termogeneza
• norepinefrin-epinefrinska vazodilacija tokom regulacije krvnog pritiska
• prenos signala
• signalni put G-protein spregnutog receptora
• aktivacija adenilat ciklaze
• respons na hladnoću
• stvaranje toplote
• negativna regulacija veličine tela
• odgovor na strah
• diferencijacija smeđih masnih ćelija
Pregled RNK izražavanja
podaci
Ortolozi
VrstaČovekMiš
Entrez15311554
EnsemblENSG00000043591ENSMUSG00000035283
UniProtP08588Q9CRR2
RefSeq (mRNA)NM_000684NM_007419
RefSeq (protein)NP_000675NP_031445
Lokacija (UCSC)Chr 10:
115.79 - 115.8 Mb		Chr 19:
56.78 - 56.78 Mb
PubMed pretraga[1][2]

Beta-1 adrenergički receptor (β1 adrenoreceptor), ili ADRB1, je beta-adrenergički receptor. ADRB1 je takođe oznaka za ljudski gen koji ga kodira.[1] On je G-protein spregnuti receptor koji vezuje Gs heterotrimerni G protein.

Receptor

Dejstva

Dejstva β1 receptora obuhvataju:

  • stimuliše viskozne, amilazom-zasićene sekrecije pljuvačnih žlezda[2]
  • Povećava srčani izlaz
    • Povećava brzinu srca [3]
    • Povećava kontraktilnost atrijalnog miokarda.
    • Povećava kontraktilnost[3] ventrikularnog miokarda.
    • Povećava provođenje[3] atrioventrikularnog čvora (AV čvor)
  • Oslobađanje renina iz jukstaglomerularnih ćelija[3].
  • Lipoliza u adipoznom tkivu[3].
  • Receptor je takođe prisutan u cerebralnom korteksu.

Agonisti

Izoprenalin ima veći afinitet za β1 od noradrenalina, koji se vezuje sa većim afinitetom od adrenalina. Selektivni agonisti beta-1 receptora su:

Antagonisti

β1-selektivni antagonisti (Beta blokatori) su:

Mehanizam

Gs uzrokuje aktivaciju adenilat ciklaze, što dovodi do povećanja cAMP koncentracije.

Gen

Ustanovljeno je da specifični polimorfizmi ovog gena utiču na brzinu rada srca i da mogu da imaju udela u srčanoj insuficijenciji.[1]

Interakcije

Za beta-1 adrenergički receptor je pokazano da interaguje sa DLG4[6] i GIPC1.[7]

Reference

  1. ↑ 1,0 1,1 „Entrez Gene: ADRB1 adrenergic, beta-1-, receptor”. 
  2. ↑ 2,0 2,1 2,2 2,3 Rang, H. P. (2003). Pharmacology. Edinburgh: Churchill Livingstone. str. 163. ISBN 0-443-07145-4. 
  3. ↑ 3,0 3,1 3,2 3,3 3,4 Fitzpatrick, David; Purves, Dale; Augustine, George (2004). „Table 20:2”. Neuroscience (Third izd.). Sunderland, Mass: Sinauer. ISBN 0-87893-725-0. 
  4. ↑ Rang, H. P. (2003). Pharmacology. Edinburgh: Churchill Livingstone. ISBN 0-443-07145-4.  Page 163
  5. ↑ American Society of Health-System Pharmacists, Inc. (1. 1. 2005.). „Bisoprolol”. MedlinePlus Drug Information. U.S. National Library of Medicine, National Institutes of Health. Arhivirano iz originala na datum 2008-05-20. Pristupljeno 6. 6. 2008. 
  6. ↑ Hu, L A; Tang Y, Miller W E, Cong M, Lau A G, Lefkowitz R J, Hall R A (December 2000). „beta 1-adrenergic receptor association with PSD-95. Inhibition of receptor internalization and facilitation of beta 1-adrenergic receptor interaction with N-methyl-D-aspartate receptors”. J. Biol. Chem. (UNITED STATES) 275 (49): 38659–66. DOI:10.1074/jbc.M005938200. ISSN 0021-9258. PMID 10995758. 
  7. ↑ Hu, Liaoyuan A; Chen Wei, Martin Negin P, Whalen Erin J, Premont Richard T, Lefkowitz Robert J (July 2003). „GIPC interacts with the beta1-adrenergic receptor and regulates beta1-adrenergic receptor-mediated ERK activation”. J. Biol. Chem. (United States) 278 (28): 26295–301. DOI:10.1074/jbc.M212352200. ISSN 0021-9258. PMID 12724327. 

Literatura

  • Rang, H. P. (2003). Pharmacology. Edinburgh: Churchill Livingstone. ISBN 0-443-07145-4. 
  • Frielle T, Kobilka B, Lefkowitz RJ, Caron MG (1989). „Human beta 1- and beta 2-adrenergic receptors: structurally and functionally related receptors derived from distinct genes.”. Trends Neurosci. 11 (7): 321–4. DOI:10.1016/0166-2236(88)90095-1. PMID 2465637. 
  • Muszkat M (2007). „Interethnic differences in drug response: the contribution of genetic variability in beta adrenergic receptor and cytochrome P4502C9.”. Clin. Pharmacol. Ther. 82 (2): 215–8. DOI:10.1038/sj.clpt.6100142. PMID 17329986. 
  • Yang-Feng TL, Xue FY, Zhong WW, et al. (1990). „Chromosomal organization of adrenergic receptor genes.”. Proc. Natl. Acad. Sci. U.S.A. 87 (4): 1516–1520. DOI:10.1073/pnas.87.4.1516. PMC 53506. PMID 2154750. 
  • Forse RA, Leibel R, Gagner M (1989). „The effect of Escherichia coli endotoxin on the adrenergic control of lipolysis in the human adipocyte.”. J. Surg. Res. 46 (1): 41–8. DOI:10.1016/0022-4804(89)90180-7. PMID 2536864. 
  • Frielle T, Collins S, Daniel KW, et al. (1987). „Cloning of the cDNA for the human beta 1-adrenergic receptor.”. Proc. Natl. Acad. Sci. U.S.A. 84 (22): 7920–7924. DOI:10.1073/pnas.84.22.7920. PMC 299447. PMID 2825170. 
  • Stiles GL, Strasser RH, Lavin TN, et al. (1983). „The cardiac beta-adrenergic receptor. Structural similarities of beta 1 and beta 2 receptor subtypes demonstrated by photoaffinity labeling.”. J. Biol. Chem. 258 (13): 8443–8449. PMID 6305985. 
  • Hoehe MR, Otterud B, Hsieh WT, et al. (1995). „Genetic mapping of adrenergic receptor genes in humans.”. J. Mol. Med. 73 (6): 299–306. DOI:10.1007/BF00231616. PMID 7583452. 
  • Elies R, Ferrari I, Wallukat G, et al. (1996). „Structural and functional analysis of the B cell epitopes recognized by antireceptor autoantibodies in patients with Chagas' disease.”. J. Immunol. 157 (9): 4203–4211. PMID 8892658. 
  • Oldenhof J, Vickery R, Anafi M, et al. (1998). „SH3 binding domains in the dopamine D4 receptor.”. Biochemistry 37 (45): 15726–36. DOI:10.1021/bi981634. PMID 9843378. 
  • Mason DA, Moore JD, Green SA, Liggett SB (1999). „A gain-of-function polymorphism in a G-protein coupling domain of the human beta1-adrenergic receptor.”. J. Biol. Chem. 274 (18): 12670–4. DOI:10.1074/jbc.274.18.12670. PMID 10212248. 
  • Moore JD, Mason DA, Green SA, et al. (1999). „Racial differences in the frequencies of cardiac beta(1)-adrenergic receptor polymorphisms: analysis of c145A>G and c1165G>C.”. Hum. Mutat. 14 (3): 271. DOI:10.1002/(SICI)1098-1004(1999)14:3<271::AID-HUMU14>3.0.CO;2-Q. PMID 10477438. 
  • Tang Y, Hu LA, Miller WE, et al. (1999). „Identification of the endophilins (SH3p4/p8/p13) as novel binding partners for the beta1-adrenergic receptor.”. Proc. Natl. Acad. Sci. U.S.A. 96 (22): 12559–64. DOI:10.1073/pnas.96.22.12559. PMC 22990. PMID 10535961. 
  • Podlowski S, Wenzel K, Luther HP, et al. (2000). „Beta1-adrenoceptor gene variations: a role in idiopathic dilated cardiomyopathy?”. J. Mol. Med. 78 (2): 87–93. DOI:10.1007/s001090000080. PMID 10794544. 
  • Shiina T, Kawasaki A, Nagao T, Kurose H (2000). „Interaction with beta-arrestin determines the difference in internalization behavor between beta1- and beta2-adrenergic receptors.”. J. Biol. Chem. 275 (37): 29082–90. DOI:10.1074/jbc.M909757199. PMID 10862778. 
  • Hu LA, Tang Y, Miller WE, et al. (2001). „beta 1-adrenergic receptor association with PSD-95. Inhibition of receptor internalization and facilitation of beta 1-adrenergic receptor interaction with N-methyl-D-aspartate receptors.”. J. Biol. Chem. 275 (49): 38659–66. DOI:10.1074/jbc.M005938200. PMID 10995758. 
  • Börjesson M, Magnusson Y, Hjalmarson A, Andersson B (2001). „A novel polymorphism in the gene coding for the beta(1)-adrenergic receptor associated with survival in patients with heart failure.”. Eur. Heart J. 21 (22): 1853–1858. DOI:10.1053/euhj.1999.1994. PMID 11052857. 
  • Xu J, Paquet M, Lau AG, et al. (2001). „beta 1-adrenergic receptor association with the synaptic scaffolding protein membrane-associated guanylate kinase inverted-2 (MAGI-2). Differential regulation of receptor internalization by MAGI-2 and PSD-95.”. J. Biol. Chem. 276 (44): 41310–7. DOI:10.1074/jbc.M107480200. PMID 11526121. 
  • Hu LA, Chen W, Premont RT, et al. (2002). „G protein-coupled receptor kinase 5 regulates beta 1-adrenergic receptor association with PSD-95.”. J. Biol. Chem. 277 (2): 1607–1613. DOI:10.1074/jbc.M107297200. PMID 11700307. 
  • Ranade K, Jorgenson E, Sheu WH, et al. (2002). „A polymorphism in the beta1 adrenergic receptor is associated with resting heart rate.”. Am. J. Hum. Genet. 70 (4): 935–42. DOI:10.1086/339621. PMC 379121. PMID 11854867. 

}}

  • Rang, H. P. (2003). Pharmacology. Edinburgh: Churchill Livingstone. str. 163. ISBN 0-443-07145-4. 
  • Fitzpatrick, David; Purves, Dale; Augustine, George (2004). „Table 20:2”. Neuroscience (Third izd.). Sunderland, Mass: Sinauer. ISBN 0-87893-725-0. 

Spoljašnje veze

  • „β1-adrenoceptor”. IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology. Arhivirano iz originala na datum 2015-06-06. 
  • p
  • r
  • u
Klasa A: Rodopsinu slični
α1 (A, B, D) • α2 (A, B, C) • β1 • β2 • β3
Adenozinski (A1, A2A, A2B, A3) • P2Y (1, 2, 4, 5, 6, 8, 9, 10, 11, 12, 13, 14)
(svi osim 5-HT3) 5-HT1 (A, B, D, E, F) • 5-HT2 (A, B, C) • 5-HT (4, 5A, 6, 7)
Drugi
Acetilholin (M1, M2, M3, M4, M5) • Dopamin (D1, D2, D3, D4, D5) • Histamin (H1, H2, H3, H4) • Melatonin (1A, 1B, 1C) • TAAR (1, 2, 3, 5, 6, 8, 9)
Metaboliti i
signalni molekuli
CysLT (1, 2) • LTB4 (1, 2) • FPRL1 • OXE • Prostaglandin (DP (1, 2), EP (1, 2, 3, 4), FP) • Prostaciklin • Tromboksan
Drugi
Žučna kiselina • Kanabinoidni (CB1, CB2, GPR (18, 55, 119)) • EBI2 • Estrogen • Slobodna masna kiselina (1, 2, 3, 4) • Laktat  • Lizofosfatidna kiselina (1, 2, 3, 4, 5, 6)  • Lizofosfolipid (1, 2, 3, 4, 5, 6, 7, 8) • Niacin (1, 2) • Oksoglutarat • PAF • Sfingozin-1-fosfat (1, 2, 3, 4, 5) • Sukcinat
Peptid
B/W (1, 2) • FF (1, 2) • S • Y (1, 2, 4, 5) • Neuromedin (B, U (1, 2)) • Neurotenzin (1, 2)
Drugi
Anafilatoksin (C3a, C5a) • Angiotenzin (1, 2) • Apelin • Bombezin (BRS3, GRPR, NMBR) • Bradikinin (B1, B2) • Hemokin • Holecistokinin (A, B) • Endotelin (A, B) • Formil peptid (1, 2, 3) • FSH • Galanin (1, 2, 3) • GHB receptor • Gonadotropin-oslobađajući hormon (1, 2) • Grelin • Kispeptin • Luteinizirajući hormon/horiogonadotropin • MAS (1, 1L, D, E, F, G, X1, X2, X3, X4) • Melanokortin (1, 2, 3, 4, 5) • MCHR (1, 2) • Motilin • Opioidni (δ, κ, μ, Nociceptin & ζ, ali ne σ) • Oreksin (1, 2) • Oksitocin • Prokineticin (1, 2) • Prolaktin-oslobađajući peptid • Relaksin (1, 2, 3, 4) • Somatostatin (1, 2, 3, 4, 5) • Tahikinin (1, 2, 3) • Tirotropin • Tirotropin-oslobađajući hormon • Urotenzin-II • Vazopresin (1A, 1B, 2)
Razno
GPR (1, 3, 4, 6, 12, 15, 17, 18, 19, 20, 21, 22, 23, 25, 26, 27, 31, 32, 33, 34, 35, 37, 39, 42, 44, 45, 50, 52, 55, 61, 62, 63, 65, 68, 75, 77, 78, 81, 82, 83, 84, 85, 87, 88, 92, 101, 103, 109A, 109B, 119, 120, 132, 135, 137B, 139, 141, 142, 146, 148, 149, 150, 151, 152, 153, 160, 161, 162, 171, 173, 174, 176, 177, 182, 183)
Drugi
Adrenomedulin • Mirisni • Opsin (3, 4, 5, 1LW, 1MW, 1SW, RGR, RRH) • Proteazom-aktivirani (1, 2, 3, 4) • SREB (1, 2, 3)
Klasa B: Sekretinu slični
GPR (56, 64, 97, 98, 110, 111, 112, 113, 114, 115, 116, 123, 124, 125, 126, 128, 133, 143, 144, 155, 157)
Drugi
Klasa C: Metabotropni
glutamat / feromon
TAS1R (1, 2, 3) • TAS2R (1, 3, 4, 5, 8, 9, 10, 12, 13, 14, 16, 19, 20, 30, 31, 38, 39, 40, 41, 42, 43, 45, 46, 50)
Drugi
Klasa F:
Frizzled / Zaglađeni
Uvojiti
Frizzled (1, 2, 3, 4, 5, 6, 7, 8, 9, 10)
Zaglađeni
B trdu: peptidi (nrpl/grfl/cytl/horl), receptori (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd, signalni putevi (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)