Alpha-2B adrenergic receptor

This MedLibrary.org supplementary page on Alpha-2B adrenergic receptor is provided directly from the open source Wikipedia as a service to our readers. Please see the note below on authorship of this content, as well as the Wikipedia usage guidelines. To search for other content from our encyclopedia supplement, please use the form below:

Related Sponsors

BM Pharmacy Generic pharmaceuticals at unbeatable prices. Insomnia, men's health, hair health, pain control. bmpharmacy.com
Online Pharmacy Carisoprodol, tadalafil, sildenafil, vardenafil and more... xlpharmacy.com
MedBasket.com Discreet. Inexpensive. Fast shipping. Great selection. What more can we say? medbasket.com
Frugalmed 2000 reasons to shop with us first. frugalmed.com
Ads by Tiva

Adrenergic, alpha-2B-, receptor
Identifiers
Symbols ADRA2B; ADRA2L1; ADRA2RL1; ADRARL1; ALPHA2BAR
External IDs OMIM: 104260 MGI: 87935 HomoloGene: 553
Orthologs
Human Mouse
Entrez 151 11552
Ensembl n/a ENSMUSG00000058620
Uniprot n/a Q6NXV9
Refseq NM_000682 (mRNA)
NP_000673 (protein)		 NM_009633 (mRNA)
NP_033763 (protein)
Location n/a Chr 2: 127.05 - 127.06 Mb
Pubmed search [1] [2]

The alpha-2B adrenergic receptor (α2B adrenoreceptor), also known as ADRA2B, is an alpha-2 adrenergic receptor, and also denotes the human gene encoding it.[1]

Contents

Receptor

Alpha-2-adrenergic receptors include 3 highly homologous subtypes: alpha2A, alpha2B, and alpha2C. These receptors have a critical role in regulating neurotransmitter release from sympathetic nerves and from adrenergic neurons in the central nervous system.

Gene

This gene encodes the alpha2B subtype, which was observed to associate with eIF-2B, a guanine nucleotide exchange protein that functions in regulation of translation. A polymorphic variant of the alpha2B subtype, which lacks 3 glutamic acids from a glutamic acid repeat element, was identified to have decreased G protein-coupled receptor kinase-mediated phosphorylation and desensitization; this polymorphic form is also associated with reduced basal metabolic rate in obese subjects and may therefore contribute to the pathogenesis of obesity. This gene contains no introns in either its coding or untranslated sequences.[1]

See also

References

  1. ^ a b "Entrez Gene: ADRA2B adrenergic, alpha-2B-, receptor".

Further reading

  • Lomasney JW, Lorenz W, Allen LF, et al. (1990). "Expansion of the alpha 2-adrenergic receptor family: cloning and characterization of a human alpha 2-adrenergic receptor subtype, the gene for which is located on chromosome 2.". Proc. Natl. Acad. Sci. U.S.A. 87 (13): 5094–8. PMID 2164221. 
  • McClue SJ, Milligan G (1990). "The alpha 2B adrenergic receptor of undifferentiated neuroblastoma x glioma hybrid NG108-15 cells, interacts directly with the guanine nucleotide binding protein, Gi2.". FEBS Lett. 269 (2): 430–4. PMID 2169434. 
  • Weinshank RL, Zgombick JM, Macchi M, et al. (1990). "Cloning, expression, and pharmacological characterization of a human alpha 2B-adrenergic receptor.". Mol. Pharmacol. 38 (5): 681–8. PMID 2172775. 
  • Chang AC, Ho TF, Chang NC (1990). "In vitro amplification by polymerase chain reaction of a partial gene encoding the third subtype of alpha-2 adrenergic receptor in humans.". Biochem. Biophys. Res. Commun. 172 (2): 817–23. PMID 2173582. 
  • Regan JW, Kobilka TS, Yang-Feng TL, et al. (1988). "Cloning and expression of a human kidney cDNA for an alpha 2-adrenergic receptor subtype.". Proc. Natl. Acad. Sci. U.S.A. 85 (17): 6301–5. PMID 2842764. 
  • Petrash AC, Bylund DB (1986). "Alpha-2 adrenergic receptor subtypes indicated by [3H]yohimbine binding in human brain.". Life Sci. 38 (23): 2129–37. PMID 3012234. 
  • Klein U, Ramirez MT, Kobilka BK, von Zastrow M (1997). "A novel interaction between adrenergic receptors and the alpha-subunit of eukaryotic initiation factor 2B.". J. Biol. Chem. 272 (31): 19099–102. PMID 9235896. 
  • Okusa MD, Huang L, Momose-Hotokezaka A, et al. (1998). "Regulation of adenylyl cyclase in polarized renal epithelial cells by G protein-coupled receptors.". Am. J. Physiol. 273 (6 Pt 2): F883–91. PMID 9435676. 
  • Prezeau L, Richman JG, Edwards SW, Limbird LE (1999). "The zeta isoform of 14-3-3 proteins interacts with the third intracellular loop of different alpha2-adrenergic receptor subtypes.". J. Biol. Chem. 274 (19): 13462–9. PMID 10224112. 
  • Heinonen P, Koulu M, Pesonen U, et al. (1999). "Identification of a three-amino acid deletion in the alpha2B-adrenergic receptor that is associated with reduced basal metabolic rate in obese subjects.". J. Clin. Endocrinol. Metab. 84 (7): 2429–33. PMID 10404816. 
  • Hein L, Altman JD, Kobilka BK (2000). "Two functionally distinct alpha2-adrenergic receptors regulate sympathetic neurotransmission.". Nature 402 (6758): 181–4. doi:10.1038/46040. PMID 10647009. 
  • Small KM, Brown KM, Forbes SL, Liggett SB (2001). "Polymorphic deletion of three intracellular acidic residues of the alpha 2B-adrenergic receptor decreases G protein-coupled receptor kinase-mediated phosphorylation and desensitization.". J. Biol. Chem. 276 (7): 4917–22. doi:10.1074/jbc.M008118200. PMID 11056163. 
  • Snapir A, Mikkelsson J, Perola M, et al. (2003). "Variation in the alpha2B-adrenoceptor gene as a risk factor for prehospital fatal myocardial infarction and sudden cardiac death.". J. Am. Coll. Cardiol. 41 (2): 190–4. PMID 12535806. 
  • Sykiotis GP, Polyzogopoulou E, Georgopoulos NA, et al. (2004). "The alpha2B adrenergic receptor deletion/insertion polymorphism in morbid obesity.". Clin. Auton. Res. 13 (3): 203–7. doi:10.1007/s10286-003-0087-5. PMID 12822042. 
  • Chotani MA, Mitra S, Su BY, et al. (2004). "Regulation of alpha(2)-adrenoceptors in human vascular smooth muscle cells.". Am. J. Physiol. Heart Circ. Physiol. 286 (1): H59–67. doi:10.1152/ajpheart.00268.2003. PMID 12946937. 
  • Von Wowern F, Bengtsson K, Lindblad U, et al. (2004). "Functional variant in the (alpha)2B adrenoceptor gene, a positional candidate on chromosome 2, associates with hypertension.". Hypertension 43 (3): 592–7. doi:10.1161/01.HYP.0000116224.51189.80. PMID 14744925. 
  • Cayla C, Heinonen P, Viikari L, et al. (2004). "Cloning, characterisation and identification of several polymorphisms in the promoter region of the human alpha2B-adrenergic receptor gene.". Biochem. Pharmacol. 67 (3): 469–78. doi:10.1016/j.bcp.2003.09.029. PMID 15037199. 
  • Phares DA, Halverstadt AA, Shuldiner AR, et al. (2004). "Association between body fat response to exercise training and multilocus ADR genotypes.". Obes. Res. 12 (5): 807–15. PMID 15166301. 
  • Siitonen N, Lindström J, Eriksson J, et al. (2005). "Association between a deletion/insertion polymorphism in the alpha2B-adrenergic receptor gene and insulin secretion and Type 2 diabetes. The Finnish Diabetes Prevention Study.". Diabetologia 47 (8): 1416–24. doi:10.1007/s00125-004-1462-z. PMID 15309292. 
  • Belfer I, Buzas B, Hipp H, et al. (2005). "Haplotype-based analysis of alpha 2A, 2B, and 2C adrenergic receptor genes captures information on common functional loci at each gene.". J. Hum. Genet. 50 (1): 12–20. doi:10.1007/s10038-004-0211-y. PMID 15592690. 
 This transmembrane receptor-related article is a stub. You can help Wikipedia by expanding it.
v • d • e
Transmembrane receptor: G protein-coupled receptors
Class A: Rhodopsin like
α1 (A, B, D), α2 (A, B, C), β1, β2, β3
CysLT (1, 2), LTB4 (1, 2), FPRL1, OXE, Prostaglandin (DP, EP (1, 2, 3, 4), PGF), Prostacyclin, Thromboxane
B/W (1, 2), FF (1, 2), S, Y (1, 2, 4, 5)
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, 79, 82, 83, 84, 85, 87, 88, 92, 101, 103, 119, 120, 132, 135, 139, 141, 142, 146, 148, 149, 150, 151, 152, 153, 160, 161, 162, 171, 172, 173, 174, 176, 177, 182)
Adenosine (A1, A2a, A2b, A3), P2Y, (1, 2, 4, 5, 6, 8, 9, 10, 11, 12, 13, 14)
(all but 5-HT3) 5-HT1 (A, B, D, E, F), 5-HT2 (A, B, C), 5-HT (4, 5A, 6, 7)
Other
Acetylcholine (M1, M2, M3, M4, M5) - Adrenomedullin - Anaphylatoxin (C3a, C5a) - Angiotensin (1, 2) - Apelin - Bile acid - Bombesin (BRS3, GRPR, NMBR) - Bradykinin (B1, B2) - Cannabinoid (CB1, CB2) - Chemokine - Cholecystokinin (A, B) - Dopamine (D1, D2, D3, D4, D5) - EBI2 - Endothelin (A, B) - Estrogen - Formyl peptide (1, L1, L2) - Free fatty acid (1, 2, 3, 4) - FSH - Galanin (1, 2, 3) - Gonadotropin-releasing hormone (1, 2) - Ghrelin - Histamine (H1, H2, H3, H4) - Kisspeptin - Luteinizing hormone/choriogonadotropin - Lysophospholipid (1, 2, 3, 4, 5, 6, 7, 8) - MAS (1, 1L, D, E, F, G, X1, X2, X3, X4) - Melanocortin (1, 2, 3, 4, 5) - MCHR (1, 2) - Melatonin (1A, 1B)- Motilin - neuromedin (B, U (1, 2)) - Neurotensin (1, 2) - Opioid (Delta, Kappa, Mu, Nociceptin, but not Sigma) - Olfactory - Opsin (3, 4, 5, 1LW, 1MW, 1SW, RGR, RRH) - Orexin (1, 2) - Oxytocin - Oxoglutarate - PAF - Prokineticin (1, 2) - Prolactin-releasing peptide - Protease-activated (1, 2, 3, 4) - Relaxin (1, 2, 3, 4) - Somatostatin (1, 2, 3, 4, 5) - SREB - Succinate - TAAR (1, 2, 3, 5, 6, 8, 9) - Tachykinin (1, 2, 3) - Thyrotropin - Thyrotropin-releasing hormone - Urotensin-II - Vasopressin (1A, 1B, 2)
Class B: Secretin like
Class C: Metabotropic
glutamate / pheromone
Calcium-sensing receptor - GABA B (1, 2) - Glutamate receptor (Metabotropic glutamate (1, 2, 3, 4, 5, 6, 7, 8)) - GPRC6A - GPR (156, 158, 179) - RAIG (1, 2, 3, 4) - Taste receptors (TAS1R (1, 2, 3) TAS2R (1, 3, 4, 5, 8, 9, 10, 12, 13, 14, 16, 38, 39, 40, 41, 43, 44, 45, 46, 47, 48, 49, 50))
Frizzled / Smoothened
Frizzled (1, 2, 3, 4, 5, 6, 7, 8, 9, 10) - Smoothened

Wikipedia content modification information:

  • This page was last modified on 8 July 2008, at 10:53.

Wikipedia Authorship and Review

Wikipedia content provided here is not reviewed directly by MedLibrary.org. Wikipedia content is authored by an open community of volunteers and is not produced by or in any way affiliated with MedLibrary.org.

Wikipedia Usage Guidelines

This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article on "Alpha-2B adrenergic receptor".

The URL for this specific entry is:

All Wikipedia text is available under the terms of the GNU Free Documentation License. (See Copyrights for details). Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc.