logo logo
 
 
SmartSection is developed by The SmartFactory (http://www.smartfactory.ca), a division of INBOX Solutions (http://inboxinternational.com)
Adrenergic Receptor Structure
Published by Anonymous on 2007/9/30 (2154 reads)
1: Postepy Hig Med Dosw. 1999;53(5):705-15.


[Beta-3 adrenergic receptor--structure and role in obesity and metabolic disorders]

[Article in Polish]

Wiejak J, Wyroba E.

Zakład Biologii Komórki, Instytut Biologii Doświadczalnej im. M. Nenckiego PAN w Warszawie.

Structure and essential motifs of beta 3-adrenergic receptor (known previously as atypical beta-AR), which plays a central role in regulation of lipid metabolism have been described. Obesity results from an imbalance between caloric intake and energy expenditure. The consequence of catecholamine activation of beta 3-AR is increased mobilization of fatty acids from triglyceride stores (lipolysis) in brown and white adipose tissue as well as increased fatty acid beta-oxidation and heat-production via UCP-1 (thermogenesis) in brown adipose tissue. A pharmacokinetic effects of beta 3-agonists and putative involvement of Trp/Arg mutation in beta 3-AR gene in obesity and another metabolic disorders have been discussed.

Publication Types:
English Abstract
Review

PMID: 10645145 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

2: Masui. 1997 Jun;46(6):770-6.


[Adrenergic receptor and alpha 2 agonist--2: Structure-function relationship of adrenoceptors]

[Article in Japanese]

Mizobe T.

Department of Anesthesiology, Kyoto Prefectural University of Medicine.

Recombinant DNA experiments using chimeric receptors containing portions of alpha 2 and beta 2 adrenoceptors demonstrated structure-function relationships of adrenoceptors. The seventh transmembrane domain determines the subtype ligand binding specificity between alpha 2 and beta 2 adrenoceptors. A further investigation by mutagenesis suggests that a direct interaction between subtype specific ligands and specific amino acids such as Phe (412) and Asn (312) in the seventh transmembrane domain of the alpha 2 and beta 2 adrenoceptors respectively. The third cytoplasmic loop is responsible for determining the specificity of interactions between the receptor and G protein. Recombinant DNA technology also demonstrated that seven transmembrane domains of adrenoceptors have a counterclockwise arrangement when viewed from the outside of the cell.

Publication Types:
English Abstract
Review

PMID: 9223879 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

3: Annu Rev Pharmacol Toxicol. 1997;37:421-50.


Structure and function of the beta 3-adrenergic receptor.

Strosberg AD.

Institut Cochin de Génétique Moléculaire, Laboratoire d'Immuno-Pharmacologie Moléculaire, CNRS UPR 0415, Paris, France.

The beta 3 subtype of adrenaline and noradrenaline receptors has now been extensively characterized at the structural and functional levels. Ligand binding and adenylyl cyclase activation studies helped define a beta-adrenergic profile that is quite distinct from that of the beta 1- and beta 2-adrenergic receptors, but strongly reminiscent of most of the "atypical" responses reported in earlier pharmacologic studies. Human, other large mammal, and rodent receptors share most of the characteristic beta 3 properties, although obvious species-specific differences have been identified. Recently, the incidence of a naturally occurring variant of the human beta 3-adrenergic receptor was shown to be correlated with hereditary obesity in Pima Indians and in Japanese individuals, and in Western obese patients with increased dynamic capacity to add on weight and develop non-insulin-dependent diabetes mellitus (NIDDM). A mild weight increase was also shown to develop in female, but not male, mice in which the beta 3 receptor gene was disrupted. Taken together, these results now provide a consistent picture of an important role of the beta 3-adrenoceptor in the regulation of lipid metabolism and as an obvious target for drugs to treat some forms of obesity.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 9131260 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

4: Circ Res. 1996 May;78(5):737-49.


alpha 1-adrenergic receptor subtypes. Molecular structure, function, and signaling.

Graham RM, Perez DM, Hwa J, Piascik MT.

Victor Chang Cardiac Research Institute, St Vincent's Hospital, Sydney, Australia.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 8620593 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

5: Pulm Pharmacol. 1995 Feb;8(1):1-10.


Implications of genetic variability of human beta 2-adrenergic receptor structure.

Green SA, Turki J, Hall IP, Liggett SB.

Department of Medicine (Pulmonary), University of Cincinnati, Ohio 45267-0564, USA.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 8535093 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

6: Annu Rev Pharmacol Toxicol. 1992;32:167-83.


Mutagenesis of the beta 2-adrenergic receptor: how structure elucidates function.

Ostrowski J, Kjelsberg MA, Caron MG, Lefkowitz RJ.

Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 1318669 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

7: Biochim Biophys Acta. 1991 Oct 26;1095(2):127-39.


Molecular biology of alpha-adrenergic receptors: implications for receptor classification and for structure-function relationships.

Lomasney JW, Cotecchia S, Lefkowitz RJ, Caron MG.

Department of Pathology, Howard Hughes Medical Institute, Duke University Medical Center, Durham 27710.

Publication Types:
Review

PMID: 1657194 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

8: Adv Exp Med Biol. 1991;308:223-38.


Structure and function of the adrenergic receptor family.

Roth NS, Lefkowitz RJ, Caron MG.

Howard Hughes Medical Institute, Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710.

Publication Types:
Review

PMID: 1801586 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

9: Vitam Horm. 1991;46:1-39.


Structure and regulation of G protein-coupled receptors: the beta 2-adrenergic receptor as a model.

Collins S, Lohse MJ, O'Dowd B, Caron MG, Lefkowitz RJ.

Howard Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710.

Publication Types:
Review

PMID: 1660639 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

10: Am Rev Respir Dis. 1990 Feb;141(2 Pt 2):S22-30.


Beta-adrenergic receptors. Relationship of primary structure, receptor function, and regulation.

Fraser CM, Venter JC.

Section of Receptor Biochemistry, National Institute of Neurological and Communicative Disorders and Stroke, National Institutes of Health, Bethesda, Maryland.

Publication Types:
Review

PMID: 2155553 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

11: Kidney Int Suppl. 1987 Dec;23:S2-13.


Structure and function of the beta 2-adrenergic receptor--homology with rhodopsin.

Dohlman HG, Caron MG, Lefkowitz RJ.

Howard Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, North Carolina.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 2831423 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

12: Bull Eur Physiopathol Respir. 1985 Sep-Oct;21(5):13s-18s.


Beta-adrenergic receptor structure, synthesis, antibodies and human disease.

Venter JC, Fraser CM.

Lung beta 2-adrenergic receptors have been isolated using a covalent affinity label and monoclonal and autoantibodies with specificity toward the receptor. The beta 2-receptor monomer has a molecular mass of 58-64,000 daltons. Target size analysis indicates that the beta 2-receptor exists as a dimer in lung membranes. The half life of the beta 2-receptor on cultured lung cells is on the order of 20-30 h. Glucocorticoids induce the synthesis of beta 2-receptors, resulting in a doubling of the membrane concentration of receptors in 24 h. Autoantibodies to beta 2-adrenergic receptors may play a role in beta 2-receptor associated human diseases including asthma. Autoantibodies to beta 2-receptors in humans are associated with decreased sensitivity of beta 2-receptor functions and increased responsiveness of alpha-adrenergic and muscarinic cholinergic receptors.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 2998518 [PubMed - indexed for MEDLINE]
 

Navigate through the articles
Previous article Adrenergic Receptor Expression Adrenergic Receptor Function Next article
Copyright © 2007-2008 by Biologicalworld.com