Document Detail


Beta-adrenergic receptors: structure, function and regulation.
MedLine Citation:
PMID:  1974837     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The diverse effects of the catecholamines (CA) epinephine and norepinephrine are mediated by a family of specific receptors (adrenergic receptors, AR). The beta-AR is a glycoprotein present in the membrane of a number of cell types. This receptor is closely associated with at least two other proteins (Gs and adenylate cyclase enzyme, AC) to form the beta-AR complex. The beta-AR recognizes the CA and is coupled to Gs which stimulates the effector enzyme AC. This enzyme converts ATP to cAMP and is the effector of the beta-AR complex. Thus the beta-AR is a G-coupled receptor which acts by raising intracellular levels of cAMP. The beta-AR is an important site of regulatory modifications through a variety of mechanisms. The best characterized is known as homologous desensitization: when the receptor is exposed to repeated stimulus by the agonist (CA), its responsiveness wanes, probably to compensate this potentially dangerous overstimulation. The gene for mammalian beta2-AR has been recently cloned and the predicted amino-acid sequence now opens the field to identification of the protein structures involved in receptor functions. The beta2-AR protein is characterized by the presence of seven membrane spanning regions. Study of the structure, function and regulation of the beta-AR will extend our knowledge of the role of beta-AR in pathological conditions and suggest new therapeutic approaches.
Authors:
A De Blasi
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  Drugs under experimental and clinical research     Volume:  16     ISSN:  0378-6501     ISO Abbreviation:  Drugs Exp Clin Res     Publication Date:  1990  
Date Detail:
Created Date:  1990-09-27     Completed Date:  1990-09-27     Revised Date:  2005-11-16    
Medline Journal Info:
Nlm Unique ID:  7802135     Medline TA:  Drugs Exp Clin Res     Country:  SWITZERLAND    
Other Details:
Languages:  eng     Pagination:  107-12     Citation Subset:  IM    
Affiliation:
Mario Negri Istituto di Ricerche Farmacologiche, Corsorzio Mario Negri Sud, Chieti, Italy.
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MeSH Terms
Descriptor/Qualifier:
Adrenergic beta-Agonists / pharmacology
Adrenergic beta-Antagonists / pharmacology
Animals
Humans
Receptors, Adrenergic, beta / drug effects,  physiology*
Chemical
Reg. No./Substance:
0/Adrenergic beta-Agonists; 0/Adrenergic beta-Antagonists; 0/Receptors, Adrenergic, beta

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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