The diverse effects of the catecholamines (CA), epinephrine 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, guanine nucleotide stimulating protein (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 stimuli by the agonist (CA), its responsiveness wanes, probably to compensate this potentially dangerous overstimulation. The gene for mammalian beta 2-AR has recently been cloned and the predicted amino acid sequence now opens the field to identification of the protein structures involved in receptor functions. The beta 2-AR protein is characterized by the presence of seven membrane spanning regions. The 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.

Advances on beta-adrenergic receptors. Molecular structure and functional regulation / DE BLASI, Antonio. - In: AMERICAN JOURNAL OF HYPERTENSION. - ISSN 0895-7061. - STAMPA. - 2:(1989), pp. 252S-256S.

Advances on beta-adrenergic receptors. Molecular structure and functional regulation.

DE BLASI, ANTONIO
1989

Abstract

The diverse effects of the catecholamines (CA), epinephrine 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, guanine nucleotide stimulating protein (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 stimuli by the agonist (CA), its responsiveness wanes, probably to compensate this potentially dangerous overstimulation. The gene for mammalian beta 2-AR has recently been cloned and the predicted amino acid sequence now opens the field to identification of the protein structures involved in receptor functions. The beta 2-AR protein is characterized by the presence of seven membrane spanning regions. The 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.
1989
01 Pubblicazione su rivista::01a Articolo in rivista
Advances on beta-adrenergic receptors. Molecular structure and functional regulation / DE BLASI, Antonio. - In: AMERICAN JOURNAL OF HYPERTENSION. - ISSN 0895-7061. - STAMPA. - 2:(1989), pp. 252S-256S.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/453531
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