Article: article from journal or magazin.
Antagonism of catecholamine receptor signaling by expression of cytoplasmic domains of the receptors.
The actions of many hormones and neurotransmitters are mediated by the members of a superfamily of receptors coupled to heterotrimeric guanine nucleotide-binding proteins (G proteins). These receptors are characterized by a highly conserved topographical arrangement in which seven transmembrane domains are connected by intracellular and extracellular loops. The interaction between these receptors and G proteins is mediated in large part by the third intracellular loop of the receptor. Coexpression of the third intracellular loop of the alpha 1B-adrenergic receptor with its parent receptor inhibited receptor-mediated activation of phospholipase C. The inhibition extended to the closely related alpha 1C-adrenergic receptor subtype, but not the phospholipase C-coupled M1 muscarinic acetylcholine receptor nor the adenylate cyclase-coupled D1A dopamine receptor. These results suggest that the receptor-G protein interface may represent a target for receptor antagonist drugs.
Amino Acid Sequence, Base Sequence, Cell Line, Cloning, Molecular, Cyclic AMP/metabolism, Cytoplasm/metabolism, GTP-Binding Proteins/metabolism, Globins/genetics, Glutathione Transferase/genetics, Glutathione Transferase/metabolism, Humans, Inositol Phosphates/metabolism, Kinetics, Molecular Sequence Data, Muscarinic Antagonists, Oligodeoxyribonucleotides, Plasmids, Protein Structure, Secondary, Receptors, Adrenergic, alpha/genetics, Receptors, Adrenergic, alpha/metabolism, Receptors, Dopamine D1/antagonists & inhibitors, Receptors, Dopamine D1/genetics, Receptors, Muscarinic/genetics, Receptors, Muscarinic/metabolism, Recombinant Fusion Proteins/metabolism, Signal Transduction, Transfection, Type C Phospholipases/metabolism
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