Muscarinic acetylcholine receptor subtypes: localization and structure/function

TY - JOUR

T1 - Muscarinic acetylcholine receptor subtypes: localization and structure/function

AU - Brann, M R

AU - Ellis, J

AU - Jørgensen, H

AU - Hill-Eubanks, D

AU - Jones, S V

AU - Bräuner-Osborne, Hans

PY - 1993

Y1 - 1993

N2 - Based on the sequence of the five cloned muscarinic receptor subtypes (m1-m5), subtype selective antibody and cDNA probes have been prepared. Use of these probes has demonstrated that each of the five subtypes has a markedly distinct distribution within the brain and among peripheral tissues. The distributions of these subtypes and their potential physiological roles are discussed. By use of molecular genetic manipulation of cloned muscarinic receptor cDNAs, the regions of muscarinic receptors that specify G-protein coupling and ligand binding have been defined in several recent studies. Overall, these studies have shown that amino acids within the third cytoplasmic loop of the receptors define their selectivities for different G-proteins and that multiple discontinuous epitopes contribute to their selectivities for different ligands. The residues that contribute to ligand binding and G-protein coupling are described, as well as the implied structures of these functional domains.

AB - Based on the sequence of the five cloned muscarinic receptor subtypes (m1-m5), subtype selective antibody and cDNA probes have been prepared. Use of these probes has demonstrated that each of the five subtypes has a markedly distinct distribution within the brain and among peripheral tissues. The distributions of these subtypes and their potential physiological roles are discussed. By use of molecular genetic manipulation of cloned muscarinic receptor cDNAs, the regions of muscarinic receptors that specify G-protein coupling and ligand binding have been defined in several recent studies. Overall, these studies have shown that amino acids within the third cytoplasmic loop of the receptors define their selectivities for different G-proteins and that multiple discontinuous epitopes contribute to their selectivities for different ligands. The residues that contribute to ligand binding and G-protein coupling are described, as well as the implied structures of these functional domains.

KW - Animals

KW - Binding Sites

KW - Brain Chemistry

KW - GTP-Binding Proteins

KW - Humans

KW - Ligands

KW - Muscle Proteins

KW - Muscle, Smooth

KW - Myocardium

KW - Nerve Tissue Proteins

KW - Organ Specificity

KW - Receptors, Muscarinic

M3 - Journal article

C2 - 8248499

SN - 0079-6123

VL - 98

SP - 121

EP - 127

JO - Progress in Brain Research

JF - Progress in Brain Research

ER -