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The human and rat genes for a fifth muscarinic receptor have been cloned and expressed in mammalian cells. The 532 amino acid human protein has 89% sequence identity to the 531 amino acid rat protein and is most closely related to the m3 receptor. Both proteins are encoded by single exons. The receptor has intermediate affinity for pirenzepine and low affinity for AF-DX 116, and it increases metabolism of phosphatidylinositol when stimulated with carbachol. Expression of mRNA has yet to be observed in brain or selected peripheral tissues, suggesting that either it is substantially less abundant than m1-m4 or its distribution is quite different.

Type

Journal article

Journal

Neuron

Publication Date

07/1988

Volume

1

Pages

403 - 410

Keywords

Amino Acid Sequence, Animals, Base Sequence, Binding, Competitive, Cell Line, Cloning, Molecular, Gene Expression, Genetic Vectors, Humans, Inositol Phosphates, Kinetics, Molecular Sequence Data, Parasympatholytics, Pirenzepine, Rats, Receptors, Muscarinic, Restriction Mapping, Sequence Homology, Nucleic Acid, Transfection