Herrera L, Carvallo P, Antonelli M, Olate J
Departamento de Fisiopatología, Facultad Ciencias Biológicas, Universidad de Concepion, Chile.
FEBS Lett. 1994 Sep 26;352(2):175-9. doi: 10.1016/0014-5793(94)00957-0.
The Xenopus laevis oocyte has endogenous sites that bind muscarinic agonists, which have been pharmacologically characterized as M3 and/or M1 receptor subtypes. In order to define the molecular identify of the receptor protein we have analyzed a Xenopus oocyte cDNA library and cloned a 2.9 kb cDNA fragment encoding a muscarinic receptor (xMR). The deduced amino acid sequence reveals a protein of 484 residues with an apparent molecular weight of 54,188 Da. Amino acid comparison with previously cloned mammalian muscarinic receptors showed a 78% identity with the human m4 subtype, presenting at the same time clustered differences within the amino-terminal region and third intracellular loop Genomic Southern analysis displayed the presence of one main gene belonging to this subtype, and the PCR analysis revealed an intronless gene.