PMID: 2110418Apr 1, 1990Paper

Ligand binding and G protein coupling of muscarinic receptors in airway smooth muscle

The American Journal of Physiology
P A LucchesiT W Honeyman

Abstract

Ligand binding properties of muscarinic receptors were examined in membranes and isolated cells prepared from bovine trachea. The binding of the muscarinic antagonist [3H]quinuclidinyl benzilate (QNB) to both membranes and isolated cells was saturable, reversible, and of high affinity [dissociation constant (KD) = 100-200 pM]. The binding constants of three selective antagonists, pirenzepine, AF-DX 116, and 4-DAMP, were examined, and the results indicate that the smooth muscle cells contain at least two receptor subtypes. The majority of receptors exhibit binding constants for these selective antagonists similar to those of the M2-subtype. AF-DX 116 binding curves indicated the presence of a small population of receptors with binding constants similar to those reported for the M3-subtype. These findings suggest that the smooth muscle cells may contain both M2- and M3-receptors and are in agreement with evidence of the presence of mRNAs coding for these two subtypes in tracheal extracts (A. Maeda, T. Kubo, M. Mishina, and S. Numa. FEBS Lett. 239: 339-342, 1988). [3H]QNB displacement curves of the muscarinic agonist oxotremorine were best described as a sum of binding to high- and low-affinity sites with KD values of 3.8 nM and 2...Continue Reading

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Jan 1, 1992·Veterinary Research Communications·M YuF J Derksen
Aug 1, 1996·Clinical and Experimental Pharmacology & Physiology·D AmoakoJ P Bourreau
Oct 1, 1998·The American Journal of Physiology·T L CroxtonC A Hirshman
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