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Am J Physiol Cell Physiol 280: C884-C896, 2001;
0363-6143/01 $5.00
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Vol. 280, Issue 4, C884-C896, April 2001

G protein coupling to M1 and M3 muscarinic receptors in sublingual glands

W. Luo, L. R. Latchney, and D. J. Culp

Center for Oral Biology and the Department of Pharmacology and Physiology, University of Rochester Medical Center, Rochester, New York 14642

Rat sublingual gland M1 and M3 muscarinic receptors each directly activate exocrine secretion. To investigate the functional role of coreceptor expression, we determined receptor-G protein coupling. Although membrane proteins of 40 and 41 kDa are ADP-ribosylated by pertussis toxin (PTX), and 44 kDa proteins by cholera toxin (CTX), both carbachol-stimulated high-affinity GTPase activity and the GTP-induced shift in agonist binding are insensitive to CTX or PTX. Carbachol enhances photoaffinity labeling ([alpha -32P]GTP-azidoaniline) of only 42-kDa proteins that are subsequently tractable to immunoprecipitation by antibodies specific for Galpha q or Galpha 11 but not Galpha 12 or Galpha 13. Carbachol-stimulated photoaffinity labeling as well as phosphatidylinositol 4,5-bisphosphate (PIP2) hydrolysis is reduced 55% and 60%, respectively, by M1 receptor blockade with m1-toxin. Galpha q/11-specific antibody blocks carbachol-stimulated PIP2 hydrolysis. We also provide estimates of the molar ratios of receptors to Galpha q and Galpha 11. Although simultaneous activation of M1 and M3 receptors is required for a maximal response, both receptor subtypes are coupled to Galpha q and Galpha 11 to stimulate exocrine secretion via redundant mechanisms.

salivary glands; muscarinic cholinergic receptors; mucous cells; m1-toxin; Galpha q/11; exocrine secretion


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