Abstract
Stimulation of taste receptors with sodium chloride, sodium acetate, sodium propionate, and the respective potassium salts gave concentration-response profiles, measured electrophysiologically, which are remarkably consistent with a two-state allosteric mechanism. The allosteric constant or equilibrium constant for the transition between the active and inactive receptor states is low, resulting in a condition in which small differences in ion affinities for the two states are sufficient to significantly alter the equilibrium. Receptor activators, such as sodium ion, displaced the equilibrium toward the active receptor state by virtue of a higher affinity for that state, whereas receptor inhibitors, such as acetate and propionate ions, displaced the equilibrium in the opposite direction as a result of a higher affinity for the inactive state. The low allosteric constant increased about 10-fold after treatment with the protein modification reagent dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide, resulting in a marked reduction in the response to sodium chloride and sodium propionate without a significant change in ion affinities. In order to fully resolve the potassium response characteristics, it was necessary to consider both a potassium activation site and a potassium inhibition site. Analysis of the response from sodium chloride/potassium chloride mixtures showed that sodium ion is competitive with potassium binding at the activation site but not the inhibition site. With potassium propionate as the stimulus, the effect of both a receptor activator and a receptor inhibitor was quantitatively consistent with depression of the response below a water baseline level at low stimulus concentrations. Estimation of active and inactive state dissociation constants for each anion and cation permitted accurate prediction of the response magnitude for a range of cation ratios in sodium chloride/potassium chloride mixtures and anion ratios in sodium chloride/sodium propionate mixtures. The association of salty taste with receptor activators and bitter taste with receptor inhibitors may be relevant to the generation of these taste qualities.
Keywords: chemoreception, gustation, membrane receptors, membrane transition
Full text
PDF




Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- BEIDLER L. M. A theory of taste stimulation. J Gen Physiol. 1954 Nov 20;38(2):133–139. doi: 10.1085/jgp.38.2.133. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Catterall W. A. Activation of the action potential Na+ ionophore by neurotoxins. An allosteric model. J Biol Chem. 1977 Dec 10;252(23):8669–8676. [PubMed] [Google Scholar]
- De Meyts P. Cooperative properties of hormone receptors in cell membranes. J Supramol Struct. 1976;4(2):241–258. doi: 10.1002/jss.400040211. [DOI] [PubMed] [Google Scholar]
- DeSimone J. A., Price S. A model for the stimulation of taste receptor cells by salt. Biophys J. 1976 Aug;16(8):869–881. doi: 10.1016/S0006-3495(76)85737-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Edelstein S. J. An allosteric mechanism for the acetylcholine receptor. Biochem Biophys Res Commun. 1972 Sep 5;48(5):1160–1165. doi: 10.1016/0006-291x(72)90832-7. [DOI] [PubMed] [Google Scholar]
- Halpern B. P., Tapper D. N. Taste stimuli: quality coding time. Science. 1971 Mar 26;171(3977):1256–1258. doi: 10.1126/science.171.3977.1256. [DOI] [PubMed] [Google Scholar]
- Krueger J. M., Cagan R. H. Biochemical studies of tast sensation. Binding of L-[3H]alanine to a sedimentable fraction from catfish barbel epithelium. J Biol Chem. 1976 Jan 10;251(1):88–97. [PubMed] [Google Scholar]
- Limbird L. E., Lefkowitz R. J. Negative cooperativity among beta-adrenergic receptors in frog erythrocyte membranes. J Biol Chem. 1976 Aug 25;251(16):5007–5014. [PubMed] [Google Scholar]
- MONOD J., WYMAN J., CHANGEUX J. P. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. J Mol Biol. 1965 May;12:88–118. doi: 10.1016/s0022-2836(65)80285-6. [DOI] [PubMed] [Google Scholar]
- Mooser G., Lambuth N. Inactivation of taste receptor cell function by two cationic protein modification reagents. J Neurobiol. 1977 May;8(3):193–206. doi: 10.1002/neu.480080303. [DOI] [PubMed] [Google Scholar]
- Mooser G. N-substituted maleimide inactivation of the response to taste cell stimulation. J Neurobiol. 1976 Sep;7(5):457–468. doi: 10.1002/neu.480070508. [DOI] [PubMed] [Google Scholar]
- Rubin M. M., Changeux J. P. On the nature of allosteric transitions: implications of non-exclusive ligand binding. J Mol Biol. 1966 Nov 14;21(2):265–274. doi: 10.1016/0022-2836(66)90097-0. [DOI] [PubMed] [Google Scholar]
- Sato T. Does an initial phasic response exist in the receptor potential of taste cells? Experientia. 1976 Nov 15;32(11):1426–1428. doi: 10.1007/BF01937414. [DOI] [PubMed] [Google Scholar]
