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J Neurophysiol (March 1, 2003). 10.1152/jn.0994.2002
Submitted on Submitted 31 October 2002; accepted in final form 18 November 2002
Department of Biomedical Sciences, Colorado State University, Fort Collins, 80523; and the Rocky Mountain Taste and Smell Center, University of Colorado Health Sciences Center, Denver, Colorado 80262
Lin, Weihong,
Tatsuya Ogura, and
Sue C. Kinnamon.
Responses to Di-Sodium Guanosine 5'-Monophosphate and Monosodium
L-Glutamate in Taste Receptor Cells of Rat Fungiform
Papillae. J. Neurophysiol. 89: 1434-1439, 2003. The 5'-ribonucleotide guanosine
5'-monophosphate (GMP) is used widely as an umami taste stimulus and a
potent flavor enhancer as it synergistically increases the umami taste
elicited by monosodium glutamate. Transduction mechanisms for GMP and
its synergy with glutamate are largely unknown. Using whole-cell
patch-clamp and Ca2+ imaging, we examined
responses to GMP, glutamate, and a mixture of GMP and glutamate in
taste-receptor cells of rat fungiform papillae. Our
electrophysiological results showed that GMP induces responses that are
similar to those of glutamate, e.g., an outward current, an inward
current, or a biphasic response. Our Ca2+ imaging
results showed that applications of GMP, glutamate, and the mixture
increased intracellular Ca2+ levels.
Interestingly, both patch-clamp and Ca2+ imaging
showed that some taste cells can respond to GMP and glutamate independently, indicating that glutamate and GMP likely activate different receptors. Simultaneous application of GMP and glutamate resulted in synergistic responses in a subset of cells; both response intensity and number of responding cells were increased. Most responses
to GMP, as well as the synergy between GMP and glutamate, were
suppressed by 8bromo-adenosine 3',5'-cyclic monophosphate (8-bromo-cAMP) in patch-clamp recordings. Together, our results suggest
that intracellular cAMP- and Ca2+-mediated
pathways are involved in umami taste transduction for GMP and its
synergistic responses with glutamate.
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