G-protein-dependent and -independent pathways in denatonium signal transduction

To clarify the involvement of G protein in denatonium signal transduction, we carried out a whole-cell patch-clamp analysis with isolated taste cells in mice. Two different responses were observed by applying GDP-beta-S, a G-protein inhibitor. One response to denatonium was reduced by GDP-beta-S (G-...

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Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2005, Vol.69 (9), p.1643-1651
Main Authors: Sawano, S.(Kyoto Univ. (Japan)), Seto, E, Mori, T, Hayashi, Y
Format: Article
Language:English
Subjects:
AMARGO
AMERTUME
ANALISIS ORGANOLEPTICO
ANALYSE ORGANOLEPTIQUE
Animals
BINDING PROTEINS
Biological and medical sciences
bitter
BITTERNESS
Calcium - metabolism
Cell Separation
denatonium signal transduction
Female
Fundamental and applied biological sciences. Psychology
GTP-Binding Proteins - physiology
GUSTO (SENTIDO)
Isoenzymes - metabolism
Membrane Potentials - drug effects
Membrane Potentials - physiology
MICE
Mice, Inbred C57BL
mouse
ORGANOLEPTIC ANALYSIS
patch-clamp
Patch-Clamp Techniques
Phospholipase C beta
Phosphoric Diester Hydrolases - metabolism
PROTEINAS AGLUTINANTES
PROTEINE DE LIAISON
Quaternary Ammonium Compounds - pharmacology
RATON
SENS DU GOUT
Signal Transduction - drug effects
Signal Transduction - physiology
SOURIS
Taste
TASTE (SENSATION)
Taste Buds - cytology
Taste Buds - drug effects
Taste Buds - physiology
Type C Phospholipases - metabolism
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Summary:To clarify the involvement of G protein in denatonium signal transduction, we carried out a whole-cell patch-clamp analysis with isolated taste cells in mice. Two different responses were observed by applying GDP-beta-S, a G-protein inhibitor. One response to denatonium was reduced by GDP-beta-S (G-protein-dependent), whereas the other was not affected (G-protein-independent). These different patterns were also observed by concurrently inhibiting the phospholipase C beta 2 and phosphodiesterase pathways via G protein. These data suggest dual, G-protein-dependent and -independent mechanisms for denatonium. Moreover, the denatonium responses were not attenuated by singly inhibiting the phospholipase C beta 2 or phosphodiesterase pathway, implying that both pathways were involved in G-protein-dependent transduction. In the G-protein-independent cells, the response was abolished by the depletion of calcium ions within the intracellular store. These results suggest that Ca(2+) release from the intracellular store is an important factor. Our data demonstrate multiple transduction pathways for denatonium in mammalian taste cells.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.69.1643