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2-dependent rise in
IP3 and 
-gustducin-dependent fall in cyclic
nucleotides
1 Department of Basic Science and Craniofacial Biology, Division of Biological Science, Medicine, and Surgery, New York University College of Dentistry, New York, New York 10010; 2 Monell Chemical Senses Center, Philadelphia 19104-3308; and 3 Philadelphia Veterans Affairs Medical Center, and University of Pennsylvania, Philadelphia, Pennsylvania 19104
Current evidence points to the existence of multiple processes
for bitter taste transduction. Previous work demonstrated involvement of the polyphosphoinositide system and an 
-gustducin
(Ggust)-mediated stimulation of phosphodiesterase in
bitter taste transduction. Additionally, a taste-enriched G protein
-subunit, G13, colocalizes with Ggust
and mediates the denatonium-stimulated production of inositol
1,4,5-trisphosphate (IP3). Using quench-flow techniques, we
show here that the bitter stimuli, denatonium and strychnine, induce
rapid (50-100 ms) and transient reductions in cAMP and cGMP and
increases in IP3 in murine taste tissue. This decrease of
cyclic nucleotides is inhibited by Ggust antibodies,
whereas the increase in IP3 is not affected by antibodies
to Ggust. IP3 production is inhibited by
antibodies specific to phospholipase C-
2
(PLC-2), a PLC isoform known to be activated by
G-subunits. Antibodies to PLC-3 or to
PLC-4 were without effect. These data suggest a
transduction mechanism for bitter taste involving the rapid and
transient metabolism of dual second messenger systems, both mediated
through a taste cell G protein, likely composed of
Ggust//13, with both systems being
simultaneously activated in the same bitter-sensitive taste receptor cell.
taste transduction; denatonium; second messenger; rapid kinetics; taste receptors; inositol 1,4,5-trisphosphate; phospholipase C
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