Chem. Senses 25: 413-421,
2000
© Oxford University Press 2000
G Protein ß
Complexes in Circumvallate Taste Cells Involved in Bitter Transduction
University Stuttgart-Hohenheim, Institute of Physiology, D-70593 Stuttgart, Germany and 1 Unilever Research Vlaardingen, P.O.B. 114, 3130 AC Vlaardingen, The Netherlands
Correspondence to be sent to: Joachim Freitag, University Stuttgart-Hohenheim, Institute of Physiology, Garbenstrasse 30, D-70593 Stuttgart, Germany. e-mail: freitag{at}uni-hohenheim.de
G protein ß
(Gß) complexes are considered to play an important role in second messenger signaling of phospholipase C (PLC). Monitoring the inositol 1,4,5-trisphosphate (IP3) response in circumvallate tissue homogenates upon stimulation with denatonium benzoate, it was demonstrated that a glutathione S-transferase–GRK3ct fusion protein—a Gß scavenger—attenuates the bitter tastant-induced second messenger reaction. Towards an identification of the Gß complex involved in rat bitter taste transduction, it was found that the G protein ß3 subtype is specifically expressed in taste receptor cells of circumvallate papillae. Gß3-specific antibodies blocked the denatonium benzoate-induced IP3 formation in a dose-dependent manner; the inhibitory effect was reversed by preincubation with the antigenic peptide. A less pronounced inhibition was observed using Gß1-specific antibodies. Analyzing individual taste cells by single cell reverse transcriptase–polymerase chain reaction approaches, overlapping expression patterns for PLCß2, G
gust, Gß3 and G3 could be demonstrated. Furthermore, the co-expression of all profiled signal transduction components in individual taste receptor cells could be detected. These data support the concept that the denatonium benzoate-induced IP3 response is mediated by an activation of PLCß2 via a Gß complex, possibly composed of Gß3 as the predominant ß subunit and G3, and imply that multiple second messenger pathways may exist in individual taste receptor cells.
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