Taste receptor cells are primary sensory receptors utilized by the nervous system to detect the presence of gustatory stimuli in the oral cavity. These cells are particularly heterogeneous and may be divided into various subtypes based on morphological, histochemical, or physiological criteria. One example is the heterogeneous expression of neuropeptides, such as cholecystokinin and vasoactive intestinal polypeptide. These peptides are hypothesized to participate in the transduction processes. To pursue examination of this hypothesis, this study explored the relationship of peptide expression with two important and mostly non-overlapping transductive elements--the taste-specific G protein gustducin, involved in bitter and sweet transduction cascades, and the seven transmembrane taste receptor T1R2, hypothesized to respond to sweet compounds. Double labeling experiments were performed on taste buds of the posterior rat tongue combining immunocytochemistry for peptide expression and in situ hybridization experiments for either gustducin or T1R2 expression. Additionally, vasoactive intestinal peptide (VIP)-expression in posterior taste receptor cells was confirmed using the technique of RT-PCR. More than half (56%) of the CCK-expressing taste receptor cells co-expressed alpha-gustducin mRNA whereas far fewer (15%) co-expressed T1R2 mRNA. A majority of VIP-expressing taste receptor cells co-expressed alpha-gustducin mRNA (60%) whereas only 19% of these cells co-expressed T1R2 mRNA. More remarkable was the observation that these two peptides displayed almost identical expression patterns with these signal transduction molecules, suggesting that peptides are not randomly expressed with relation to signal transduction molecules. This observation supports the hypothesis that peptides may play roles in transduction. Further physiological exploration will be required to elucidate the nature of these roles.