Chemical Senses

This Article Abstract FREE Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Add to My Personal Archive Download to citation manager Request Permissions Disclaimer Google Scholar Articles by Miyoshi, M. A. Articles by Emori, Y. Search for Related Content PubMed PubMed Citation Articles by Miyoshi, M. A. Articles by Emori, Y. Social Bookmarking          What's this?

Chem. Senses 26: 259-265, 2001
© Oxford University Press 2001

IP₃ receptor type 3 and PLCß2 are co-expressed with taste receptors T1R and T2R in rat taste bud cells

Misaki Asano Miyoshi^1,2,3, Keiko Abe² and Yasufumi Emori³

¹ Bio-oriented Technology Research Advancement Institution, 1-40-2 Nisshin-cho, Oomiya, Saitama 331-0044, ² Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657 and ³ Department of Biophysics and Biochemistry, Faculty of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan

Correspondence to be sent to: Misaki Asano-Miyoshi, c/o Dr Emori, Department of Biophysics and Biochemistry, Faculty of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan. e-mail: amiyoshi{at}mail.ecc.u-tokyo.ac.jp

	Abstract

Top Abstract Introduction Materials and methods Results Discussion References

 
The Ca²⁺ signaling cascade has been reported to be activated by many tastants in vertebrate taste systems. Recently we have shown that G_i2 and phospholipase Cß2 (PLCß2) are co-expressed in a subset of taste bud cells and are possibly involved in Ca²⁺ triggering of taste signaling in rats. We report here that, as a component downstream of PLCß2, the type 3 isoform of the inositol 1,4,5-trisphosphate (IP₃) receptor (IP₃R3) is specifically expressed in the same cells as PLCß2 in rat taste buds. We also show that cells expressing rT2R9, a probable cycloheximide receptor, are included among PLCß2- and IP₃R3-positive cells, as in the case of rT1R2, a different type of taste receptor. Our findings indicate that PLCß2 and IP₃R3 co-localize together with G_i2 as downstream components of two different types of taste receptors, T1R and T2R, in taste bud cells.

	Introduction

Top Abstract Introduction Materials and methods Results Discussion References

 
In the taste buds of vertebrates the Ca²⁺ signaling cascade of PLC followed by inositol 1,4,5-trisphosphate (IP₃)-dependent Ca²⁺ release from intracellular stores has been reported to be activated by various tastants, including many bitter tastants (Akabas et al., 1988; Hwang et al., 1990; Spielman et al., 1994; Ogura et al., 1997), some non-sugar sweeteners (Bernhardt et al., 1996) and several amino acids (Bryant and Leftheris, 1991). In our most recent report (Asano-Miyoshi et al., 2000) we showed that a subset of taste bud cells contain a taste transduction pathway comprising rT1R2 as a G protein-coupled receptor, G_i2 as a G protein and PLCß2, although the ligand of rT1R2 is unknown.

Recently another type of G protein-coupled receptor, T2R, was isolated and shown to be specifically expressed in a subset of taste bud cells (Alder et al., 2000; Matsunami et al., 2000) independent of T1R2-expressing cells. It was shown that cells expressing T2Rs are gustducin-positive cells (Alder et al., 2000) and that one type of T2R, mouse mT2R5, responds to a bitter tastant, cycloheximide, and induces an increase in intracellular Ca²⁺ concentration in a heterologous expression system with G₁₅ (Chandrashekar et al., 2000). However, the native signaling pathway downstream of these receptors is not yet known.

On the other hand, the inositol 1,4,5-trisphosphate receptor (IP₃R) is a ligand-gated ion channel that releases Ca²⁺ from internal stores and directly causes an increase in intracellular Ca²⁺ concentration as one of the components downstream of PLC. Three subtypes of IP₃R, IP₃R1–IP₃R3, have been identified and each shows a distinct tissue distribution (Newton et al., 1994), but it not known which types of IP₃R are expressed in taste tissues.

In this study we have identified a type of IP₃ receptor, IP₃R3, a probable component downstream of PLCß2, in rat taste bud cells. In addition, we examined the correlation between the expression of calcium signaling components such as PLCß2 and IP₃R3 and that of two different types of taste receptors in taste bud cells.

	Materials and methods

Top Abstract Introduction Materials and methods Results Discussion References

 
RNA preparation and reverse transcription–PCR (RT–PCR)

The poly(A)⁺ RNA of the circumvallate and foliate papillae containing many taste buds was isolated as described previously (Asano-Miyoshi et al., 1998). The cDNA fragments encoding rat IP₃Rs were amplified using the poly(A)⁺ RNA and degenerate primers:

and

corresponding to the amino acids sequences EYCQGPCHENQ and EHNMWHYLCF, respectively, conserved among the three types of rat IP₃Rs. Each cDNA fragment was subcloned into the pBluescript SK(–) vector, sequenced and subjected to further analyses.

In situ hybridization

RNA probes labeled with digoxigenin-UTP were synthesized with T3 or T7 RNA polymerase from the cDNA fragments encoding rat IP₃Rs obtained above, the full-length cDNA of rT1R2 (Hoon et al., 1999), a gift from Dr C.S. Zuker, and a partial cDNA corresponding to the open reading frame of rT2R9 (Alder et al., 2000), which was obtained by PCR using a rat genomic DNA as template (GenBank accession no. AF227146).

The circumvallate papillae of the tongue of a 5-week-old rat (Wistar) were excised and 4-µm-thick frozen sections were prepared to be used for in situ hybridization as described previously (Asano-Miyoshi et al., 2000; Yasuoka et al., 1999). In the double labeling analysis a signal amplification method using two tylamide fluorogenic substrates was adopted according to the method described previously (Asano-Miyoshi et al., 2000). Fluorescent images were obtained under a fluorescence microscope (Olympus BX60) using a MicroMax cooled CCD camera system (Nippon Roper) and analyzed with MetaMorph imaging software (Universal Imaging Corp.).

Immunohistochemistry

The circumvallate papillae of the tongue of a 5-week-old rat (Wistar) were excised, and 10 µm thick frozen sections were prepared in the same way as for in situ hybridization. The sections were post-fixed in 4% paraformaldehyde for 10 min. After washing three times in phosphate-buffered saline (PBS), the sections were blocked with 3% normal goat serum and 1% bovine serum albumin (BSA) in PBS for 1 h at room temperature. Then, the sections were incubated with a mixture of the primary antibodies, a monoclonal IP₃R3 antibody (Transduction Laboratories) and either a polyclonal PLCß2 antibody (Q-15) (Santa Cruz Biotechnology) or a polyclonal Ggust antibody (I-20) (Santa Cruz Biotechnology), each diluted 1:200 in 1% normal goat serum and 1% BSA at 4°C overnight. After washing three times in PBS, the sections were incubated in the secondary antibodies, Texas Red-labeled donkey anti-mouse IgG and FITC-labeled donkey anti-rabbit IgG (Jackson Immuno Research), each diluted 1:100 in 1% normal goat serum and 1% BSA at room temperature for 1 h. After washing three times in PBS, the sections were mounted with Gel/Mount (Biomeda). Fluorescent images were obtained as described above.

	Results

Top Abstract Introduction Materials and methods Results Discussion References

 
We first tried to identify IP₃R isoforms expressed in rat taste tissues by RT–PCR using the degenerate primers corresponding to the amino acid sequences conserved among the three types of rat IP₃Rs (see Materials and methods). As a result, two of types of IP₃R cDNA, IP₃R1 and IP₃R3 (GenBank accession nos A36579 and A46719), were obtained. Next, in situ hybridization experiments were performed with these IP₃R subtypes. The results clearly indicated that IP₃R3 is highly expressed in a subset of cells in all taste buds with a frequency similar to that of PLCß2 (Rosseler et al., 1998; Asano-Miyoshi et al., 2000) (Figure 1). No significant signals were observed when IP₃R1 was used as probe (data not shown).

View larger version (144K): [in this window] [in a new window]   Figure 1 Cellular localization of IP3R3 in taste buds. The result of an in situ hybridization experiment on rat circumvallate papillae with an antisense RNA probe for IP3R3 is shown. Bars represent 50 µm.

 
Next, we examined the correlation between expression of PLCß2 and IP₃R3 by in situ hybridization (Figure 2). The expression profiles of PLCß2 and IP₃R3 were compared in longitudinal (Figure 2a) and transverse (Figure 2b) serial sections of taste buds of the circumvallate papillae, where each cell would be divided into two or more adjacent sections. In this analysis when a certain cell expressed two genes, probes for the two genes should both give positive signals in the same cell divided between two serial sections (Asano-Miyoshi et al., 2000). As a result, it was revealed that PLCß2 and IP₃R3 are expressed in the same cells. We also carried out double labeling in situ hybridization experiments using digoxigenin- and FITC-labeled probes, which gave a clearer indication of the correlation (Figure 2c). The results of overlaid images of a single section were essentially the same as that obtained with the serial sections. It is thus revealed that a certain subtype of IP₃ receptor, IP₃R3, is expressed in the same cells that express PLCß2.

View larger version (143K): [in this window] [in a new window]   Figure 2 Co-expression of PLCß2 and IP3R3. In situ hybridization experiments on 4 µm thick longitudinal (a) and transverse (b) serial sections of rat circumvallate papillae with antisense RNA probes for PLCß2 and IP3R3 were performed. The serial sections in each panel are aligned along the arrow below the panel. The red arrowheads show cells positive to both probes. (c) The result of double label fluorescent in situ hybridization with PLCß2 (green) and IP3R3 (red). Cells positive for both probes show yellowish signals as a result of overlap of the green (FITC) and red (Cyanine 3) signals. Bars represent 10 µm.

 
To gain further insight into the molecular process of the taste transduction pathway, we next examined the correlations between these cells and cells expressing two types of taste receptors, including a recently identified T2R, rT2R9, a rat homolog of the mouse cycloheximide receptor (mT2R5) (Alder et al., 2000), in taste buds of rat circumvallate papillae (Figure 3).

View larger version (113K): [in this window] [in a new window]   Figure 3 Correlation between the expression of taste receptors and calcium signaling components. In situ hybridization experiments on 4 µm thick transverse serial sections of rat circumvallate papillae with antisense RNA probes for the taste receptors rT1R2 (a) or rT2R9 (b), PLCß2 and IP3R3 were performed. The serial sections in each panel are aligned along the arrow below the panel. The red arrowheads show the cells positive for both probes. (c–f) The results of double label fluorescent in situ hybridization with (c) PLCß2 (green) versus rT1R2 (red), (d) PLCß2 (green) versus rT2R9 (red), (e) IP3R3 (red) versus rT1R2 (green) and (f) IP3R3 (red) versus rT2R9 (green). Cells positive for both probes show yellowish signals as a result of overlap of the green (FITC) and red (Cyanine 3) signals. Bars represent 10 µm.

 
In order to examine the relationship between expression of taste receptors and calcium signaling components, we performed in situ hybridization experiments using 4 µm thick transverse serial sections of rat circumvallate papillae in the same way as described for Figure 2b. As shown in Figure 3a,b, all rT1R2- and rT2R9-positive cells expressed PLCß2 and IP₃R3. Next, we also carried out double labeling in situ hybridization experiments, which again revealed that all of the receptor-positive signals were in PLCß2- (Figure 3c,d) and IP₃R3-expressing (Figure 3e,f) cells. Consequently, the results suggest that both types of taste receptor can transduce the taste signal to activation of PLCß2, leading to activation of IP₃R3, and induce IP₃-dependent Ca²⁺ release from intracellular stores.

Finally, we examined the existence of PLCß2 and IP₃R3 proteins by double labeling immunofluorescense staining (Figure 4a–d). The results show the same correlation as those of the in situ hybridization experiments (Figure 2), i.e. cells expressing IP₃R3 protein and those expressing PLCß2 protein were identical. On the other hand, gustducin-positive cells were also IP₃R3 positive (Figure 4e–h).

View larger version (128K): [in this window] [in a new window]   Figure 4 Correlation of the expression of IP3R3, PLCß2 and gustducin proteins. Double labeling immunofluorescense stainings on 10 µm thick sections of rat circumvallate papillae with (a–d) anti-IP3R3 Ab (a) and anti-PLCß2 Ab (c); and (e–h) anti-IP3R3 Ab (e) and anti-gustducin Ab (g) were performed. Co-distributed signals for both proteins appear yellowish as a result of overlap of the green (FITC) and red (Texas Red) signals on each composite image (b, f). The bar on each transparent view (d, h) represents 10 µm.

 

	Discussion

Top Abstract Introduction Materials and methods Results Discussion References

 
Although many reports have described the physiological features of Ca²⁺ signaling cascades in vertebrate taste systems (Akabas, 1993; Lindemann, 1996), there is little information concerning the molecular components. Our in situ hybridization results show that in taste buds a certain subtype of IP₃R, IP₃R3, is highly expressed in the same subset of cells that express PLCß2 as one of two downstream signaling molecules generated by PLCß2, IP₃ and diacylglycerol. In addition, double labeling immunostaining showed that IP₃R3 protein and PLCß2 protein co-existed in the same cells, which included gustducin protein-containing cells, although further investigations are needed to determine their functional linkage in terms of subcellular localization, because it might be altered during experimental procedures, including fixation and permeabilization. These observations strongly suggest that these components mediate Ca²⁺ responses induced by various taste stimuli. It is thus confirmed that Ca²⁺ release from internal stores triggered by IP₃ has an important function in taste transduction.

IP₃R3 is a subtype that is expressed predominantly in gastrointestinal tissues, such as in the apical region of villous enterocytes in the jejunum and pancreatic acinar cells, as well as kidney, lung, testis and brain (Blondel et al., 1993). Its activation is considered to result in a single transient, but global, increase in the concentration of cytosolic Ca²⁺ (Hagar et al., 1998), as observed in isolated taste bud cells (Akabas et al., 1988; Spielman et al., 1994; Ogura et al., 1997). Thus, IP₃R3 is better suited to signal initiation in taste cells than other types of IP₃Rs, whose properties are ideal for Ca²⁺ oscillation.

The finding that both rT1R2- and rT2R9-positive cells express PLCß2 and IP₃R3 (Figure 3) suggests that taste stimuli received by these receptors probably induce the calcium response mediated by PLCß2 and IP₃R3. In our most recent report (Asano-Miyoshi et al., 2000) we found that PLCß2 and G_i2 are co-expressed in the same subset of cells and that gustducin-positive cells are also included in this subset. It is thus possible that the ß subunits of G_i2 are the general upstream components activating taste cell PLCß2 and that those of gustducin might also act in a limited subpopulation of PLCß2-positive cells. Since no correlation has been observed between expression of rT1R2 and gustducin (Hoon et al., 1999; Asano-Miyoshi et al., 2000), rT1R2 appears to transduce the taste signal of its unknown ligand through a pathway comprising G_i2(G_ß), PLCß2 and IP₃R3. On the other hand, T2R-positive cells have been reported to be included among gustducin-positive cells and the ß subunits (G_ß113) of gustducin have been shown to mediate IP₃ responses to a bitter tastant, denatonium (Huang et al., 1999). Therefore, cycloheximide, a ligand of rT2R9, probably causes the Ca²⁺ response in taste bud cells through a pathway comprising rT2R9, gustducin (G_ß113) and/or G_i2(G_ß), PLCß2 and IP₃R3.

In summary, a significant subset of taste bud cells have a Ca²⁺ signaling pathway involving PLCß2 and IP₃R3 and these cells are taste cells showing IP₃ responses to several of the tastants reported in previous physiological studies. In a subpopulation of Ca²⁺-signaling PLCß2- and IP₃R3-positive taste cells both types of taste receptors, T1R and T2R, might receive some specific taste stimulus, such as cycloheximide for rT2R9, and might transduce the signals through the Ca²⁺ signaling pathway. Identification of downstream components following Ca²⁺ release are needed, together with further physiological studies using native Ca²⁺ signaling components, taste receptors and their specific ligands.

	Acknowledgments

 
This study was supported by a grant from the Program of the Bio-oriented Technology Research Advancement Institution.

	References

Top Abstract Introduction Materials and methods Results Discussion References

 
Akabas, M.H. (1993) The molecular biology of chemotransduction. In Simon, A. and Roper, S.D. (eds), Mechanisms of Taste Transduction. CRC Press, Boca Raton, FL, pp. 175–200.

Akabas, M.H., Dodd, J. and Al-Awqati, Q. (1988) A bitter substance induces a rise in intracellular calcium in a subpopulation of rat taste cells. Science, 242, 1047–1050.[Abstract/Free Full Text]

Alder, E., Hoon, M.A., Mueller, K.L., Chandrashekar, J., Ryba, J.P. and Zuker, C.S. (2000) A novel family of mammalian taste receptors. Cell, 100, 693–702.[Web of Science][Medline]

Asano-Miyoshi, M., Kusakabe, Y., Abe, K. and Emori, Y. (1998) Identification of taste-tissue specific cDNA clones from a subtraction cDNA library of rat circumvallate and foliate papillae. J. Biochem., 124, 927–933.[Abstract/Free Full Text]

Asano-Miyoshi,M., Abe, K. and Emori, Y. (2000) Co-expression of calcium signaling components of vertebrate taste bud cells. Neurosci. Lett., 283, 61–64.[Web of Science][Medline]

Bernhardt, S.J., Naim, M., Zehavi, U. and Lindemann, B. (1996) Changes in IP₃ and cytosolic Ca²⁺ in response to sugars and nonsugar sweeteners in transduction of sweet taste in the rat. J. Physiol. Lond., 490, 325–336.[Abstract/Free Full Text]

Blondel, O., Takeda, J., Janssen, H., Seino, S. and Bell, G.I. (1993) Sequence and functional characterization of a third inositol trisphosphate receptor subtype, IP₃R-3, expressed in pancreatic islets, kidney, gastrointestinal tract, and other tissues. J. Biol. Chem., 268, 11356–11363.[Abstract/Free Full Text]

Bryant, B.P. and Leftheris, K. (1991) Structure/activity relationships in the L-alanine taste receptor system of channel catfish, Ictalurus punctatus. Physiol. Behav., 49, 891–898.[Medline]

Chandrashekar, J. Mueller, K.L., Hoon, M.A., Alder, E., Feng, L., Guo, W., Zuker, C.S. and Ryba, N.J. (2000) T2Rs function as bitter taste receptors. Cell, 100, 703–711.[Web of Science][Medline]

Hagar, R.E., Burgstahler, A.D., Nathanson, M.H. and Ehrlich, B.E. (1998) Type III InsP3 receptor channel stays open in the presence of increased calcium. Nature, 396, 81–84.[Medline]

Hoon, M.A., Adler, E., Lindemeier, J., Battey, J.F., Ryba, N.J. and Zucker, C.S. (1999) Putative mammalian taste receptors: a class of taste-specific GPCRs with distinct topographic selectivity. Cell, 96, 541–551.[Web of Science][Medline]

Huang, L., Shanker, Y.G., Dubauskaite, J., Zheng, J.Z., Yan, W., Rosenzweig, S., Spielman, A.I., Max, M. and Margolskee, R.F. (1999) G13 colocalizes with gustducin in taste receptor cells and mediates IP₃ responses to bitter denatonium. Nature Neurosci., 2, 1055–1062.[Web of Science][Medline]

Hwang, P.M., Verma, A., Bredt, D.S. and Snyder, S.H. (1990) Localization of phosphatidylinositol signalling components in rat taste cells: role in bitter taste transduction. Proc. Natl Acad. Sci. USA, 83, 7395–7399.

Lindemann, B. (1996) Taste reception. Physiol. Rev., 76, 719–766.[Abstract/Free Full Text]

Matsunami, H, Montmayeur, J.-P. and Buck, L.B. (2000) A family of candidate taste receptors in human and mouse. Nature, 404, 601–604.[Medline]

Newton, C.L., Mignery, G.A. and Südhof, T.C. (1994) Co-expression in vertebrate tissues and cell lines of multiple inositol 1,4,5-trisphosphate (InsP3) receptors with distinct affinities for InsP3. J. Biol. Chem., 269, 28613–28619.[Abstract/Free Full Text]

Ogura, T. Mackay-Sim, A. and Kinnamon, S.C. (1997) Bitter taste transduction of denatonium in the mudpuppy Nectrurus maculosus. J. Neurosci., 17, 3580–3587.[Abstract/Free Full Text]

Rossler, P., Kroner, C., Freitag, J., Noe, J. and Breer, H. (1998) Identification of phospholipase C beta subtype in rat taste cells. Eur. J. Cell Biol., 77, 253–261.[Web of Science][Medline]

Spielman, A.I., Huque, T., Nagai, H., Whitney, G. and Brand, J.G. (1994) Generation of inositol phosphates in bitter taste transduction. Physiol. Behav., 56, 1149–1155.[Medline]

Yasuoka, A., Endo, K., Asano-Miyoshi, M., Abe, K. and Emori, Y. (1999) Two subfamilies of olfactory receptor genes in medaka fish, Oryzias latipes: genomic organization and differential expression in olfactory epithelium. J. Biochem., 126, 866–873.[Abstract/Free Full Text]

Accepted November 1, 2000

CiteULike    Connotea    Del.icio.us    What's this?

This article has been cited by other articles:

				Y. Shindo, M.-R. Kim, H. Miura, T. Yuuki, T. Kanda, A. Hino, and Y. Kusakabe Lrmp/Jaw1 is Expressed in Sweet, Bitter, and Umami Receptor-Expressing Cells Chem Senses, February 1, 2010; 35(2): 171 - 177. [Abstract] [Full Text] [PDF]

				A. San Gabriel, T. Maekawa, H. Uneyama, and K. Torii Metabotropic glutamate receptor type 1 in taste tissue Am. J. Clinical Nutrition, September 1, 2009; 90(3): 743S - 746S. [Abstract] [Full Text] [PDF]

				S. C Kinnamon Umami taste transduction mechanisms Am. J. Clinical Nutrition, September 1, 2009; 90(3): 753S - 755S. [Abstract] [Full Text] [PDF]

				S. Thirumangalathu, D. E. Harlow, A. L. Driskell, R. F. Krimm, and L. A. Barlow Fate mapping of mammalian embryonic taste bud progenitors Development, May 1, 2009; 136(9): 1519 - 1528. [Abstract] [Full Text] [PDF]

				T. Ohkuri, K. Yasumatsu, N. Horio, M. Jyotaki, R. F. Margolskee, and Y. Ninomiya Multiple sweet receptors and transduction pathways revealed in knockout mice by temperature dependence and gurmarin sensitivity Am J Physiol Regulatory Integrative Comp Physiol, April 1, 2009; 296(4): R960 - R971. [Abstract] [Full Text] [PDF]

				Y. Ishimaru and H. Matsunami Transient Receptor Potential (TRP) Channels and Taste Sensation Journal of Dental Research, March 1, 2009; 88(3): 212 - 218. [Abstract] [Full Text] [PDF]

				K. Hacker, A. Laskowski, L. Feng, D. Restrepo, and K. Medler Evidence for Two Populations of Bitter Responsive Taste Cells in Mice J Neurophysiol, March 1, 2008; 99(3): 1503 - 1514. [Abstract] [Full Text] [PDF]

				S. Kataoka, R. Yang, Y. Ishimaru, H. Matsunami, J. Sevigny, J. C. Kinnamon, and T. E. Finger The Candidate Sour Taste Receptor, PKD2L1, Is Expressed by Type III Taste Cells in the Mouse Chem Senses, March 1, 2008; 33(3): 243 - 254. [Abstract] [Full Text] [PDF]

				C. Hisatsune, K. Yasumatsu, H. Takahashi-Iwanaga, N. Ogawa, Y. Kuroda, R. Yoshida, Y. Ninomiya, and K. Mikoshiba Abnormal Taste Perception in Mice Lacking the Type 3 Inositol 1,4,5-Trisphosphate Receptor J. Biol. Chem., December 21, 2007; 282(51): 37225 - 37231. [Abstract] [Full Text] [PDF]

				H. Miura, A. Nakayama, Y. Shindo, Y. Kusakabe, H. Tomonari, and S. Harada Expression of Gustducin Overlaps with That of Type III IP3 Receptor in Taste Buds of the Rat Soft Palate Chem Senses, September 1, 2007; 32(7): 689 - 696. [Abstract] [Full Text] [PDF]

				H. Oike, T. Nagai, A. Furuyama, S. Okada, Y. Aihara, Y. Ishimaru, T. Marui, I. Matsumoto, T. Misaka, and K. Abe Characterization of Ligands for Fish Taste Receptors J. Neurosci., May 23, 2007; 27(21): 5584 - 5592. [Abstract] [Full Text] [PDF]

				R. K. Palmer The Pharmacology and Signaling of Bitter, Sweet, and Umami Taste Sensing Mol. Interv., April 1, 2007; 7(2): 87 - 98. [Abstract] [Full Text] [PDF]

				M. Ohmoto, I. Matsumoto, T. Misaka, and K. Abe Taste Receptor Cells Express Voltage-Dependent Potassium Channels in a Cell Age-Specific Manner Chem Senses, October 1, 2006; 31(8): 739 - 746. [Abstract] [Full Text] [PDF]

				Y. Ishimaru, H. Inada, M. Kubota, H. Zhuang, M. Tominaga, and H. Matsunami Transient receptor potential family members PKD1L3 and PKD2L1 form a candidate sour taste receptor PNAS, August 15, 2006; 103(33): 12569 - 12574. [Abstract] [Full Text] [PDF]

				R. A. DeFazio, G. Dvoryanchikov, Y. Maruyama, J. W. Kim, E. Pereira, S. D. Roper, and N. Chaudhari Separate Populations of Receptor Cells and Presynaptic Cells in Mouse Taste Buds J. Neurosci., April 12, 2006; 26(15): 3971 - 3980. [Abstract] [Full Text] [PDF]

				J. W. Kim, C. Roberts, Y. Maruyama, S. Berg, S. Roper, and N. Chaudhari Faithful Expression of GFP from the PLC{beta}2 Promoter in a Functional Class of Taste Receptor Cells Chem Senses, March 1, 2006; 31(3): 213 - 219. [Abstract] [Full Text] [PDF]

				C. D. Dotson, S. D. Roper, and A. C. Spector PLC{beta}2-Independent Behavioral Avoidance of Prototypical Bitter-Tasting Ligands Chem Senses, September 1, 2005; 30(7): 593 - 600. [Abstract] [Full Text] [PDF]

				T. E. Finger Cell Types and Lineages in Taste Buds Chem Senses, January 1, 2005; 30(suppl_1): i54 - i55. [Full Text] [PDF]

				R. F. Margolskee Molecular Mechanisms of Bitter and Sweet Taste Transduction J. Biol. Chem., January 4, 2002; 277(1): 1 - 4. [Full Text]

This Article Abstract FREE Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Add to My Personal Archive Download to citation manager Request Permissions Disclaimer Google Scholar Articles by Miyoshi, M. A. Articles by Emori, Y. Search for Related Content PubMed PubMed Citation Articles by Miyoshi, M. A. Articles by Emori, Y. Social Bookmarking          What's this?

Online ISSN 1464-3553 - Print ISSN 0379-864X

Copyright © 2010 Oxford University Press

Oxford Journals Oxford University Press

• Site Map
• Privacy Policy
• Frequently Asked Questions

Other Oxford University Press sites: Oxford University Press Oxford Journals China Oxford Journals Japan American National Biography Booksellers' Information Service Children's Fiction and Poetry Children's Reference Corporate & Special Sales Dictionaries Dictionary of National Biography Digital Reference English Language Teaching Higher Education Textbooks Humanities International Education Unit Law Medicine Music Online Products Oxford English Dictionary Reference Rights and Permissions Science School Books Social Sciences Very Short Introductions World's Classics