Calcium signaling in taste cells

Medler, Kathryn F.

doi:10.1016/j.bbamcr.2014.11.013

Cited by 15 publications

(9 citation statements)

References 48 publications

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“…Evaluation of saT1Rs pharmacological responses to L-AAs and sweet ligands was conducted by systematic transient transfections of the heterodimers saT1R1 / R3 , saT1R2a / R3 or saT1R2b / R3 in HEK293 cells lines stably expressing pGL3- NFAT -luc reporter construct for intracellular Ca 2+ / NFAT signaling detection. The basic principle in the use of NFAT luciferase constructs for quantification of saT1R responses lies in the role of Ca 2+ as major secondary messenger in both taste transduction [ 52 , 53 , 54 ] and NFAT -mediated immune responses [ 55 ]. NFAT proteins reside ubiquitously in the cytosol in their inactive phosphorylated state [ 56 ].…”

Section: Discussionmentioning

confidence: 99%

Insights into the Function and Evolution of Taste 1 Receptor Gene Family in the Carnivore Fish Gilthead Seabream (Sparus aurata)

Angotzi

Puchol

Cerdá‐Reverter

et al. 2020

IJMS

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A plethora of molecular and functional studies in tetrapods has led to the discovery of multiple taste 1 receptor (T1R) genes encoding G-protein coupled receptors (GPCRs) responsible for sweet (T1R2 + T1R3) and umami (T1R1 + T1R3) taste. In fish, the T1R gene family repertoires greatly expanded because of several T1R2 gene duplications, and recent studies have shown T1R2 functional divergence from canonical mammalian sweet taste perceptions, putatively as an adaptive mechanism to develop distinct feeding strategies in highly diverse aquatic habitats. We addressed this question in the carnivore fish gilthead seabream (Sparus aurata), a model species of aquaculture interest, and found that the saT1R gene repertoire consists of eight members including saT1R1, saT1R3 and six saT1R2a-f gene duplicates, adding further evidence to the evolutionary complexity of fishT1Rs families. To analyze saT1R taste functions, we first developed a stable gene reporter system based on Ca2+-dependent calcineurin/NFAT signaling to examine specifically in vitro the responses of a subset of saT1R heterodimers to L-amino acids (L-AAs) and sweet ligands. We show that although differentially tuned in sensitivity and magnitude of responses, saT1R1/R3, saT1R2a/R3 and saT1R2b/R3 may equally serve to transduce amino acid taste sensations. Furthermore, we present preliminary information on the potential involvement of the Gi protein alpha subunits saGαi1 and saGαi2 in taste signal transduction.

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Section: Discussionmentioning

confidence: 99%

Insights into the Function and Evolution of Taste 1 Receptor Gene Family in the Carnivore Fish Gilthead Seabream (Sparus aurata)

Angotzi

Puchol

Cerdá‐Reverter

et al. 2020

IJMS

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“…Next, a plausible mechanism for voltage-dependent Ca 2+ entry has to be considered. General belief is that type II cells are devoid of VDCCs, since neither their expression nor voltage-dependent Ca 2+ signals were observed [50,64] (for review, [189]). Thus, to generate Ca 2+ influx, taste-bud cells might employ cyclic-nucleotide-suppressible channels [146,199] or, as upon prolonged bitter stimulation, store-operated Ca 2+ entry [216].…”

Section: Brief Access ✘mentioning

confidence: 99%

An alternative pathway for sweet sensation: possible mechanisms and physiological relevance

Molitor

Riedel

Krohn

et al. 2020

Pflugers Arch - Eur J Physiol

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Sweet substances are detected by taste-bud cells upon binding to the sweet-taste receptor, a T1R2/T1R3 heterodimeric G proteincoupled receptor. In addition, experiments with mouse models lacking the sweet-taste receptor or its downstream signaling components led to the proposal of a parallel "alternative pathway" that may serve as metabolic sensor and energy regulator. Indeed, these mice showed residual nerve responses and behavioral attraction to sugars and oligosaccharides but not to artificial sweeteners. In analogy to pancreatic β cells, such alternative mechanism, to sense glucose in sweet-sensitive taste cells, might involve glucose transporters and K ATP channels. Their activation may induce depolarization-dependent Ca 2+ signals and release of GLP-1, which binds to its receptors on intragemmal nerve fibers. Via unknown neuronal and/or endocrine mechanisms, this pathway may contribute to both, behavioral attraction and/or induction of cephalic-phase insulin release upon oral sweet stimulation. Here, we critically review the evidence for a parallel sweet-sensitive pathway, involved signaling mechanisms, neural processing, interactions with endocrine hormonal mechanisms, and its sensitivity to different stimuli. Finally, we propose its physiological role in detecting the energy content of food and preparing for digestion. Keywords Taste-bud cells . Sweet-taste receptor . TAS1R2 . TAS1R3 . Artificial sweeteners . Cephalic-phase insulin release . Glucagon-like peptide-1 . Glucose transporters Abbreviations CPIR Cephalic-phase insulin release DMNX Dorsal motor nucleus of vagus nerve GLP-1 Glucagon-like peptide-1 GLUT Glucose -transporter IP3 Inositol triphosphate K ATP ATP-sensitive K + channels NTS Nucleus of the solitary tract PLCβ2 Phospholipase-Cβ2 SGLT Sodium/glucose cotransporter T1R1 Taste receptor type 1 member 1 T1R2 Taste receptor type 1 member 2 T1R3 Taste receptor type 1 member 3 TRPM5 Membrane-associated transient receptor potential channel subfamily M member 5 VDCCs Voltage-dependent calcium channels VRAC Volume-regulated anion channel

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“…Intracellular Ca 2+ dynamics are crucial to regulating diverse cellular processes, including cell proliferation, differentiation, and cell–cell communication 1 – 3 . Intracellular Ca 2+ is stored in the endoplasmic reticulum (ER), and cell surface receptor-mediated extracellular stimuli trigger Ca 2+ influx into the cytoplasm to initiate a physiological response 4 .…”

Section: Introductionmentioning

confidence: 99%

Jaw1/LRMP increases Ca2+ influx upon GPCR stimulation with heterogeneous effect on the activity of each ITPR subtype

Okumura

Kozono

Sato

et al. 2022

Sci Rep

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Ca2+ influx upon G protein-coupled receptor (GPCR) stimulation is observed as a cytosolic Ca2+ concentration oscillation crucial to initiating downstream responses including cell proliferation, differentiation, and cell–cell communication. Although Jaw1 is known to interact with inositol 1,4,5-triphosphate receptor (ITPRs), Ca2+ channels on the endoplasmic reticulum, the function of Jaw1 in the Ca2+ dynamics with physiological stimulation remains unclear. In this study, using inducible Jaw1-expressing HEK293 cells, we showed that Jaw1 increases Ca2+ influx by GPCR stimulation via changing the Ca2+ influx oscillation pattern. Furthermore, we showed that Jaw1 increases the Ca2+ release activity of all ITPR subtypes in a subtly different manner. It is well known that the Ca2+ influx oscillation pattern varies from cell type to cell type, therefore these findings provide an insight into the relationship between the heterogeneous Ca2+ dynamics and the specific ITPR and Jaw1 expression patterns.

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Calcium signaling in taste cells

Cited by 15 publications

References 48 publications

Insights into the Function and Evolution of Taste 1 Receptor Gene Family in the Carnivore Fish Gilthead Seabream (Sparus aurata)

Insights into the Function and Evolution of Taste 1 Receptor Gene Family in the Carnivore Fish Gilthead Seabream (Sparus aurata)

An alternative pathway for sweet sensation: possible mechanisms and physiological relevance

Jaw1/LRMP increases Ca2+ influx upon GPCR stimulation with heterogeneous effect on the activity of each ITPR subtype

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