Gustatory sensory cells express a receptor responsive to protein breakdown products (GPR92)

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Gustatory sensory cells express a receptor responsive to protein breakdown products (GPR92). / Haid, Désirée; Widmayer, Patricia; Voigt, Anja; Chaudhari, Nirupa; Boehm, Ulrich; Breer, Heinz.

In: HISTOCHEM CELL BIOL, Vol. 140, No. 2, 01.08.2013, p. 137-45.

Research output: SCORING: Contribution to journalSCORING: Journal articleResearchpeer-review

Harvard

Haid, D, Widmayer, P, Voigt, A, Chaudhari, N, Boehm, U & Breer, H 2013, 'Gustatory sensory cells express a receptor responsive to protein breakdown products (GPR92)', HISTOCHEM CELL BIOL, vol. 140, no. 2, pp. 137-45. https://doi.org/10.1007/s00418-013-1080-2

APA

Haid, D., Widmayer, P., Voigt, A., Chaudhari, N., Boehm, U., & Breer, H. (2013). Gustatory sensory cells express a receptor responsive to protein breakdown products (GPR92). HISTOCHEM CELL BIOL, 140(2), 137-45. https://doi.org/10.1007/s00418-013-1080-2

Vancouver

Bibtex

@article{b67a1982237c4b4e8b54e3ad1d82654d,
title = "Gustatory sensory cells express a receptor responsive to protein breakdown products (GPR92)",
abstract = "The ingestion of dietary protein is of vital importance for the maintenance of fundamental physiological processes. The taste modality umami, with its prototype stimulus, glutamate, is considered to signal the protein content of food. Umami was thought to be mediated by the heterodimeric amino acid receptor, T1R1 + T1R3. Based on knockout studies, additional umami receptors are likely to exist. In addition to amino acids, certain peptides can also elicit and enhance umami taste suggesting that protein breakdown products may contribute to umami taste. The recently deorphanized peptone receptor, GPR92 (also named GPR93; LPAR5), is expressed in gastric enteroendocrine cells where it responds to protein hydrolysates. Therefore, it was of immediate interest to investigate if the receptor GPR92 is expressed in gustatory sensory cells. Using immunohistochemical approaches we found that a large population of cells in murine taste buds was labeled with an GPR92 antibody. A molecular phenotyping of GPR92 cells revealed that the vast majority of GPR92-immunoreactive cells express PLCβ2 and can therefore be classified as type II cells. More detailed analyses have shown that GPR92 is expressed in the majority of T1R1-positive taste cells. These results indicate that umami cells may respond not only to amino acids but also to peptides in protein hydrolysates.",
author = "D{\'e}sir{\'e}e Haid and Patricia Widmayer and Anja Voigt and Nirupa Chaudhari and Ulrich Boehm and Heinz Breer",
year = "2013",
month = aug,
day = "1",
doi = "10.1007/s00418-013-1080-2",
language = "English",
volume = "140",
pages = "137--45",
journal = "HISTOCHEM CELL BIOL",
issn = "0948-6143",
publisher = "Springer",
number = "2",

}

RIS

TY - JOUR

T1 - Gustatory sensory cells express a receptor responsive to protein breakdown products (GPR92)

AU - Haid, Désirée

AU - Widmayer, Patricia

AU - Voigt, Anja

AU - Chaudhari, Nirupa

AU - Boehm, Ulrich

AU - Breer, Heinz

PY - 2013/8/1

Y1 - 2013/8/1

N2 - The ingestion of dietary protein is of vital importance for the maintenance of fundamental physiological processes. The taste modality umami, with its prototype stimulus, glutamate, is considered to signal the protein content of food. Umami was thought to be mediated by the heterodimeric amino acid receptor, T1R1 + T1R3. Based on knockout studies, additional umami receptors are likely to exist. In addition to amino acids, certain peptides can also elicit and enhance umami taste suggesting that protein breakdown products may contribute to umami taste. The recently deorphanized peptone receptor, GPR92 (also named GPR93; LPAR5), is expressed in gastric enteroendocrine cells where it responds to protein hydrolysates. Therefore, it was of immediate interest to investigate if the receptor GPR92 is expressed in gustatory sensory cells. Using immunohistochemical approaches we found that a large population of cells in murine taste buds was labeled with an GPR92 antibody. A molecular phenotyping of GPR92 cells revealed that the vast majority of GPR92-immunoreactive cells express PLCβ2 and can therefore be classified as type II cells. More detailed analyses have shown that GPR92 is expressed in the majority of T1R1-positive taste cells. These results indicate that umami cells may respond not only to amino acids but also to peptides in protein hydrolysates.

AB - The ingestion of dietary protein is of vital importance for the maintenance of fundamental physiological processes. The taste modality umami, with its prototype stimulus, glutamate, is considered to signal the protein content of food. Umami was thought to be mediated by the heterodimeric amino acid receptor, T1R1 + T1R3. Based on knockout studies, additional umami receptors are likely to exist. In addition to amino acids, certain peptides can also elicit and enhance umami taste suggesting that protein breakdown products may contribute to umami taste. The recently deorphanized peptone receptor, GPR92 (also named GPR93; LPAR5), is expressed in gastric enteroendocrine cells where it responds to protein hydrolysates. Therefore, it was of immediate interest to investigate if the receptor GPR92 is expressed in gustatory sensory cells. Using immunohistochemical approaches we found that a large population of cells in murine taste buds was labeled with an GPR92 antibody. A molecular phenotyping of GPR92 cells revealed that the vast majority of GPR92-immunoreactive cells express PLCβ2 and can therefore be classified as type II cells. More detailed analyses have shown that GPR92 is expressed in the majority of T1R1-positive taste cells. These results indicate that umami cells may respond not only to amino acids but also to peptides in protein hydrolysates.

U2 - 10.1007/s00418-013-1080-2

DO - 10.1007/s00418-013-1080-2

M3 - SCORING: Journal article

C2 - 23436159

VL - 140

SP - 137

EP - 145

JO - HISTOCHEM CELL BIOL

JF - HISTOCHEM CELL BIOL

SN - 0948-6143

IS - 2

ER -