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 journal › SCORING: Journal article › Research › peer-review
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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 -