Segregated Expression of ENaC Subunits in Taste Cells
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Segregated Expression of ENaC Subunits in Taste Cells. / Lossow, Kristina; Hermans-Borgmeyer, Irm; Meyerhof, Wolfgang; Behrens, Maik.
in: CHEM SENSES, Jahrgang 45, Nr. 4, 21.05.2020, S. 235-248.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Segregated Expression of ENaC Subunits in Taste Cells
AU - Lossow, Kristina
AU - Hermans-Borgmeyer, Irm
AU - Meyerhof, Wolfgang
AU - Behrens, Maik
N1 - © The Author(s) 2020. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.
PY - 2020/5/21
Y1 - 2020/5/21
N2 - Salt taste is one of the 5 basic taste qualities. Depending on the concentration, table salt is perceived either as appetitive or aversive, suggesting the contribution of several mechanisms to salt taste, distinguishable by their sensitivity to the epithelial sodium channel (ENaC) blocker amiloride. A taste-specific knockout of the α-subunit of the ENaC revealed the relevance of this polypeptide for low-salt transduction, whereas the response to other taste qualities remained normal. The fully functional ENaC is composed of α-, β-, and γ-subunits. In taste tissue, however, the precise constitution of the channel and the cell population responsible for detecting table salt remain uncertain. In order to examine the cells and subunits building the ENaC, we generated mice carrying modified alleles allowing the synthesis of green and red fluorescent proteins in cells expressing the α- and β-subunit, respectively. Fluorescence signals were detected in all types of taste papillae and in taste buds of the soft palate and naso-incisor duct. However, the lingual expression patterns of the reporters differed depending on tongue topography. Additionally, immunohistochemistry for the γ-subunit of the ENaC revealed a lack of overlap between all potential subunits. The data suggest that amiloride-sensitive recognition of table salt is unlikely to depend on the classical ENaCs formed by α-, β-, and γ-subunits and ask for a careful investigation of the channel composition.
AB - Salt taste is one of the 5 basic taste qualities. Depending on the concentration, table salt is perceived either as appetitive or aversive, suggesting the contribution of several mechanisms to salt taste, distinguishable by their sensitivity to the epithelial sodium channel (ENaC) blocker amiloride. A taste-specific knockout of the α-subunit of the ENaC revealed the relevance of this polypeptide for low-salt transduction, whereas the response to other taste qualities remained normal. The fully functional ENaC is composed of α-, β-, and γ-subunits. In taste tissue, however, the precise constitution of the channel and the cell population responsible for detecting table salt remain uncertain. In order to examine the cells and subunits building the ENaC, we generated mice carrying modified alleles allowing the synthesis of green and red fluorescent proteins in cells expressing the α- and β-subunit, respectively. Fluorescence signals were detected in all types of taste papillae and in taste buds of the soft palate and naso-incisor duct. However, the lingual expression patterns of the reporters differed depending on tongue topography. Additionally, immunohistochemistry for the γ-subunit of the ENaC revealed a lack of overlap between all potential subunits. The data suggest that amiloride-sensitive recognition of table salt is unlikely to depend on the classical ENaCs formed by α-, β-, and γ-subunits and ask for a careful investigation of the channel composition.
KW - Amiloride/metabolism
KW - Animals
KW - Cloning, Molecular
KW - Epithelial Sodium Channels/metabolism
KW - Gene Knock-In Techniques
KW - Genotyping Techniques
KW - Humans
KW - Kidney
KW - Luminescent Proteins/genetics
KW - Mice
KW - Mice, Inbred C57BL
KW - Models, Animal
KW - Protein Conformation
KW - Taste
KW - Taste Buds/cytology
KW - Taste Perception
KW - Tissue Distribution
U2 - 10.1093/chemse/bjaa004
DO - 10.1093/chemse/bjaa004
M3 - SCORING: Journal article
C2 - 32006019
VL - 45
SP - 235
EP - 248
JO - CHEM SENSES
JF - CHEM SENSES
SN - 0379-864X
IS - 4
ER -