Cited by 65Biochemical Analysis and Sensing TechniquesRenin-Angiotensin System StudiesIon Channels and Receptors

Expression of Renin-Angiotensin System Components in the Taste Organ of Mice

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Shigemura, Noriatsu, Takai, Shingo, Hirose, Fumie, Yoshida, Ryusuke, Sanematsu, Keisuke, Ninomiya, Yuzo·2019·Nutrients

Abstract

The systemic renin-angiotensin system (RAS) is an important regulator of body fluid and sodium homeostasis. Angiotensin II (AngII) is a key active product of the RAS. We previously revealed that circulating AngII suppresses amiloride-sensitive salt taste responses and enhances the responses to sweet compounds via the AngII type 1 receptor (AT1) expressed in taste cells. However, the molecular mechanisms underlying the modulation of taste function by AngII remain uncharacterized. Here we examined the expression of three RAS components, namely renin, angiotensinogen, and angiotensin-converting enzyme-1 (ACE1), in mouse taste tissues. We found that all three RAS components were present in the taste buds of fungiform and circumvallate papillae and co-expressed with αENaC (epithelial sodium channel α-subunit, a salt taste receptor) or T1R3 (taste receptor type 1 member 3, a sweet taste receptor component). Water-deprived mice exhibited significantly increased levels of renin expression in taste cells (p < 0.05). These results indicate the existence of a local RAS in the taste organ and suggest that taste function may be regulated by both locally-produced and circulating AngII. Such integrated modulation of peripheral taste sensitivity by AngII may play an important role in sodium/calorie homeostasis.

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  • Angiotensin-converting enzyme 2, the receptor that mediates entry of SARS-CoV-2 into cells, is expressed in the oral mucosa and is enriched in human tongue cells among both gustatory and nongustatory tongue epithelium.

    “Angiotensin‐converting enzyme 2, the receptor that mediates entry of SARS‐CoV‐2 into cells, is expressed in the oral mucosa and is enriched in human tongue cells among both gustatory and nongustatory tongue epithelium.”

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Authors
Shigemura, N., Takai, S., Hirose, F., Yoshida, R., Sanematsu, K., & Ninomiya, Y.
Affiliations
Kyushu University (JP)
Corresponding author
  • Shigemura, Noriatsu
  • Ninomiya, Yuzo
Venue
Nutrients
Publisher
MDPI AG
Published
2019-09-19
Volume
11
Issue
9
Pages
2251
ISSN
2072-6643 (ISSN-L)
OpenAlex
W2974276026
Cited by
65
References
53
Citations by year
2026: 3 · 2025: 3 · 2024: 6 · 2023: 6 · 2022: 7 · 2021: 15 · 2020: 25
FWCI
8.92
Type
journal article
Language
en
Open access
Locations
  • Nutrients (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
The Ministry of Education, Culture, Sports, Science and Technology of Japan (Grants-in-Aid for Scientific Research 15K11044, 18K19652 and 19H03818 (N.S.), 18077004 and 18109013 (Y.N.))
Topics
  • Health Sciences › Nursing › Nutrition and Dietetics › Biochemical Analysis and Sensing Techniques
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Renin-Angiotensin System Studies
  • Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Keywords
renin-angiotensin system, angiotensin II, taste buds, taste cells, renin, angiotensinogen, angiotensin-converting enzyme, T1R3, sweet taste, salty taste, water deprivation, sodium homeostasis, local renin-angiotensin system
MeSH terms
Angiotensinogen, Animals, Female, Gene Expression Regulation, Glutamate Decarboxylase, Male, Renin, Renin-Angiotensin System, Taste, Taste Buds, Receptors, G-Protein-Coupled, Green Fluorescent Proteins, Mice, Epithelial Sodium Channels

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