CAMP: A role in sweet taste adaptation

Nirupa Chaudhari, Sue C. Kinnamon

Research output: Chapter in Book/Report/Conference proceedingConference contribution

1 Scopus citations


Sweet taste transduction is initiated by sugars or synthetic sweeteners binding to the G protein coupled receptor, T1R2+T1R3, and activating G protein(s) and downstream signaling effectors. Recent genetic and functional studies implicated phospholipase C (PLCβ2) and Ca2 + release from intracellular stores in sweet transduction. Considerable evidence suggests that cAMP also plays a role in the sweet response. Initial observations pointed to cAMP as the second messenger, because sweet stimuli modulate cAMP levels in taste tissue, and because membrane permeant cAMP strongly influences the physiological response of taste buds to sweet stimuli. Further, enzymes that regulate cAMP levels, adenylyl cyclases (ACs) and phosphodiesterases (PDEs) and gustducin, a G protein that can activate PDEs, are all expressed in many sweet-sensitive taste ceils. And, loss of gustducin impairs sweet responses. Yet, the precise role of cAMP in sweet taste remains unclear. Here, we review evidence that cAMP is produced as a direct consequence of receptor activation, that cAMP directly depolarizes mammalian taste cells, and that cAMP-dependent Protein Kinase (PKA) likely underlies adaptation to the sweet response. We suggest a model in which the role of α-gustducin is to keep cAMP levels low to prevent chronic adaptation of sweet-sensitive taste cells.

Original languageEnglish (US)
Title of host publicationSweetness and Sweeteners
Subtitle of host publicationBiology, Chemistry and Psychophysics
PublisherAmerican Chemical Society
Number of pages10
ISBN (Print)9780841274327
StatePublished - Mar 4 2008

Publication series

NameACS Symposium Series
ISSN (Print)0097-6156
ISSN (Electronic)1947-5918

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)


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