Adenylyl cyclase expression and modulation of cAMP in rat taste cells.

Journal Article (Journal Article)

cAMP is a second messenger implicated in sensory transduction for taste. The identity of adenylyl cyclase (AC) in taste cells has not been explored. We have employed RT-PCR to identify the AC isoforms present in taste cells and found that AC 4, 6, and 8 are expressed as mRNAs in taste tissue. These proteins are also expressed in a subset of taste cells as revealed by immunohistochemistry. Alterations of cAMP concentrations are associated with transduction of taste stimuli of several classes. The involvement of particular ACs in this modulation has not been investigated. We demonstrate that glutamate, which is a potent stimulus eliciting a taste quality termed umami, causes a decrease in cAMP in forskolin-treated taste cells. The potentiation of this response by inosine monophosphate, the lack of response to d-glutamate, and the lack of response to umami stimuli in nonsensory lingual epithelium all suggest that the cAMP modulation represents umami taste transduction. Because cAMP downregulation via ACs can be mediated through Galpha(i) proteins, we examined the colocalization of the detected ACs with Galpha(i) proteins and found that 66% of AC8 immunopositive taste cells are also positive for gustducin, a taste-specific Galpha(i) protein. Whether AC8 is directly involved in signal transduction of umami taste remains to be established.

Full Text

Duke Authors

Cited Authors

  • Abaffy, T; Trubey, KR; Chaudhari, N

Published Date

  • June 2003

Published In

Volume / Issue

  • 284 / 6

Start / End Page

  • C1420 - C1428

PubMed ID

  • 12606315

International Standard Serial Number (ISSN)

  • 0363-6143

Digital Object Identifier (DOI)

  • 10.1152/ajpcell.00556.2002


  • eng

Conference Location

  • United States