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Chemical Senses Advance Access originally published online on March 5, 2007
Chemical Senses 2007 32(5):411-421; doi:10.1093/chemse/bjm006
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© The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Expression of Aquaporin Water Channels in Rat Taste Buds

Kristina J. Watson1 *, Insook Kim2 *, Arian F. Baquero1, Catherine A. Burks1, Lidong Liu3 and Timothy A. Gilbertson1

1 Department of Biology and The Center for Advanced Nutrition, Utah State University, Logan, UT 84322, USA 2 Department of Pediatrics, University of Arkansas Medical Sciences, Little Rock, AR 72202, USA 3 Brain Research Centre, University of British Columbia, Vancouver, BC V6T 2B5, Canada

Correspondence to be sent to: Kristina J. Watson, Department of Biology, 5305 Old Main Hill, Logan, UT 84322-5305, USA. e-mail: kspray{at}biology.usu.edu


   Abstract

In order to gain insight into the molecular mechanisms that allow taste cells to respond to changes in their osmotic environment, we have used primarily immunocytochemical and molecular approaches to look for evidence of the presence of aquaporin-like water channels in taste cells. Labeling of isolated taste buds from the fungiform, foliate, and vallate papillae in rat tongue with antibodies against several of the aquaporins (AQPs) revealed the presence of AQP1, AQP2, and AQP5 in taste cells from these areas. AQP3 antibodies failed to label isolated taste buds from any of the papillae. There was an apparent difference in the regional localization of AQP labeling within the taste bud. Antibodies against AQP1 and AQP2 labeled predominantly the basolateral membrane, whereas the AQP5 label was clearly evident on both the apical and basolateral membranes of cells within the taste bud. Double labeling revealed that AQP1 and AQP2 labeled many, but not all, of the same taste cells. Similar double-labeling experiments with anti-AQP2 and anti-AQP5 clearly showed that AQP5 was expressed on or near the apical membranes whereas AQP2 was absent from this area. The presence of these 3 types of AQPs in taste buds but not in non–taste bud-containing epithelia was confirmed using reverse transcription–polymerase chain reaction. Experiments using patch clamp recording showed that the AQP inhibitor, tetraethylammonium, significantly reduced hypoosmotic-induced currents in rat taste cells. We hypothesize that the AQPs may play roles both in the water movement underlying compensatory mechanisms for changes in extracellular osmolarity and, in the case of AQP5 in particular, in the gustatory response to water.

Key words: aquaporin, immunocytochemistry, RT–PCR, taste, water


* These authors contributed equally to this work.

Accepted 1 February 2007


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