Conjugated bile acids such as taurocholic acid (TChA) are potent olfac
tory stimuli for Atlantic salmon (Salmo salar). A plasma membrane rich
fraction was derived from salmon olfactory rosettes and used to inves
tigate TChA signal transduction and receptor binding. In the presence
of GTP gamma S, TChA caused dose-dependent stimulation of phosphatidyl
inositol 4,5-bisphosphate (PIP2) breakdown, half maximal at less than
10(-7) M TChA. Stimulation of PIP2 breakdown by TChA required GTP gamm
a S, was blocked by GDP beta S, and was mimicked by AlF4-, consistent
with a G protein requirement. AlF4- and Ca2+ stimulated breakdown of P
IP2, but not phosphatidylcholine, arguing against a non-specific lipas
e activation. Stimulation of PIP2 breakdown by TChA was maximal at low
Ca2+ concentration, less than or equal to 10 nM. Conventional binding
analysis with H-3-TChA was inconclusive due to a high degree of non-s
pecific binding and to lack of tissue specificity expected for an olfa
ctory receptor. Analysis of odorant amino acid binding indicated possi
ble interaction of TChA with a putative acidic amino acid receptor but
no interaction of TChA with a putative neutral amino acid receptor. W
e conclude that olfactory discrimination between amino acids and bile
acids occurs in part at the receptor level while both classes of odors
appear to use the same signal transduction mechanism, G protein media
ted activation of phosphoinositide specific phospholipase C (PLC).