Rc. Bruch, PHOSPHOINOSITIDE 2ND-MESSENGERS IN OLFACTION, Comparative biochemistry and physiology. B. Comparative biochemistry, 113(3), 1996, pp. 451-459
Olfactory stimuli (odorants) are detected and recognized by binding to
receptors belonging to the G-protein-coupled receptor superfamily. Th
e binding of odorants to some receptors stimulates the activity of an
odorant-sensitive phospholipase C (PLC) thereby generating the second
messengers inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG)
. IP3 plays a key role in membrane depolarization by binding to a rece
ptor that is itself a cation channel. The formation of DAG is expected
to stimulate the activity of protein kinase C (PKC). PKC, together wi
th G-protein-coupled receptor kinases, mediates signal termination by
phosphorylation of odorant receptors and possibly other substrates. Th
is review summarizes recent evidence regarding the role of phosphoinos
itide-derived second messengers in the molecular events underlying olf
actory signaling. In addition, the role of calcium as a ''third messen
ger'' that provides a mechanism for interaction between phosphoinositi
de second messengers and components of the cyclic AMP signaling pathwa
y is also discussed.