The Journal of Neuroscience, June 15, 1999, 19(12):4881-4888
A Lobster Phospholipase C-
That Associates with G-Proteins in
Response to Odorants
Fuqiang
Xu and
Timothy S.
McClintock
Department of Physiology, University of Kentucky College of
Medicine, Lexington, Kentucky 40536-0298
A cDNA clone encoding a protein of 1116 amino acids with
significant homology to 
-isoforms of phospholipase C was isolated from lobster olfactory organ cDNA libraries and named lobPLC. This
cDNA hybridized predominantly to a 9 kb transcript in RNA from
olfactory organ, pereiopod, brain, and eye-eyestalk and to several
smaller minor transcripts only in eye-eyestalk. An antiserum raised to
the C terminus of lobPLC detected immunoreactivity in a single 130 kDa band in olfactory aesthetasc hairs, olfactory organ, pereiopod,
dactyl, and brain. In eye-eyestalk this 130 kDa band was abundant, and
minor bands of 100, 79, and 57 kDa also were detected. In cross
sections of the aesthetasc hairs, immunoreactivity was detected in the
outer dendritic segments of the olfactory receptor neurons, the site of
olfactory transduction. A complex odorant caused lobPLC
immunoreactivity to increase in membrane fractions and decrease in
soluble fractions of homogenates of aesthetasc hairs. The odorant also
increased the amount of lobPLC in immunoprecipitates of
G
q and G
from homogenates of aesthetasc
hairs. These results support the conclusion that lobPLC mediates
olfactory transduction.
Key words:
olfaction; vision; sensory transduction; phospholipase C; inositol phospholipids; inositol 1,4,5-trisphosphate; GTP binding
protein; G-protein; Crustacea; Arthropoda
Copyright © 1999 Society for Neuroscience 0270-6474/99/19124881-08$05.00/0
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