We examined the molecular structural and functional properties of meta
botropic glutamate receptors (mGluRs) in rat brains, especially the su
btypes 1 and 5 which are known to stimulate phosphoinositide (PI) meta
bolism. We found that mGluR5 as well as mGluR1 has structural variants
, most likely derived by the alternative splicing of the gene. We also
found that, under certain circumstances, mGluR1 could inhibit, instea
d of stimulate, PI turnover in a G protein-dependent manner. This find
ing may give a possible explanation for the discrepancy we observed be
tween the postnatal development of glutamate-stimulated PI turnover an
d the postnatal ontogenesis of mGluRs.