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Journal of Neuroscience, Vol 13, 2001-2012, Copyright © 1993 by Society for Neuroscience
Differential localization of phosphoinositide-linked metabotropic glutamate receptor (mGluR1) and the inositol 1,4,5-trisphosphate receptor in rat brain
M Fotuhi, AH Sharp, CE Glatt, PM Hwang, M von Krosigk, SH Snyder and TM Dawson
Department of Neuroscience, Neurology Pharmacology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
The type 1 metabotropic glutamate receptor (mGluR1) is through to act via
the phosphoinositide (PI) system with the associated formation of inositol
1,4,5-trisphosphate (IP3) and Ca2+ release. Utilizing immunohistochemistry
and in situ hybridization, we have localized protein and mRNA,
respectively, for the mGluR1 and the IP3 receptor (IP3R). We have also
localized glutamate-linked PI turnover by autoradiography with 3H-cytidine.
We observe a striking contrast in localizations of mGluR1 and IP3R both for
protein and mRNA. For instance, mGluR1 occurs in the apparent absence of
IP3R in neurons of the stratum oriens of the CA1 hippocampus, islands of
Calleja, anterodorsal nucleus of thalamus, lateral nucleus of hypothalamus,
and the granular cell layer and the deep nuclei of cerebellum. mGluR1
actions in these brain regions may primarily be mediated through the
protein kinase C limb of the PI system, as they contain moderate amounts of
3H-phorbol ester binding. The subthalamic nucleus, red nucleus, and
Darkshevich's nucleus, which possess high levels of mGluR1, are devoid of
both IP3R immunoreactivity and 3H-phorbol ester binding. These reciprocal
localizations suggest that mGluR1 actions in many brain areas may not
primarily involve IP3, reflecting instead influences on protein kinase C or
other second messengers.
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