Correlation of glutamate binding activity with glutamate-binding protein immunoreactivity in the brain of control and alcohol-treated rats

E. Michaelis, S. Roy, N. Galton, M. Cunningham, E. LeCluyse, M. Michaelis

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Specific antibodies raised against a glutamate binding protein purified from bovine brain were used to trace the immunoreactivity of this protein in rat brain subcellular fractions. In the subcellular fractions obtained from whole brain homogenates, the synaptic membranes had the highest immunochemical reactivity towards the anti-glutamate-binding protein antibodies. The combination of measurements of glutamate binding activity and glutamate-binding protein immunoreactivity indicated that in brain synaptic membranes from control animals the highest activity in these two measures was associated with a synaptic plasma membrane subfraction that was enriched with synaptic junctions. In animals treated with ethanol for 14 days, there was a significant increase in the density of synaptic membrane glutamate binding sites. This increase in glutamate binding capacity was correlated with a greater than two-fold increase in the glutamate binding activity and binding protein immunoreactivity of the light synaptic membrane subfraction, a subfraction which does not contain many recognizable synaptic junctions. Acute administration of ethanol to rats produced a moderate but non-significant decrease in glutamate binding capacity of synaptic membranes. The increase in the number of glutamate binding protein subunits in brain plasma membranes may be an adaptive response of central nervous system neurons to the acute effects of ethanol on glutamate synaptic transmission.

Original languageEnglish (US)
Pages (from-to)209-218
Number of pages10
JournalNeurochemistry International
Issue number2
StatePublished - 1987

Bibliographical note

Funding Information:
Acknowledgements--This work was supported by grants from the National Institute on Alcoholism and Alcohol Abuse (AA 04732), from the American Heart Association, Kansas Affiliate (KS-83-73 and KS-84-G21), and from the U.S. Army Research Office (DAAG29-83-K0065). We acknowledge the support provided by the Center for Biomedical Research--The University of Kansas. We thank Ms Mary Seyk and Linda Kunkle for typing the manuscript.

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