Journal
JOURNAL OF NEUROSCIENCE
Volume 35, Issue 3, Pages 873-877Publisher
SOC NEUROSCIENCE
DOI: 10.1523/JNEUROSCI.2293-14.2015
Keywords
benzolamide; CA1; Ca2+ ATPase; carbonic anhydrase; carboxyeosin; hippocampus
Categories
Funding
- National Institutes of Health, National Institute of Neurological Disorders and Stroke [NS032123]
- Attilio and Olympia Ricciardi Fund
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The plasma membrane Ca2+-ATPase (PMCA) is found near postsynaptic NMDARs. This transporter is a Ca2+-H+ exchanger that raises cell surface pH. We tested whether the PMCA acts in an autocrine fashion to boost pH-sensitive, postsynaptic NMDAR currents. In mouse hippocampal slices, NMDAR EPSCs in a singly activated CA1 pyramidal neuron were reduced when buffering was augmented by exogenous carbonic anhydrase (XCAR). This effect was blocked by the enzyme inhibitor benzolamide and mimicked by the addition of HEPES buffer. Similar EPSC reduction occurred when PMCA activation was prevented by dialysis of BAPTA or the PMCA inhibitor carboxyeosin. Using HEPES, BAPTA, or carboxyeosin, the effect of XCAR was completely occluded. XCAR similarly curtailed NMDAR EPSCs of minimal amplitude, but had no effect on small AMPAR responses. These results indicate that a significant fraction of the postsynaptic NMDAR current is reliant on a perisynaptic extracellular alkaline shift generated by the PMCA.
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