Cited by 40Ion channel regulation and functionNeuroscience and Neuropharmacology ResearchIon Channels and Receptors

“Fast” plasma membrane calcium pump PMCA2a concentrates in GABAergic terminals in the adult rat brain

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Burette, Alain C., Strehler, Emanuel E., Weinberg, Richard J.·2009·Journal of Comparative Neurology

Abstract

The plasma membrane Ca 2+‐ATPases (PMCA) represent the major high‐affinity Ca 2+ extrusion system in the brain. PMCAs comprise four isoforms and over 20 splice variants. Their different functional properties may permit different PMCA splice variants to accommodate different kinds of local [Ca 2+] transients, but for a specific PMCA to play a unique role in local Ca 2+ handling it must be targeted to the appropriate subcellular compartment. We used immunohistochemistry to study the spatial distribution of PMCA2a—one of the two major carboxyl‐terminal splice variants of PMCA2—in the adult rat brain, testing whether this isoform, with especially high basal activity, is targeted to specific subcellular compartments. In striking contrast to the widespread distribution of PMCA2 as a whole, we found that PMCA2a is largely restricted to parvalbumin‐positive inhibitory presynaptic terminals throughout the brain. The only major exception to this targeting pattern was in the cerebellar cortex, where PMCA2a also concentrates postsynaptically, in the spines of Purkinje cells. We propose that the fast Ca 2+ activation kinetics and high V max of PMCA2a make this pump especially suited for rapid clearance of presynaptic Ca 2+ in fast‐spiking inhibitory nerve terminals, which face severe transient calcium loads. J. Comp. Neurol. 512:500–513, 2009. © 2008 Wiley‐Liss, Inc.

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  • Ca2+ is rapidly removed from cytoplasm into extracellular space by plasma membrane calcium ATPases; ATP2B2 encodes PMCA2, whose kinetics and Ca2+ affinity make it critical to synaptic function and plasticity especially in Purkinje cell dendritic spines and parvalbumin-positive GABAergic interneurons.

    “Ca2+ is rapidly removed from the cytoplasm into the extracellular space by plasma membrane calcium ATPases (PMCAs); the ATP2B2 gene encodes for PMCA2, whose faster kinetic and broader Ca2+ affinity range makes this PMCA critical to synaptic function and plasticity especially in the dendritic spines of Purkinje cells and in parvalbumin-positive gabaergic interneurons [244–246].”

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Authors
Burette, A. C., Strehler, E. E., & Weinberg, R. J.
Affiliations
  • University of North Carolina at Chapel Hill (US)
  • Mayo Clinic (US)
Corresponding author
Burette, Alain C.
Venue
Journal of Comparative Neurology
Publisher
Wiley
Published
2008-11-24
Volume
512
Issue
4
Pages
500-513
ISSN
  • 0021-9967 (ISSN-L)
  • 1096-9861
OpenAlex
W2072251721
Cited by
40
References
49
Citations by year
2024: 1 · 2022: 2 · 2021: 2 · 2020: 1 · 2019: 2 · 2018: 3 · 2017: 2 · 2016: 1 · 2015: 3 · 2014: 2 · 2013: 3 · 2012: 2
FWCI
2.19
Type
journal article
Language
en
Open access
Locations
  • The Journal of Comparative Neurology (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
  • UNC Libraries
Funders
National Institute of Neurological Disorders and Stroke (NS 44306, NS51769, R01NS035527, P01NS044306, R01NS051769, NS-35527)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Keywords
plasma membrane calcium ATPase, calcium efflux, GABAergic synapses, parvalbumin, presynaptic terminals, Purkinje cells, calcium handling, splice variants, subcellular targeting, inhibitory neurons, fast-spiking neurons, rat brain
MeSH terms
Animals, Brain, Calcium, Cell Membrane, gamma-Aminobutyric Acid, Immunohistochemistry, Isoenzymes, Male, Spinal Cord, Rats, Sprague-Dawley, Alternative Splicing, Presynaptic Terminals, Rats, Plasma Membrane Calcium-Transporting ATPases

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