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An Analysis of γ‐Aminobutyrate Receptors and Uptake by Isolated Purkinje Cells

  • Fritz A. Henn(corresponding author)
    ,
  • Rick Venema
    ,
  • David Anderson
    ,
  • Ake Sellstrom
*Corresponding author for this work
  • University of Iowa
Scholary Output:
Contribution to journal
Article
Peer-review

Abstract

Abstract: An isolated fraction of Purkinje perikarya was prepared. This fraction had [3H]GABA receptor binding and [3H]muscimol binding analogous to that reported for heterogeneous cerebellar membranes. The finding of two binding components with each ligand suggests that these components do not represent two binding sites, one presynaptic and the other postsynaptic, since both are clearly seen on purified Purkinje cell bodies. Subcellular fractionation indicates that synaptic endings and plasma membranes are enriched in GABA receptors compared with intracellular organelles. Purkinje cell bodies were also found to possess a high‐affinity transport system for GABA, which was sensitive to inhibition by diaminobutyric acid (DABA) but not by β‐alanine. They showed no evidence of homoexchange (the movement of label without net transport). This supports our suggestion that homoexchange is an artifact of synaptic particle formation.

Publication Information

Output type

Scholary Output:
Contribution to journal
Article
Peer-review

Original language

English (US)

Pages from-to (Number of pages)

Pages 1671-1677 (7 pages)

Journal (Volume, Issue Number)

Journal of Neurochemistry (Volume 34, Issue 6)

Publication milestones

  • Published - 06/1980

Publication status

Published - 06/1980

ISSN

0022-3042

Publication IDs

  • Scopus: 0018908658
  • PubMed: 7381493

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