• Media type: E-Article
  • Title: An Analysis of γ‐Aminobutyrate Receptors and Uptake by Isolated Purkinje Cells
  • Contributor: Henn, Fritz A.; Venema, Rick; Anderson, David; Sellstrom, Ake
  • Published: Wiley, 1980
  • Published in: Journal of Neurochemistry
  • Extent: 1671-1677
  • Language: English
  • DOI: 10.1111/j.1471-4159.1980.tb11259.x
  • ISSN: 0022-3042; 1471-4159
  • Keywords: Cellular and Molecular Neuroscience ; Biochemistry
  • Abstract: <jats:p><jats:bold>Abstract: </jats:bold> An isolated fraction of Purkinje perikarya was prepared. This fraction had [<jats:sup>3</jats:sup>H]GABA receptor binding and [<jats:sup>3</jats:sup>H]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.</jats:p>
  • Description: <jats:p><jats:bold>Abstract: </jats:bold> An isolated fraction of Purkinje perikarya was prepared. This fraction had [<jats:sup>3</jats:sup>H]GABA receptor binding and [<jats:sup>3</jats:sup>H]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.</jats:p>
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