Antibodies directed against ubiquitin inhibit high affinity [3H]choline uptake in rat cerebral cortical synaptosomes

E. M. Meyer, C. M. West, V. Chau

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21 Scopus citations

Abstract

Sodium-dependent [3H]choline uptake and coupled [3H]acetylcholine synthesis were inhibited in rat cerebral cortical synaptosomes in a dose- (1-10 μg/ml) and time-dependent manner by affinity-purified antibodies directed against ubiquitin (anti-Ub). Neither sodium-independent [3H]choline uptake nor [3H]acetylcholine release was affected by up to 10 μg/ml anti-Ub, indicating that the cholinergic terminals were not depolarized by the anti-Ub. Binding of anti-Ub to synaptosomes, as measured with 125I-protein A, was saturable and occurred over the same concentration range (1-10 μg/ml) at which uptake inhibition was observed. Although preimmune IgG bound to the synaptosome preparation to a greater extent and was apparently not readily saturable, this fortuitous binding was without effect on high affinity choline uptake and conversion to acetylcholine. The results suggest the presence of a ubiquitin-protein conjugate on the synaptosomal surface and a functional relationship between this protein conjugate and the sodium-dependent choline transport system.

Original languageEnglish (US)
Pages (from-to)14365-14368
Number of pages4
JournalJournal of Biological Chemistry
Volume261
Issue number31
StatePublished - 1986

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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