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ON THE MECHANISM OF OUABAIN INHIBITION OF SYNAPTOSOME PROTEIN SYNTHESIS
Author(s) -
Verity M. Anthony,
Brown W. Jann,
Cheung Marshall K.
Publication year - 1979
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1979.tb11057.x
Subject(s) - ouabain , synaptosome , cycloheximide , protein biosynthesis , glycine , leucine , chemistry , biochemistry , amino acid , sodium , in vitro , organic chemistry
— Ouabain (200μ m ) inhibited incorporation of radiolabelled leucine or glycine into the protein of neonatal synaptosome fractions but had minimal effect on preparations from adult rats. Leucine uptake into synaptosomes was rapid but not influenced by 200μ m ‐ouabain in contrast to ouabain inhibition of [ 14 C]glycine and [ 14 C]γ‐aminobutyric acid uptake. Ouabain blocked the Na + ‐dependent (stimulated) component of synaptosome fraction protein synthesis in the presence of 25m m ‐K + . Ouabain inhibition was not alleviated by addition of ADP or ATP. 100μ m ‐atractylate failed to influence [ 3 H]leucine uptake or incorporation. Synergistic inhibition by ouabain was observed with the cycloheximide‐sensitive component of protein synthesis and the chloramphenicol sensitive phase. Increasing the medium Ca 2+ concentration stimulated protein synthesis and this stimulated component was inhibited by ouabain. Ouabain inhibition was associated with decreasing intraterminal K + concentration and [K] i was linearly related to the protein synthesis rate in control and ouabain treated preparations.