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Calcium Ion Impedes Translation Initiation at the Synapse
Author(s) -
Weiler Ivan Jeanne,
Childers William S.,
Greenough William T.
Publication year - 1996
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 - 10.1046/j.1471-4159.1996.66010197.x
Subject(s) - metabotropic glutamate receptor , calcium , calmodulin , nmda receptor , stimulation , glutamate receptor , synapse , metabotropic receptor , biology , microbiology and biotechnology , long term potentiation , biochemistry , receptor , biophysics , metabotropic glutamate receptor 1 , chemistry , neuroscience , organic chemistry
Stimulation of synaptoneurosome suspensions by the neurotransmitter glutamate gives rise to rapid loading of ribosomes onto mRNA and increased incorporation of amino acids into trichloroacetic acid‐precipitable polypeptides. Metabotropic glutamate receptors (mGluRs) are responsible for this effect. Although simultaneous Ca 2+ entry and mGluR stimulation do not change the response, entry of Ca 2+ 30 s or 3 min before mGluR stimulation markedly depresses the polyribosomal loading. Either NMDA or ionophore (A23187) produces the depression. A calmodulin antagonist, W7, alleviates the effect, suggesting that inactivation of phospholipase A 2 by calcium‐calmodulin‐dependent kinase II is partially responsible for the phenomenon. Thus, interaction between different classes of glutamate receptors affects the control of protein translation at the synapse. This effect may partially explain recent observations of negative interactions between receptor classes in induction of long‐term potentiation.