Literature DB >> 2983842

Cations differentially affect subpopulations of L-glutamate receptors in rat synaptic plasma membranes.

E E Mena, D T Monaghan, S R Whittemore, C W Cotman.   

Abstract

Several cations were examined for their ability to specifically affect one of the 3 L-glutamate (L-Glu) binding sites in rat forebrain synaptic plasma membranes (i.e. Na+-dependent, Cl--dependent and Cl--independent). Na+-dependent binding was potently inhibited by K+ and NH4+ ions. Other monovalent cations tested (Cs+, Li+, triethylammonium) had no effect on this binding site. Polyvalent cations (Co2+, Ni2+, Cu2+, Zn2+, Cd2+ and Cr3+) also had little effect on the Na+-dependent L-Glu binding site. Cl--dependent L-Glu binding was potently inhibited by Na+ ions but was not affected by other monovalent ions. All of the divalent cations were potent inhibitors of both Cl--dependent and -independent binding. The results show that these binding sites of L-Glu can be distinguished by their response to cations and suggest possible novel modes of regulation in vivo.

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Year:  1985        PMID: 2983842     DOI: 10.1016/0006-8993(85)90542-6

Source DB:  PubMed          Journal:  Brain Res        ISSN: 0006-8993            Impact factor:   3.252


  2 in total

1.  Non-NMDA excitatory amino acid receptors in a subcellular fraction enriched in cerebellar glomeruli.

Authors:  F Viennot; J de Barry; G Gombos
Journal:  Neurochem Res       Date:  1991-04       Impact factor: 3.996

2.  Hepatic encephalopathy influences high-affinity uptake of transmitter glutamate and aspartate into the hippocampal formation.

Authors:  W Schmidt; G Wolf; K Grüngreiff; M Meier; T Reum
Journal:  Metab Brain Dis       Date:  1990-03       Impact factor: 3.584

  2 in total

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