Titlebook: Excitatory Amino Acids and Second Messenger Systems; Vivian I. Teichberg,Lechoslaw Turski Conference proceedings 1991 Springer-Verlag Berl

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Protein Dephosphorylation as a Mediator of NMDA Receptor Signal Transduction,tory amino acid glutamate. At least some of these events are likely to be mediated by changes in protein phosphorylation, either through activation of calcium-dependent protein kinases or through activation of the calcium-dependent protein phosphatase calcineurin. Glutamate acts on several different

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From Excitatory Amino Acid Receptors to Long-Term Potentiation: An Insight into the Role of Ca2+,athway, the induction of LTP involves (a) the activation of NMDA receptors [3] and (b) increases in Ca. concentration in the postsynaptic cells [4, 5]. This has led to the popular notion that the neurotransmitter, through its action on NMDA (and possibly other glutamate) receptors, generates a Ca. s

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Evidence that Arachidonic Acid Plays a Role in Long-Term Potentiation, receptor together with strong depolarization of the postsynaptic membrane relieves the Mg. block on the NMDA-associated Ca . channel and allows influx of Ca.; the subsequent change in Ca. concentration triggers LTP. Although there is no consensus of opinion on mechanisms underlying maintenance of L

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Protein Dephosphorylation as a Mediator of NMDA Receptor Signal Transduction,hyl-.-aspartate (NMDA) receptors — induces membrane depolarization, which in turn can lead to opening of voltage-sensitive calcium channels [1,3,4]. In addition, NMDA receptors [5,6], and possibly some species of kainate receptors [7], are themselves permeable to calcium ions. Thus, activation of an

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Anja Pitton,Dirk Scholten-Akoun EAA pathways can be thought of as functionally and pharmacologically distinct EAA systems. Furthermore, in addition to this level of complexity, recent studies have shown that individual EAA receptor types can represent multiple isoforms that can differ in function [1]. Thus, there is considerable

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