Abstract：
:Depolarizing actions of 4 conformationally restricted L-glutamate analogues, (2S,3S,4S) isomer (L-CCG-I), (2S,3R,4R) isomer (L-CCG-II), (2S,3S,4R) isomer (L-CCG-III) and (2S,3R,4S) isomer (L-CCG-IV) of L-alpha-(carboxycyclopropyl)-glycine (L-CCG), were investigated in the isolated rat spinal cord by extracellular recordings of potential changes of motoneurones from the ventral roots, in order to study the interaction between the conformation of glutamate and its receptor subtype. The order of the depolarizing activity was quisqualate greater than L-CCG-IV = kainate greater than NMDA greater than L-CCG-I greater than L-CCG-III greater than L-CCG-II. The depolarization caused by L-CCG-IV was effectively blocked by the NMDA antagonists and Mg2+ ions, while the L-CCG-I response was not affected by these blockers. These results suggest that the NMDA-type receptor is activated by a folded form of L-glutamate.
journal_name
Brain Resjournal_title
Brain researchauthors
Shinozaki H,Ishida M,Shimamoto K,Ohfune Ydoi
10.1016/0006-8993(89)90207-2subject
Has Abstractpub_date
1989-02-20 00:00:00pages
355-9issue
1-2eissn
0006-8993issn
1872-6240pii
0006-8993(89)90207-2journal_volume
480pub_type
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