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Evidence that Aspartate Aminotransferase Activity and Ketodicarboxylate Carrier Function Are Essential for Biosynthesis of Transmitter Glutamate
Author(s) -
Palaiologos Georgios,
Hertz Left,
Schousboe Arne
Publication year - 1988
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.1471-4159.1988.tb04872.x
Subject(s) - aminooxyacetic acid , glutamate receptor , glutaminase , glutamate aspartate transporter , glutamine , glutamatergic , biochemistry , biology , glutamine synthetase , glutamic acid , microbiology and biotechnology , chemistry , metabotropic glutamate receptor , amino acid , enzyme , receptor
Based on the selective inhibition of glutamate release in cerebellar granule cells in primary cultures by the aspartate aminotransferase inhibitor, aminooxyacetic acid, and by the ketodicarboxylate carrier inhibitor, phenylsuccinate, a novel model for synthesis of transmitter glutamate is suggested: Glutamate is formed from glutamine in the mitochondrial intramembrane space by phosphate‐activated glutaminase, transported across the inner membrane in exchange with aspartate, transaminated in the matrix to a‐ketoglutarate, which via the ketodicarboxylate carrier is transferred to the cytoplasm, and transaminated to form transmitter glutamate. Such a mechanism would explain the functional role of aspartate aminotransferase in glutamatergic neurons.