Evidence that Aspartate Aminotransferase Activity and Ketodicarboxylate Carrier Function Are Essential for Biosynthesis of Transmitter Glutamate
- 1 July 1988
- journal article
- research article
- Published by Wiley in Journal of Neurochemistry
- Vol. 51 (1) , 317-320
- https://doi.org/10.1111/j.1471-4159.1988.tb04872.x
Abstract
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 .alpha.-ketoglutarate, which via the ketodicarboxylate carrier is transferred to the cytoplasm, and transminated to form transmitter glutamate. Such a mechanism would explain the functional role of aspartate aminotransferase in glutamatergic neurons.Keywords
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