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Glutamate and glutamine metabolism in the ovine placenta

Published online by Cambridge University Press:  27 March 2009

Jennifer M. Pell ,
Marjorie K. Jeacock  and
D. A. L. Shepherd
Jennifer M. Pell
Affiliation:
Department of Physiology and Biochemistry, University of Reading, Whiteknights, Reading, RG5 2AJ
Marjorie K. Jeacock
Affiliation:
Department of Physiology and Biochemistry, University of Reading, Whiteknights, Reading, RG5 2AJ
D. A. L. Shepherd
Affiliation:
Department of Physiology and Biochemistry, University of Reading, Whiteknights, Reading, RG5 2AJ
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Summary

The concentration of glutamate and of glutamine was measured in whole blood obtained from a maternal artery, a uterine vein, a foetal artery and an umbilical vein of chronically catherized ewes and foetuses from 100 to 140 days after conception. The activities of glutamate dehydrogenase, phosphate-dependent glutaminase, phosphateindependent glutaminase, glutamine synthetase, γ-glutamyl transferase and glutamine-oxo-acid aminotransferase were measured in placentomes obtained from ewes during a similar period of gestation.

The concentrations of glutamate in blood from maternal vessels remained constant, whereas there was a significant decline (P < 0·001) in the concentration of glutamate in foetal blood. Glutamine concentrations declined significantly (P < 0·05) in maternal blood and in foetal arterial blood (P < 0·001), whereas the concentration of glutamine in umbilical venous blood remained constant.

Mean arterio-venous differences for glutamate indicated that there was no net uptake from or release into maternal blood by the uterus. However, there was a significant (P < 0·02) uptake of glutamate by the placenta from the foetal circulation. Glutamine release from the placenta into the foetal circulation increased as the foetus matured.

Significant activities of glutamate dehydrogenase, γ-glutamyl transferase, glutamine synthetase and phosphate-dependent glutaminase were found in the placenta but there was no significant relationship between the activities of these enzymes and the gestational age of the foetus. The enzyme profile indicated that the placenta has a substantial potential for net glutamine synthesis.

It is concluded that, for a 140-day foetus, the release of glutamine from the placenta accounts for more than half of its nitrogen requirement. Direct placental transfer of glutamine from maternal blood accounts for only one-third of the glutamine released by the placenta into the foetal circulation of a 140-day foetus. Therefore, the remainder of the glutamine is synthesized in the placenta from glutamate. Only one-third of the glutamate required for this placental glutamine synthesis is from the glutamate released by the foetus. The remainder must be derived either from 2-oxoglutarate, as the result of aminotransferase or glutamate dehydrogenase activities, or from glutathione by the action of γ-glutamyl transferase.

Type
Research Article
Information
The Journal of Agricultural Science , Volume 101 , Issue 2 , October 1983 , pp. 275 - 281
Copyright
Copyright © Cambridge University Press 1983

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