Article date: October 1994
By: Gethin J. McBean, in Volume 113, Issue 2, pages 536-540
The effect of the gliotoxic analogue of glutamate, ocaminoadipate, on the high affinity transport of D‐[3H]‐aspartate into a crude striatal P2 preparation, and on the activity of two enzymes of which glutamate is the substrate has been examined.
The L‐isomer of ocaminoadipate competitively inhibited the transport protein, with a Ki value of 192 μm, whereas the D‐isomer of ocaminoadipate was ineffective. The potent convulsant, L‐methionine‐S‐sulphoximine, was also without effect on the activity of the gluatmate transport protein.
L‐αAminoadipate was a competitive inhibitor of both glutamine synthetase, and γ‐glutamylcysteine synthetase, with Ki values of 209 μm and 7 mm respectively. Once again, the D‐isomer of ocaminoadipate was a far weaker inhibitor of either enzyme.
The results are discussed in terms of the mechanism of action of ocaminoadipate in causing toxicity of glial cells.
The effect of the gliotoxic analogue of glutamate, ocaminoadipate, on the high affinity transport of D‐[3H]‐aspartate into a crude striatal P2 preparation, and on the activity of two enzymes of which glutamate is the substrate has been examined.
The L‐isomer of ocaminoadipate competitively inhibited the transport protein, with a Ki value of 192 μm, whereas the D‐isomer of ocaminoadipate was ineffective. The potent convulsant, L‐methionine‐S‐sulphoximine, was also without effect on the activity of the gluatmate transport protein.
L‐αAminoadipate was a competitive inhibitor of both glutamine synthetase, and γ‐glutamylcysteine synthetase, with Ki values of 209 μm and 7 mm respectively. Once again, the D‐isomer of ocaminoadipate was a far weaker inhibitor of either enzyme.
The results are discussed in terms of the mechanism of action of ocaminoadipate in causing toxicity of glial cells.
DOI: 10.1111/j.1476-5381.1994.tb17022.x
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