1998 Fiscal Year Final Research Report Summary
MOLECULAR PHARMACOLOGICAL STUDIES ON MECHANISMS ASSOCIATED WITH NEUROMODULATION BY GLUTATHIONE
| Project/Area Number |
09670111
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
General pharmacology
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| Research Institution | SETSUNAN UNIVERSITY |
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Principal Investigator |
OGITA Kiyokazu SETSUNAN UNIVERSITY,DEPARTMENT OF PHARMACOLOGY,LECTURER, 薬学部, 講師 (90169219)
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| Project Period (FY) |
1997 – 1998
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| Keywords | GLUTATHIONE / NEUROMODULATOR / GLUTAMIC ACID / TRANSCRIPTION FACTOR / ACTIVATOR PROTEINN-1 / KINIC ACID / GLUTATHIONE DEPLETOR / GLUTATHIONE BINDING PROTEIN |
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| Research Abstract |
In vitro addition of glutathione did not significantly affect uptake of [^3H]-glutamic (Glu) and [^3H] gamma-aminobutyrrc (GABA) acids into rat synaptosomal fractions at a concentration range of up to 1 mM These results suggest that glutathione plays no physiological role in transport systems of Glu and GABA into neuronal and/or glial cells. On the other hand, an intraperitoneal injection of kainic acid (KA) at a subconvulsive low dose markedly potentiated DNA binding ac tivity of the transcription factor activator protein-l (APl) in the hippocampus of mice with reduced contents of brain endogenous gluthatione following a previous injection of the glutathione depletor 2-cyclohexen-l-one, without markedly affecting that in animals previously injected with saline alone. However, the depletor did not significantly modulate the potentiation of APl DNA binding by the administration of N-methyl-D-aspartic acid (NMDA) in murine hippocampus. The data cited here raise the possibility that endogenous glutathione may play a critical role in mechanisms underlying signaling cascade through KA, but not NMDA,receptors to nuclear AP1 in murine hippocampus. Moreover, several membrane proteins with different molecular weights were isolated from porcine brains following column chromatography using affinity resins immobilized with glutathione.
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