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Mutual regulation between serine and nitric oxide metabolism in human glioblastoma cells

d-Serine indirectly caused dose- and time-dependent inhibition of neuronal nitric oxide synthase (nNOS) without affecting endothelial nitric oxide synthase (eNOS) in human glioblastoma cell line U87. Activity of d-amino acid oxidase (DAAO), catalyzing the oxidative deamination of d-amino acid, was e...

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Bibliographic Details
Published in:Neuroscience letters 2006-02, Vol.394 (3), p.163-167
Main Authors: Shoji, Kazuo, Mariotto, Sofia, Ciampa, Anna Rosa, Suzuki, Hisanori
Format: Article
Language:English
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Summary:d-Serine indirectly caused dose- and time-dependent inhibition of neuronal nitric oxide synthase (nNOS) without affecting endothelial nitric oxide synthase (eNOS) in human glioblastoma cell line U87. Activity of d-amino acid oxidase (DAAO), catalyzing the oxidative deamination of d-amino acid, was enhanced by NO in a dose-dependent manner. Recently, we have reported that serine racemase (SR) is inhibited by NO and activated by d-serine through nitrosylation and denitrosylation, respectively [K. Shoji, S. Mariotto, A.R. Ciampa, H. Suzuki, Regulation of serine racemase activity by d-serine and nitric oxide in human glioblastoma cells, Neurosci. Lett., in press]. Thus, the metabolism of both d-serine and NO in U87 cells is functionally correlated in a complex manner. Suppression of NO production by d-serine in U87 cells contrasts its known action in enhancing nNOS in neurons.
ISSN:0304-3940
1872-7972
DOI:10.1016/j.neulet.2005.10.064