Loading…
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...
Saved in:
Published in: | Neuroscience letters 2006-02, Vol.394 (3), p.163-167 |
---|---|
Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
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 |