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Basic information of Nos2 :

Official Symbol of Gene Nos2
Species Mus musculus
Entrez Gene ID 18126
Official Full Name nitric oxide synthase 2, inducible
Also known as iNOS; Nos-2; Nos2a; i-NOS; NOS-II; MAC-NOS
Gene Type protein coding
dbXrefs Ensembl:ENSMUSG00000020826 AllianceGenome:MGI:97361
Map Location 11 B5; 11 46.74 cM

Sample information of multiple sclerosis:

Detected Sample brain
Sample Detail Neonate Astrocytes
Detected Method immunoblot analysis
Disease stroke, multiple sclerosis, Parkinson’s disease, and HIV dementia
Disease subtype N/A
Population N/A
Sample Size n = 5–6 mice group

Literature information of multiple sclerosis :

Pubmed ID 12655043
Year 2002
Title Translational control of inducible nitric oxide synthase expression by arginine can explain the arginine paradox

Results of multiple sclerosis :

Expression up-regulation
Risk type Disease risk
Result we demonstrate that, as expected, iNOS activity in astrocytes is governed by arginine transported into the cell from the extracellular medium. Unexpectedly, however, we found that arginine concentration not only regulates NO production by limiting availability of substrate for iNOS, it also regulates iNOS expression via translational control of iNOS mRNA
Mechanism/Pathway inhibition of iNOS activity by arginine depletion in stimulated astrocyte cultures occurs via inhibition of translation of iNOS mRNA. After stimulation by cytokines, uptake of L-arginine negatively regulates the phosphorylation status of the eukaryotic initiation factor (eIF2a), which, in turn, regulates translation of iNOS mRNA. eIF2a phosphorylation correlates with phosphorylation of the mammalian homolog of yeast GCN2 eIF2a kinase. As the kinase activity of GCN2 is activated by phosphorylation, these findings suggest that GCN2 activity represents a proximal step in the iNOS translational regulation by availability of L-arginine. These results provide an explanation for the arginine paradox for iNOS and define a distinct mechanism by which a substrate can regulate the activity of its associated enzyme