In the context of LPS-activated Ms, the expression of Idh1 has been conflicting as various studies have reported its expression to be increased ( 2 with concomitant NADPH production by 10-formyl-THF dehydrogenases ( Since the concentration of NADPH in resting Ms is in the micromolar range ( m s of NADPH-dependent enzymes, such as NOS2 ( t -butyl hydroperoxide, a substrate for glutathione peroxidase, inhibited the production of superoxide (59), which implied that the increased activity of the antioxidative pathway limits the availability of NADPH for the use by oxidative pathways (60)
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