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Since we found no link between ALDH2-catalyzed GTN metabolism and mitochondrial nitrite reduction (Kollau A., Beretta M. & Mayer B.; unpublished), we investigated the possibility that an activator of sGC is produced directly in the course of ALDH2 reaction by co-incubation of purified human ALDH2 with purified sGC in the presence of GTN. In the absence of ALDH2, GTN had no effect on sGC activity (0.28 ± 0.07 μmol/mg/min). In the presence of 25 μg of ALDH2 there was a biphasic stimulation of cGMP formation with an EC50 (half-maximally effective concentration) of ~1 μM GTN and a maximum at 10 μM GTN (1.66 ± 0.22 μmol/mg/min). The effect of ALDH2 was dependent on the protein concentration, with a linear increase from 1 to 100 μg (2.10 ± 0.23 μmol/ mg/min) and saturation between 100 and 250 μg of ALDH2. ALDH2-dependent sGC activation was inhibited by 1 mM chloral hydrate (41.5% of control) and by 100 μM daidzin (18.9% of control). The effect of ALDH2 on cGMP formation was almost completely inhibited by the NO scavenger oxy-haemoglobin, the superoxide generator flavin adenine dinucleotide, and the heme site sGC inhibitor ODQ (0.1 mM, each).

Activation of soluble guanylate cyclase in the presence of purified human aldehyde dehydrogenases