Nitric oxide (II) as a modulator of aldehyde dehydrogenase activity in human erythrocytes

The aim of this work is estimation of effects and its mechanisms of gaseous nitric oxide and dinitrosyl iron complexes (DNIC) on catalytic activity of aldehyde dehydrogenase. We estimated the influence of different doses of free (NO concentration in gas flow – 20, 50, 100 and 800 ppm) and bounded (3 mM of DNIC) nitric oxide on aldehyde dehydrogenase activity and erythrocyte level of malone aldehyde in vitro. It was observed that blood processing with gaseous nitric oxide from different NO-generators caused the moderate inhibition of aldehyde dehydrogenase activity and minimal levation of malonic dialdehyde level. Use of DNIC low doses (lesser than 0,3 mcmol) led to dose-dependent stimulation of enzyme catalytic. Increasing of DNIC dose activated aldehyde dehydrogenase lesser clear, than its low doses. It was stated that erythrocyte aldehyde dehydrogenase is very sensitive to exogenic nitric oxide in gaseous phase and DNIC water solutions. We fixed that modification of aldehyde dehydrogenase activity by nitric oxide is dose dependent.