Enzymes in the 100 000g supernatant fraction of guinea-pig lungs, in the presence of NAD-+, converted PGF-2 α (prostaglanding F-2 α) into a less-polar compound. The u.v. spectrum of this metabolite showed a strong absorption band at 230 nm, which is characteristic of a carbonyl group in conjugation with a double bond. Reduction of this metabolite with NaBH4 resulted in a compound that behaved like PGF2 α on t.l.c. and g.l.c. From this evidence we concluded that PGF2α is metabolized in vitro to 15-oxo-PGF2 α by the NAD-+-dependent prostaglandin dehydrogenase system of guinea-pig lung. The effect of exposure of the animal to SO-2 and O2 on the rate of prostaglanding biosynthesis and catabolism by lung fractions in vitro was studied. Exposure of guinea pigs to 500 p.m. of SO2 for 5h or to 50p.p.m for 9 days (6h/day) did not alter the production or degradation of prostaglandings by lung fractions in vitro. In contrast, exposure of guinea pigs to 100%O2 for 48 h inhibited the rate of prostaglanding metabolism in vitro by 60-70% without significantly altering the rate of biosynthesis by lung fractions. Inhibition of prostaglandin dehydrogenase activity in vitro by lung fractions after exposure of the animal to O2 was dependent on the duration of exposure. Gluthathione S-aryltransferase and catechol O-methyltransferase activites of guinea-pig lung 100 000g supernatant were unaltered by exposure of the animal to O2. Thus it appears that inhibition of pulmonary prostaglandin dehydrogenase by exposure of the animal to O2 is not the result of a general tox;ic response. It was postulated that the inhibition of prostaglanding dehydrogenase may occur after exposure of the animal to other oxidant gases.
- © 1975 London: The Biochemical Society