Inhibition of protein carboxylmethylation and dopamine autoreceptor functioning.

S-Adenosyl-L-homocysteine (SAH, 2-100 microM) greatly inhibited protein carboxymethylation (PCM) in rat striatal synaptosomes, but did not alter the ability of apomorphine and other DA agonists to inhibit DA synthesis. SAH (10 microM) also did not significantly alter the ability of either 0.5 or 1.0 microM apomorphine to inhibit DA release from superfused rat striatal tissue slices, but it did antagonize the response to 5.0 microM apomorphine. The former two concentrations of apomorphine predominantly affected only DA release, whereas the latter concentration suppressed both DA and acetylcholine release. These findings are discussed with regard to the possible relationship between DA autoreceptor functioning and PCM activity.