Serine transhydroxymethylase activity in vertebrate retina.

The presence of serine transhydroxymethylase (STHM; EC 2.1.2.1) in crude homogenates of rat, guinea pig and goat retina has been demonstrated. There was a variation in the levels of retinal STHM activity in the three species. Substantial STHM activity was found in all the three retinal preparations in the absence of pyridoxal-5-phosphate in the incubation medium. There was direct correlation (r = 0.995; p less than 0.001) between the STHM activity and the glycine content in rat telencephalon, midbrain, medulla-pons, spinal cord and retina. These findings suggest that STHM is probably an important enzyme for the synthesis of neural glycine in the vertebrate retina.

Action of oxotremorine on the sub-cellular distribution of glycine in the rat spinal cord.

Intraperitoneal (i.p.) injection of 250 micrograms/kg of oxotremorine (OT) caused a 50% decrease in the glycine content of the synaptosomal-mitochondrial fraction of spinal cord homogenates prepared from rats killed 15 min after treatment. The glycine content of the supernatant fraction was correspondingly raised. In synaptosomes isolated from the spinal cord of OT-treated rats, the decrease in glycine content was 30%. Prior administration of atropine, but not of methylatropine, abolished this effect of OT on synaptosomal glycine content. Eserine exerted a potentiating effect on the action of OT in lowering the glycine content of spinal synaptosomes. Prior administration of L-DOPA, apomorphine, haloperidol, muscarine or mecamylamine had no significant effect on the action of OT on synaptosomal glycine content. OT alone or in combination with eserine, and acetylcholine (ACh) in combination with eserine, did not alter the rate of release of glycine from spinal synaptosomes of untreated rats incubated under appropriate conditions. OT was also without effect on the rate of release of glycine from normal spinal synaptosomes subjected to electrical stimulation, as well as on the eventual glycine content of the synaptosomes. On the basis of the present findings it has been suggested that (i) glycine may be released from Renshaw cells at their synapses with motoneurones in response to the muscarinic action of OT; (ii) dopaminergic modulation may not be involved in the OT-induced glycine release from Renshaw cells; and (iii) excessive release of glycine onto motoneurones may be the causative factor of the akinesia observed in OT-induced experimental Parkinsonism.

Glyoxylate aminotransferase activity in vertebrate retina.

Glyoxylate aminotransferase activity with L-glutamate, L-glutamine and L-alanine as substrates, has been estimated in rat, guinea pig and goat retinae. Enhanced enzyme activity was found in the presence of Triton X-100. The presence of significant aminotransferase activity raises a possibility of glyoxylate as a precursor of glycine in vertebrate retina.