The characteristics of arginine transport by rat cerebellar and cortical synaptosomes
| Autor: | Keith J. Collard, Christian R. Aldridge |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Sodium Acetate
Arginine Biology Tritium Biochemistry Ammonium Chloride Cellular and Molecular Neuroscience chemistry.chemical_compound Cerebellum Extracellular Animals Enzyme Inhibitors Rats Wistar Cerebral Cortex Synaptosome Arginine transport Sodium Biological Transport Depolarization General Medicine Hydrogen-Ion Concentration Membrane transport Rats Kinetics chemistry Potassium Biophysics Calcium Female Nitric Oxide Synthase Veratridine Intracellular Synaptosomes |
| Zdroj: | Neurochemical Research. 21:1539-1546 |
| ISSN: | 1573-6903 0364-3190 |
| DOI: | 10.1007/bf02533103 |
| Popis: | The uptake of L-[3H]arginine into synaptosomes prepared from rat cerebellum and cortex occurred by a high-affinity carrier-mediated process. The uptake of arginine appeared to be potentiated by removal of extracellular Na+, inhibited by high levels of extracellular K+, but not by depolarization with veratridine or 4-amino pyridine. The effect of Na+ removal or K+ elevation did not seem to be due to changes in intracellular Ca2+ or pH. In both brain regions, uptake was significantly inhibited by L-arginine, L-lysine, L-ornithine, and L-homoarginine, but not by D-arginine nor L-citrulline. Uptake was also inhibited by NG-monomethyl-L-arginine acetate, but not by NG-nitro-L-arginine methyl ester nor NG-nitro-L-arginine except in the cortex at a concentration of 1 mM. The results indicate that the carrier system operating in synaptosomes showed many of the characteristics of the ubiquitous y+ system seen in many other tissues, although its apparent sensitivity to variations in extracellular Na+ was unusual. |
| Databáze: | OpenAIRE |
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