High-affinity binding of proline to mouse brain synaptic membranes.
There is evidence suggestive of the possible neuromodulatory role for L-proline in the mammalian brain. The binding of proline to whole mouse brain synaptic membranes has been partially characterized. Several binding sites for this imino acid have been identified; one in the nanomolar range and at least two in the submicromolar range. The binding of proline is inhibited by NaCl. Pipecolic acid (40 microM), ornithine, aminooxyacetic acid (AOAA), glycine, GABA, and glutamate were capable of significantly inhibiting proline binding. Although detailed pharmacological and functional studies are needed, these results are consistent with a brain-specific function for this imino acid, as well as, with the presence of specific binding site(s) for proline.
Ortiz
J G
JG
Department of Pharmacology, University of Puerto Rico School of Medicine, San Juan 00936.
Negrón
A E
AE
Bruno
M S
MS
D026921:Amino Acid Transport Systems, Neutral; D000818:Animals; D001667:Binding, Competitive; D001921:Brain / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D007700:Kinetics; D051379:Mice; D008810:Mice, Inbred C57BL; D011392:Proline / Q000378:metabolism*; D013570:Synaptic Membranes / Q000378:metabolism*; D013574:Synaptosomes / Q000378:metabolism*
D026921:Amino Acid Transport Systems, Neutral; D002352:Carrier Proteins; C041832:proline transport protein; D011392:Proline