Micromolar calcium stimulates proteolysis and glutamate binding in rat brain synaptic membranes.
Incubation of cortical synaptic membranes with low concentrations of calcium resulted in a decrease in the amount of a high-molecular-weight doublet protein and an increase in the sodium-independent binding of glutamate. Both effects were blocked by the thiol protease inhibitor leupeptin. These results suggest that calcium-induced proteolysis of membrane components regulates the number of glutamate receptors in neuronal membranes.
D000818:Animals; D002118:Calcium / Q000037:antagonists & inhibitors / Q000494:pharmacology*; D002531:Cerebellum / Q000378:metabolism; D002540:Cerebral Cortex / Q000378:metabolism; D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000378:metabolism*; D005971:Glutamates / Q000378:metabolism*; D007976:Leupeptins / Q000494:pharmacology; D008565:Membrane Proteins / Q000378:metabolism*; D008970:Molecular Weight; D051381:Rats; D013570:Synaptic Membranes / Q000378:metabolism*
D005971:Glutamates; D007976:Leupeptins; D008565:Membrane Proteins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D002118:Calcium