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The binding of glutamate to glutamate receptors reconstituted in liposomes of different phospholipid composition


, : The binding of glutamate to glutamate receptors reconstituted in liposomes of different phospholipid composition. Biologicheskie Membrany (Moscow) 12(3): 303-309

The binding of 3H-L-glutamate to affinity-purified glutamate binding proteins (GBP) from rat brain was studied after reconstitution in liposomes of different phospholipid composition. It was shown that the amount of GBP inserted in the liposomal membrane under reconstitution did not depend on the phospholipid composition of liposomes. The specific binding activity of GBP after reconstitution in liposomes from any of the used phospholipids - phosphatidylcholine (PC), phosphatidylethanolamine (PEA), phosphatidylserine (PS), phosphatidylinositol (PI) - was higher than of GBP in buffer solution. The maximal binding activity was exhibited by GBP reconstituted in liposomes from PC or PEA. The mixture of PC and PEA (1:1) was as effective as PC or PEA alone in reconstituting ligand binding; however, when PI was also included in the mixture, there was a pronounced increase in binding (about 2-fold compared to the PC:PEA mixture and about 10-fold compared to GBP in buffer solution). Addition of PS instead of PI to the PC : PEA mixture did not have the same effect. The most effective reconstitution of GBP was reached at the ratio of lipids : proteins 1000:1. GBP reconstituted in liposomes from PC : PEA : PI revealed the binding constant that was similar to those observed for native membranes isolated from rat brain. The results suggest that at the environment of PC, PEA and PI in membrane GBP has an optimal conformation for the interaction with L-glutamate.

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