Ion fluxes associated with excitatory amino acid transport

Abstract

Flux of substrate and charge mediated by three cloned excitatory amino acid transporters widely expressed in human brain were studied in voltage-clamped Xenopus oocytes. Superfusion of L-glutamate or D-aspartate resulted in currents due in part to electrogenic Na+ cotransport, which contributed 1 net positive charge per transport cycle. A significant additional component of the currents was due to activation of a reversible anion flux that was not thermodynamically coupled to amino acid transport. The selectivity sequence of this ligand-activated conductance was NO3- > 1- > Br- > Cl- > F-. The results suggest that these proteins mediate both transporter- and channel-like modes of permeation, providing a potential mechanism for dampening cell excitability, in addition to removal of transmitter.