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.
journal_name
Neuronjournal_title
Neuronauthors
Wadiche JI,Amara SG,Kavanaugh MPdoi
10.1016/0896-6273(95)90159-0subject
Has Abstractpub_date
1995-09-01 00:00:00pages
721-8issue
3eissn
0896-6273issn
1097-4199pii
0896-6273(95)90159-0journal_volume
15pub_type
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