Background
EAAT1, also known as SLC1A3 or GLAST, is a membrane-bound protein localized in glial cells and pre-synaptic glutamatergic nerve endings. It transports the excitatory neurotransmitters L-glutamate and D-aspartate, which is essential for terminating the postsynaptic acction of glutamate. Recently, a correlation between expression/function of glial EAAT-1 and tumor proliferation has been reported. The exceptionally rare expression of EAAT-1 in non-neoplastic choroid plexus (CP) compared to choroid plexus tumors (CPT) may distinguishes neoplastic from normal CP. There are a number of splicing variants of SLC1A3, like GLAST1a and GLAST1b, exist due to the exon skipping. It also undergo glycosylation. Variety of bands can be observed in the western blotting assay: 50-55 kDa represents the unglycosylated GLAST1a or GLAST1b, 65-70 kDa correspond to the glycosylated proteins, larger proteins between 90 - 130 kDa may be the multimers of SLC1A3.
Cellular location
Cell membrane