Abstract

Glioblastoma multiform is a primary brain tumor derived from glial cells. The aim of this study is to investigate how glutamate metabolism is regulated by glutamate transporter 1 (GLT-1) degradation pathway in glioblastoma and glial cell lines. The protein expression levels of GLT-1, total ubiquitin, protein kinase C (PKC) proteins involved in the GLT-1 degradation pathway were measured by the western blot technique. Additionally, in glial and glioblastoma cells, the level of glutamate accumulated in the medium and the lysates was measured with the glutamate assay. GLT-1 protein expression was increased significantly in glioblastoma cells. The expression levels of the PKC protein and total ubiquitin were found to be decreased in glioblastoma cells although not significantly. The glutamate accumulated in the medium and lysates of glioblastoma cells is reduced compared to glial cells. Further research regarding excitotoxicity in glioblastoma focusing on GLT-1 degradation or activation pathway may create new opportunities of drug and treatment development.

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