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Proteomics reveals differential protein regulation in human glioma cells by imipramine
In the majority of psychiatric disorders, little is known about cellular dysfunction and mechanisms by which antipsychotics act. Proteomics provides a method to investigate the regulation of the complex cellular protein pattern (proteome), which is of increasing interest in clinical neuroscience (1).
To investigate the influence of antipsychotics on proteome, we cultured human glioblastoma cells (86HG39) for two month with 10µM imipramine. Cells were harvested and after the extraction of the total amount of protein analysed by two-dimensional gel electrophoresis.
Our experiments reveal clear differences in respect to the number of protein spots and the amount of comparable proteins. Changes in protein pattern were expected because an increase of clozapine transport was measured after long-term incubation with imipramine (unpublished data). Further analysis by mass spectroscopy for identification of proteins and the adjustment of the protein pattern with databases are necessary to identify the proteins specially regulated by antipsychotic drugs.
(1) Rohlff, C. Int J Neuropsychopharmacol 4(1) (2001) 93–102