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Analysis of posttranslational glycosylation of glutamate receptor subunits in schizophrenia Posttranslational modifications of cellular proteins can influence molecular structure and cellular function. The proteins involved in glutamatergic signaling have been shown to be modified through phosphorylation, glycosylation and ubiquitination which all affect receptor assembly, molecular interactions and degradation. It is therefore of importance also in the study of mental illnesses such as schizophrenia to include posttranslational modifications as a component of cellular function that might be compromised in these conditions. In this study we analyze the glycosylation pattern of AMPA and NMDA receptor subunits in schizophrenia. Differential sensitivity to the deglycosylating enzymes Endo-H and PNGase F allows us to differentiate between processed and unprocessed forms of these proteins. Using this approach, possibly in combination with more sensitive methods such as mass spectrometry (MALDI-TOF), we propose in this project to analyze changes in glycosylation pattern of AMPA and NMDA molecules in postmortem tissue from patients with schizophrenia and matched control subjects.
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