DIFFERENTIAL CELL SURFACE PROTEOMICS OF FLOTILLIN-1, HMGB1 AND AMINOPEPTIDASE IN H3 MUTATED PAEDIATRIC HIGH-GRADE GLIOMA

Abstract AIMS High-grade gliomas (HGG) are the deadliest central nervous system tumour in children. Despite this, treatment options remain elusive, leaving children with a dismal prognosis. Histone H3.3 mutations, K27M and G34V/R have been identified as two most common recurrent somatic mutations paediatric HGG (pHGG). These present 50% of pHGG compared to only 1% adults. Our previous research on cell membrane protein analyses different signature unique proteins H3-G34R/V mutated pHGG, comparison H3 wild type tumour. Among these we flotillin-1, HMGB1 aminopeptidase N. Flotillin-1 promotes numerous malignancies, High mobility group box 1(HMGB1) functions an oncogene N is surface metallo- protease involved progression. We now verified expression localization wildtype tumour, order target them for developing novel therapeutics. METHOD Cell proteomics were further though mass-spectrometric data analyses. Expression Aminopeptidase lines glioma analysed, using assays including immunofluorescence microscopy western blot assays. RESULTS Experimental showed differential Flotillin-1, proteomic H3-G34V wild- pHGG. CONCLUSIONS This new knowledge will help us utilise N, potential therapeutic targets children’s brain tumours.