Journal
JOURNAL OF NEURO-ONCOLOGY
Volume 118, Issue 2, Pages 247-256Publisher
SPRINGER
DOI: 10.1007/s11060-014-1430-5
Keywords
Glioblastoma; Mitochondria; Clinical proteomics
Categories
Funding
- Melville Trust
- Brain Tumour Research Fund
- Synthsys
- BBSRC
- EPSRC [BB/D019621/1]
- BBSRC [BB/D019621/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D019621/1] Funding Source: researchfish
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Mitochondrial dysfunction is putatively central to glioblastoma (GBM) pathophysiology but there has been no systematic analysis in GBM of the proteins which are integral to mitochondrial function. Alterations in proteins in mitochondrial enriched fractions from patients with GBM were defined with label-free liquid chromatography mass spectrometry. 256 mitochondrially-associated proteins were identified in mitochondrial enriched fractions and 117 of these mitochondrial proteins were markedly (fold-change a parts per thousand yen2) and significantly altered in GBM (p a parts per thousand currency sign 0.05). Proteins associated with oxidative damage (including catalase, superoxide dismutase 2, peroxiredoxin 1 and peroxiredoxin 4) were increased in GBM. Protein-protein interaction analysis highlighted a reduction in multiple proteins coupled to energy metabolism (in particular respiratory chain proteins, including 23 complex-I proteins). Qualitative ultrastructural analysis in GBM with electron microscopy showed a notably higher prevalence of mitochondria with cristolysis in GBM. This study highlights the complex mitochondrial proteomic adjustments which occur in GBM pathophysiology.
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