Interactions among mitochondrial proteins altered in glioblastoma

• DOI: 10.1007/s11060-014-1430-5
• Publication Date: 2014-04-12T06:47:14Z
• Authors: Ruth F. Deighton; Thierry Le Bihan; Sarah F. Martin; Alice M. J. Gerth; Mailis McCulloch; Julia M. Edgar; Lorraine E. Kerr; Ian R. Whittle; James McCulloch
• Keywords: Peroxiredoxin; Mitochondrial respiratory chain

Mitochondrial dysfunction is putatively central to glioblastoma (GBM) pathophysiology but there has been no systematic analysis in GBM of the proteins which are integral mitochondrial function. Alterations enriched fractions from patients with were defined label-free liquid chromatography mass spectrometry. 256 mitochondrially-associated identified and 117 these markedly (fold-change ≥2) significantly altered (p ≤ 0.05). Proteins associated oxidative damage (including catalase, superoxide dismutase 2, peroxiredoxin 1 4) increased GBM. Protein–protein interaction highlighted a reduction multiple coupled energy metabolism (in particular respiratory chain proteins, including 23 complex-I proteins). Qualitative ultrastructural electron microscopy showed notably higher prevalence mitochondria cristolysis This study highlights complex proteomic adjustments occur pathophysiology.