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Cell BiologyBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
Peer-reviewed journal article

A stagewise response to mitochondrial dysfunction in mitochondrial DNA maintenance disorders

Amy E. VincentiD, Chun CheniD, Tiago M. Bernardino GomesiD, Valeria Di LeoiD, Tuomas LaaloiD, Kamil PabisiD, Rodrick Capaldi, Michael F. Marusich, David McDonaldiD, Andrew J. FilbyiD, Andrew Fuller, Diana Lehmann UrbaniD, Stephan Zierz, Marcus DeschaueriD, Douglass M. TurnbulliD, Amy Katherine ReeveiD, Conor LawlessiD

Abstract

Mitochondrial DNA deletions clonally expand in skeletal muscle of patients with mtDNA maintenance disorders, impairing mitochondrial oxidative phosphorylation dysfunction. Previously we have shown that these mtDNA deletions originally arise and accumulate in the perinuclear mitochondria causing localised mitochondrial dysfunction before spreading through the muscle fibre. We believe that mito-nuclear signalling is a key contributor in this process. To further understand the role of mito-nuclear signalling, we use imaging mass cytometry to characterise the levels of mitochondrial respiratory complexes I-IV and ATP synthase alongside a mitochondrial mass marker, in a cohort of patients with mtDNA maintenance dosirders. We then expanded this panel to include protein markers of key signalling pathways to investigate the cellular response in fibres with different combinations of oxidative phosphorylation dysfunction and in ragged red fibres. We find CI and CIV deficiency to be most common, with a smaller proportion of cells that are also CIII and/or CV deficient. Interestingly, we also note that in cells deficient for one or more complexes, any complexes which are not deficient are commonly upregulated beyond the increase of mitochondrial mass typically observed in ragged red fibres. We further find that oxidative phosphorylation deficient fibres exhibit an increase in abundance of proteins involved in the proteostasis e.g. HSP60 and LONP1, and mitochondrial protein synthesis e.g. PHB1. Our analysis suggests that the cellular response to mitochondrial dysfunction changes depending on the combination of deficient oxidative phosphorylation complexes in each cell.

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