physiological oxygen levels. In our previous study, we found changes in the lipidome that signified mitochondrial changes. Several mitochondrial proteins were elevated (fold change >2) in high oxygen conditions, including proteins that are part of the electron transport chain complex III, IV and V, superoxide dismutase and proteins involved in cell metabolism. SDH is present in complex II of the electron transport chain and its protein levels were not altered by oxygen. However, its activity showed a negative correlation with oxygen levels in monolayer cultures of chondrocytes. MALDI-MSI followed by LDA was used to identify oxygen induced changes in metabolites. Amongst others, we could identify adenosine triphosphate (ATP), adenosine diphosphate (ADP) and adenosine monophosphate (AMP). Conclusions: Using multimodal mass spectrometry approaches, we show that human chondrocytes have a distinct, oxygen-dependent molecular profile. These changes in the lipidome, metabolome and proteome signify changes in mitochondria and may be a sign of elevated levels of ROS in high oxygen conditions. These mitochondrial changes may explain why chondrocytes perform poorly and lose their phenotype in supraphysiological oxygen levels and cartilage degenerative disease Targeting these mitochondrial changes may restore the balance between anabolic and catabolic activities and thereby halt cartilage degeneration.
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