Publications by authors named "D M Glerum"

Article Synopsis
  • Inherited defects in cytochrome oxidase (COX) are linked to various diseases that disrupt the mitochondrial respiratory chain, which is vital for energy production in cells.
  • COX is a complex enzyme made up of 14 subunits and requires the interaction of around 30 proteins for proper assembly, with yeast studies being crucial in identifying mutations and understanding their implications.
  • Recent advancements in genome sequencing have allowed for the discovery of new COX assembly factors, highlighting the need for functional studies to clarify the role of genetic variants in COX deficiencies, while yeast remains a key model for exploring these defects.
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Genetic defects in the nuclear encoded subunits and assembly factors of cytochrome c oxidase (mitochondrial complex IV) are very rare and are associated with a wide variety of phenotypes. Biallelic pathogenic variants in the COX11 protein were previously identified in two unrelated children with infantile-onset mitochondrial encephalopathies. Through comprehensive clinical, genetic and functional analyses, here we report on a new patient harboring novel heterozygous variants in , presenting with Leigh-like features, and provide additional experimental evidence for a direct correlation between COX11 protein expression and sensitivity to oxidative stress.

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The terminal electron acceptor of most aerobic respiratory chains, cytochrome c oxidase (COX), has been highly conserved throughout evolution, from aerobic prokaryotes to complex eukaryotes. Oxygen metabolism in parasitic helminths differs significantly from that of most aerobic eukaryotes, as these organisms can switch between aerobic and anaerobic metabolisms throughout their life cycles. Early studies suggested a lack of COX activity in certain parasitic helminths, and the role of COX in helminth mitochondria remains unclear.

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Tissues and organs consist of cells organized in specified patterns that support their function, as exemplified by tissues such as skin, muscle, and cornea. It is, therefore, important to understand how external cues, such as engineered surfaces or chemical contaminants, can influence the organization and morphology of cells. In this work, we studied the impact of indium sulfate on human dermal fibroblast (GM5565) viability, production of reactive oxygen species (ROS), morphology, and alignment behavior on tantalum/silicon oxide parallel line/trench surface structures.

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Article Synopsis
  • Cell adhesion plays a crucial role in biological processes like division, migration, signaling, and tissue development, and can be affected by nanometer-scale surface structures.
  • The study investigated how indium chloride influences human dermal fibroblast adherence and morphology by using advanced imaging techniques.
  • Results indicated that exposure to indium chloride significantly decreased the alignment of cells along a nanopattern and altered their mitochondrial structure, highlighting the negative effects of indium compounds on cell behavior.
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