title: The cellular energy crisis: mitochondria and cell death.
abstract: Exploding nuclear reactors, environmental destruction, and global warming; the danger of energy production is clear. It is quite remarkable that in this modern age, where power usage is at a premium, we find that even on a cellular level, generation of large quantities of power comes at a cost. Mitochondria, which produce the majority of cellular energy in the form of ATP, have recently been shown to play an essential role in the death of a cell by a process known as apoptosis. During apoptosis, the integrity of mitochondria is compromised and various pro-apoptotic proteins are released into the cytoplasm. This results in activation of caspases, proteases that orchestrate the death of the cell. Cells in which apoptosis is inhibited upstream of mitochondria generally maintain the potential to proliferate, whereas inhibition of caspases downstream of mitochondria generally only delays cell death. Although breaches of the mitochondrial outer membrane result in the release of proteins that are important for respiration, mitochondria appear capable of maintaining at least some of their functions, including ATP production, even after this event. This has important implications both for the mechanism of outer-membrane permeabilization and the mechanism by which the cells eventually die in the absence of caspase activity. The events surrounding the breach of the mitochondrial outer membrane during apoptosis have therefore received much interest over the past few years.
authors.affiliation: Cancer Immunology Research, Peter MacCallum Cancer Institute, Melbourne, Australia. nigelwaterhouse@hotmail.com
authors.forename: Nigel J
authors.initials: NJ
authors.lastname: Waterhouse
mesh_terms: D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D020169:Caspases / Q000502:physiology; D003574:Cytochrome c Group / Q000502:physiology; D004734:Energy Metabolism / Q000502:physiology; D006801:Humans; D008565:Membrane Proteins / Q000502:physiology; D008928:Mitochondria / Q000378:metabolism / Q000502:physiology*; D024101:Mitochondrial Proteins / Q000378:metabolism; D011518:Proto-Oncogene Proteins / Q000502:physiology; D019253:Proto-Oncogene Proteins c-bcl-2 / Q000502:physiology; D050998:bcl-2 Homologous Antagonist-Killer Protein; D051028:bcl-2-Associated X Protein
chemical_list: C494772:BAK1 protein, human; D003574:Cytochrome c Group; D008565:Membrane Proteins; D024101:Mitochondrial Proteins; D011518:Proto-Oncogene Proteins; D019253:Proto-Oncogene Proteins c-bcl-2; D050998:bcl-2 Homologous Antagonist-Killer Protein; D051028:bcl-2-Associated X Protein; D020169:Caspases