Abstract
Dysfunctions of the F(1)F(o)-ATPase complex cause severe mitochondrial diseases affecting primarily the paediatric population. While in the maternally inherited ATPase defects due to mtDNA mutations in the ATP6 gene the enzyme is structurally and functionally modified, in ATPase defects of nuclear origin mitochondria contain a decreased amount of otherwise normal enzyme. In this case biosynthesis of ATPase is down-regulated due to a block at the early stage of enzyme assembly-formation of the F(1) catalytic part. The pathogenetic mechanism implicates dysfunction of Atp12 or other F(1)-specific assembly factors. For cellular energetics, however, the negative consequences may be quite similar irrespective of whether the ATPase dysfunction is of mitochondrial or nuclear origin.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Adenosine Triphosphatases / genetics
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Animals
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Cell Nucleus / enzymology
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Cell Nucleus / metabolism
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DNA, Mitochondrial / genetics
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DNA, Mitochondrial / metabolism
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Fibroblasts / metabolism
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Humans
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Mitochondria / enzymology
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Mitochondrial Diseases / enzymology
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Mitochondrial Diseases / genetics*
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Mitochondrial Proton-Translocating ATPases / biosynthesis
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Mitochondrial Proton-Translocating ATPases / deficiency
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Mitochondrial Proton-Translocating ATPases / genetics*
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Mutation
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Reactive Oxygen Species / analysis
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Reactive Oxygen Species / metabolism
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Vacuolar Proton-Translocating ATPases / genetics*
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Vacuolar Proton-Translocating ATPases / metabolism
Substances
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DNA, Mitochondrial
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MT-ATP6 protein, human
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Reactive Oxygen Species
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Adenosine Triphosphatases
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Vacuolar Proton-Translocating ATPases
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Mitochondrial Proton-Translocating ATPases