Abstract
The mev-1(kn1) mutation of Caenorhabditis elegans is in Cyt-1, which encodes a subunit of succinate-coenzyme Q oxidoreductase in the mitochondrial electron transport chain. Mutants are hypersensitive to oxidative stress and age precociously in part because of increased superoxide anion production. Here, we show that mev-1 mutants are defective in succinate-coenzyme Q oxidoreductase, possess ultrastructural mitochondrial abnormalities (especially in muscle cells), show a loss of membrane potential, have altered CED-9 and Cyt-1 protein levels under hyperoxia, and contain ced-3-and ced-4-dependent supernumerary apoptotic cells. These defects likely explain the failure of mev-1 to complete embryonic development under hyperoxia as well as its reduced life span.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aging*
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Animals
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Antibodies, Monoclonal / metabolism
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Apoptosis Regulatory Proteins
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Apoptosis*
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Blotting, Western
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Caenorhabditis elegans
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Caenorhabditis elegans Proteins / metabolism*
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Calcium-Binding Proteins / metabolism*
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Caspases / metabolism*
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Cytochromes / genetics*
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Cytochromes b*
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Hypoxia
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Immunohistochemistry
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Membrane Potentials
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Microscopy, Electron
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Microscopy, Fluorescence
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Mitochondria / metabolism*
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Models, Biological
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Mutation
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Oxygen / metabolism
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Proto-Oncogene Proteins / metabolism
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Proto-Oncogene Proteins c-bcl-2
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Time Factors
Substances
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Antibodies, Monoclonal
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Apoptosis Regulatory Proteins
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Caenorhabditis elegans Proteins
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Calcium-Binding Proteins
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Ced-4 protein, C elegans
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Ced-9 protein, C elegans
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Cytochromes
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MEV-1 protein, C elegans
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Proto-Oncogene Proteins
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Proto-Oncogene Proteins c-bcl-2
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Cytochromes b
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Caspases
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ced-3 protein, C elegans
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Oxygen