Abstract
Overexpression of the UCP3 gene in both murine and human myotube cell cultures leads to a significant activation of the different proteolytic systems involved in muscle myofibrillar protein breakdown. Thus, lysosomal (cathepsin B) and non-lysosomal (m-calpain and ubiquitin-proteasome) mRNA content was significantly increased in the different cell culture systems used. Interestingly, the overexpression of the UCP3 gene was not associated with any changes in apoptosis. Although the function of the UCP3 protein is not completely understood (uncoupling, oxidative stress), these results suggest a possible relation between these main mechanisms involved in muscle wasting during cancer.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Calpain / biosynthesis
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Carrier Proteins / biosynthesis*
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Cathepsin B / biosynthesis
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Cells, Cultured
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Enzyme Activation
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Gene Expression
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Humans
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Ion Channels
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Mice
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Mitochondrial Proteins
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Muscle Fibers, Skeletal / metabolism*
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Muscular Atrophy / etiology*
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Muscular Atrophy / physiopathology
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Neoplasms / complications
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Peptide Hydrolases / metabolism*
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Proteasome Endopeptidase Complex / biosynthesis
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Transfection
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Uncoupling Protein 3
Substances
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Carrier Proteins
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Ion Channels
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Mitochondrial Proteins
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UCP3 protein, human
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Ucp3 protein, mouse
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Uncoupling Protein 3
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Peptide Hydrolases
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Calpain
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m-calpain
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Cathepsin B
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Proteasome Endopeptidase Complex