Abstract
Although the mutated protein causing Huntington's disease (HD) is expressed throughout the body, the major pathology of HD is localized to the striatum of the brain. We previously reported that the striatal-enriched protein Rhes binds the mutated huntingtin protein and enhances its cytotoxicity. We now demonstrate that Rhes-deleted mice are dramatically protected from neurotoxicity and motor dysfunction in a striatal-specific model of HD elicited by 3-nitropropionic acid. This finding suggests that Rhes may, in part, determine the striatal selectivity of HD.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Disease Models, Animal
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Exploratory Behavior / drug effects
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Exploratory Behavior / physiology
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GTP-Binding Proteins / deficiency*
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Huntington Disease / chemically induced*
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Huntington Disease / genetics
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Huntington Disease / metabolism*
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Mice
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Mice, Inbred C57BL
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Mice, Knockout
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Neurotoxins / toxicity*
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Nitro Compounds / toxicity*
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Propionates / toxicity*
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Psychomotor Performance / drug effects
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Succinate Dehydrogenase / metabolism
Substances
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Neurotoxins
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Nitro Compounds
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Propionates
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Succinate Dehydrogenase
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GTP-Binding Proteins
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Rasd2 protein, mouse
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3-nitropropionic acid