TY - JOUR
T1 - Rhes deletion is neuroprotective in the 3-nitropropionic acid model of Huntington's disease
AU - Mealer, Robert G.
AU - Subramaniam, Srinivasa
AU - Snyder, Solomon H.
PY - 2013/2/27
Y1 - 2013/2/27
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84874610368&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84874610368&partnerID=8YFLogxK
U2 - 10.1523/JNEUROSCI.3730-12.2013
DO - 10.1523/JNEUROSCI.3730-12.2013
M3 - Article
C2 - 23447628
AN - SCOPUS:84874610368
SN - 0270-6474
VL - 33
SP - 4206
EP - 4210
JO - Journal of Neuroscience
JF - Journal of Neuroscience
IS - 9
ER -