| Literature DB >> 19664996 |
Andreas Weiss1, Dorothée Abramowski, Miriam Bibel, Ruth Bodner, Vanita Chopra, Marian DiFiglia, Jonathan Fox, Kimberly Kegel, Corinna Klein, Stephan Grueninger, Steven Hersch, David Housman, Etienne Régulier, H Diana Rosas, Muriel Stefani, Scott Zeitlin, Graeme Bilbe, Paolo Paganetti.
Abstract
The genetic mutation causing Huntington's disease is a polyglutamine expansion in the huntingtin protein where more than 37 glutamines cause disease by formation of toxic intracellular fragments, aggregates, and cell death. Despite a clear pathogenic role for mutant huntingtin, understanding huntingtin expression during the presymptomatic phase of the disease or during disease progression has remained obscure. Central to clarifying the role in the pathomechanism of disease is the ability to easily and accurately measure mutant huntingtin in accessible human tissue samples as well as cell and animal models. Here we describe a highly sensitive time-resolved Förster resonance energy transfer (FRET) assay for quantification of soluble mutant huntingtin in brain, plasma, and cerebrospinal fluid. Surprisingly, in mice, soluble huntingtin levels decrease during disease progression, inversely correlating with brain aggregate load. Mutant huntingtin is easily detected in human brain and blood-derived fractions, providing a utility to assess mutant huntingtin expression during disease course as well as a pharmacodynamic marker for disease-modifying therapeutics targeting expression, cleavage, or degradation of mutant huntingtin. The design of the homogeneous one-step method for huntingtin detection is such that it can be easily applied to measure other proteins of interest.Entities:
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Year: 2009 PMID: 19664996 DOI: 10.1016/j.ab.2009.08.001
Source DB: PubMed Journal: Anal Biochem ISSN: 0003-2697 Impact factor: 3.365