Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei.

@article{Karpuj1999TransglutaminaseAH,
  title={Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei.},
  author={Marcela Viviana Karpuj and Hideki Garren and Hilda H. Slunt and Donald L. Price and James Gusella and Mark W. Becher and Lawrence Steinman},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 13},
  pages={7388-93}
}
The protein huntingtin (htt), aggregated in neuronal nuclear inclusions, is pathognomonic of Huntington's disease (HD). Constructs, translated in vitro from the N terminus of htt, containing either polyQ23 from a normal individual, or polyQ41 or polyQ67 from an HD patient, were all soluble. Transglutaminase (TGase) crosslinked these proteins, and the aggregations did not have the staining properties of amyloid. More TGase-catalyzed aggregates formed when the polyglutamine domain of htt exceeded… CONTINUE READING