Tissue transglutaminase-catalyzed formation of high-molecular-weight aggregates in vitro is favored with long polyglutamine domains: a possible mechanism contributing to CAG-triplet diseases.

@article{Gentile1998TissueTF,
  title={Tissue transglutaminase-catalyzed formation of high-molecular-weight aggregates in vitro is favored with long polyglutamine domains: a possible mechanism contributing to CAG-triplet diseases.},
  author={Vincenzo Gentile and Ciro Sepe and Menotti Calvani and Mariarosa A. B. Melone and Roberto Cotrufo and Arthur J. L. Cooper and John P. Blass and Gianfranco Peluso},
  journal={Archives of biochemistry and biophysics},
  year={1998},
  volume={352 2},
  pages={314-21}
}
To investigate possible biochemical mechanisms underlying the "toxic gain of function" associated with polyglutamine expansions, the ability of guinea pig liver tissue transglutaminase to catalyze covalent attachments of various polyamines to polyglutamine peptides was examined. Of the polyamines tested, spermine is the most active substrate, followed by spermidine and putrescine. Formation of covalent cross links between polyglutamine peptides and polyamines yields high-M(r) aggregates--a… CONTINUE READING