N(epsilon)-(gamma-L-glutamyl)-L-lysine (GGEL) is increased in cerebrospinal fluid of patients with Huntington's disease. Academic Article uri icon

Overview

abstract

  • Pathological-length polyglutamine (Q(n)) expansions, such as those that occur in the huntingtin protein (htt) in Huntington's disease (HD), are excellent substrates for tissue transglutaminase in vitro, and transglutaminase activity is increased in post-mortem HD brain. However, direct evidence for the participation of tissue transglutaminase (or other transglutaminases) in HD patients in vivo is scarce. We now report that levels of N(epsilon)-(gamma-L-glutamyl)-L-lysine (GGEL)--a 'marker' isodipeptide produced by the transglutaminase reaction--are elevated in the CSF of HD patients (708 +/- 41 pmol/mL, SEM, n = 36) vs. control CSF (228 +/- 36, n = 27); p < 0.0001. These data support the hypothesis that transglutaminase activity is increased in HD brain in vivo.

publication date

  • December 1, 2001

Research

keywords

  • Dipeptides
  • Huntington Disease

Identity

Scopus Document Identifier

  • 0034747325

Digital Object Identifier (DOI)

  • 10.1046/j.1471-4159.2001.00673.x

PubMed ID

  • 11739625

Additional Document Info

volume

  • 79

issue

  • 5