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N ε ‐(γ‐ l ‐Glutamyl)‐ l ‐lysine (GGEL) is increased in cerebrospinal fluid of patients with Huntington's disease
Author(s) -
Jeitner Thomas M.,
Bogdanov Mikhail B.,
Matson Wayne R.,
Daikhin Yevgeny,
Yudkoff Marc,
Folk John E.,
Steinman Lawrence,
Browne Susan E.,
Beal M. Flint,
Blass John P.,
Cooper Arthur J. L.
Publication year - 2001
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.2001.00673.x
Subject(s) - tissue transglutaminase , huntington's disease , huntingtin , cerebrospinal fluid , lysine , in vivo , huntingtin protein , microbiology and biotechnology , pathological , enzyme , brain tissue , chemistry , pathology , biology , biochemistry , medicine , disease , genetics , amino acid
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 ε ‐(γ‐ 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 .