| Title | N(epsilon)-(gamma-L-glutamyl)-L-lysine (GGEL) is increased in cerebrospinal fluid of patients with Huntington's disease. |
| Publication Type | Journal Article |
| Year of Publication | 2001 |
| Authors | Jeitner TM, Bogdanov MB, Matson WR, Daikhin Y, Yudkoff M, Folk JE, Steinman L, Browne SE, Beal MF, Blass JP, Cooper AJ |
| Journal | J Neurochem |
| Volume | 79 |
| Issue | 5 |
| Pagination | 1109-12 |
| Date Published | 2001 Dec |
| ISSN | 0022-3042 |
| Keywords | Adult, Chromatography, Liquid, Dipeptides, Electrochemistry, Female, Humans, Huntington Disease, Male, o-Phthalaldehyde, Radioisotope Dilution Technique, Transglutaminases |
| 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. |
| DOI | 10.1046/j.1471-4159.2001.00673.x |
| Alternate Journal | J Neurochem |
| PubMed ID | 11739625 |
| Grant List | P01 AG14930 / AG / NIA NIH HHS / United States |
Related Institute:
Molecular Imaging Innovations Institute (MI3)