| Title | γ-Glutamylamines and neurodegenerative diseases. |
| Publication Type | Journal Article |
| Year of Publication | 2013 |
| Authors | Jeitner TM, Battaile K, Cooper AJL |
| Journal | Amino Acids |
| Volume | 44 |
| Issue | 1 |
| Pagination | 129-42 |
| Date Published | 2013 Jan |
| ISSN | 1438-2199 |
| Keywords | Amines, Animals, Dipeptides, gamma-Glutamylcyclotransferase, Glutamine, Humans, Lysine, Neurodegenerative Diseases, Protein Processing, Post-Translational, Transglutaminases |
| Abstract | Transglutaminases catalyze the formation of γ-glutamylamines utilizing glutamyl residues and amine-bearing compounds such as lysyl residues and polyamines. These γ-glutamylamines can be released from proteins by proteases in an intact form. The free γ-glutamylamines can be catabolized to 5-oxo-L-proline and the free amine by γ-glutamylamine cyclotransferase. Free γ-glutamylamines, however, accumulate in the CSF and affected areas of Huntington Disease brain. This observation suggests transglutaminase-derived γ-glutamylamines may play a more significant role in neurodegeneration than previously thought. The following monograph reviews the metabolism of γ-glutamylamines and examines the possibility that these species contribute to neurodegeneration. |
| DOI | 10.1007/s00726-011-1209-3 |
| Alternate Journal | Amino Acids |
| PubMed ID | 22407484 |
| PubMed Central ID | PMC3491119 |
| Grant List | P01 AG014930 / AG / NIA NIH HHS / United States 2P01 AG14930 / AG / NIA NIH HHS / United States |
Related Institute:
Molecular Imaging Innovations Institute (MI3)
