Does tissue transglutaminase play a role in Huntington's disease?

@article{Lesort2002DoesTT,
  title={Does tissue transglutaminase play a role in Huntington's disease?},
  author={Mathieu J Lesort and Wanjoo Chun and Janusz Tucholski and Gail V. W. Johnson},
  journal={Neurochemistry International},
  year={2002},
  volume={40},
  pages={37-52}
}
Tissue transglutaminase (tTG) likely plays a role in numerous processes in the nervous system. tTG posttranslationally modifies proteins by transamidation of specific polypeptide bound glutamines (Glns). This reaction results in the incorporation of polyamines into substrate proteins or the formation of protein crosslinks, modifications that likely have significant effects on neural function. Huntington's disease is a genetic disorder caused by an expansion of the polyglutamine domain in the… Expand
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TLDR
This review is focused on the function of tTG in celiac disease, although it also deals with novel advances in tTG-based therapies. Expand
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Dissecting the mechanisms of tissue transglutaminase-induced cross-linking of alpha-synuclein: implications for the pathogenesis of Parkinson disease.
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TLDR
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References

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Tissue Transglutaminase Is Increased in Huntington's Disease Brain
TLDR
Tissue transglutaminase is elevated in HD brain and may play a role in the disease process, and quantitative analysis of immunoblots and immunohistochemical and biochemical methods clearly indicate. Expand
Tissue transglutaminase: a possible role in neurodegenerative diseases
TLDR
Evidence that dysregulation of tissue transglutaminase may contribute to the pathology of several neurodegenerative conditions including Alzheimer's disease and Huntington's disease is provided. Expand
Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei.
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  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
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TLDR
TGase-mediated crosslinking of htt may be involved in the formation of the nonamyloidogenic nuclear inclusions found in the HD brain, and the staining properties of nuclear in Included revealed that they were not amyloid. Expand
Tissue Transglutaminase Selectively Modifies Proteins Associated with Truncated Mutant Huntingtin in Intact Cells
TLDR
This study is the first to demonstrate that tTG specifically interacts with a truncated form of huntingtin, and that activated tTG selectively modifies mutant huntingtin-associated proteins. Expand
Tissue Transglutaminase Does Not Contribute to the Formation of Mutant Huntingtin Aggregates
TLDR
In HD, as well as in other polyglutamine diseases, tTG is unlikely to play a role in the formation of aggregates, and does not facilitate the process of aggregate formation. Expand
Transglutaminase action imitates Huntington's disease: selective polymerization of Huntingtin containing expanded polyglutamine.
TLDR
It is shown here that huntingtin is a substrate of transglutaminase in vitro and that the rate constant of the reaction increases with length of the polyglutamine over a range of an order of magnitude. Expand
Impaired Mitochondrial Function Results in Increased Tissue Transglutaminase Activity In Situ
TLDR
It is demonstrated for the first time that impairment of mitochondrial function significantly increases TG activity in situ, a finding that may have important relevance to the etiology of HD. Expand
Tau Is Modified by Tissue Transglutaminase In Situ: Possible Functional and Metabolic Effects of Polyamination
TLDR
Data indicate that tau is likely to be modified physiologically and pathophysiologically by tTG, and tTG may play a role in Alzheimer's disease. Expand
Distinct Nuclear Localization and Activity of Tissue Transglutaminase*
Tissue transglutaminase is a calcium-dependent transamidating enzyme that has been postulated to play a role in the pathology of expanded CAG repeat disorders with polyglutamine expansions expressedExpand
Transglutaminase activity is increased in Alzheimer's disease brain
TLDR
The elevation of transglutaminase in the Alzheimer's disease samples occurred in the prefrontal cortex, where neurofibrillary pathology is usually abundant, and not in the cerebellum, which is usually spared in Alzheimer’s disease, so it can be suggested that transglUTaminase could be a contributing factor in neuro fibrillary tangle formation. Expand
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