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LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics
Published on: April 9, 2017
Transglutaminases and neurodegeneration
Thomas M Jeitner1, John T Pinto, Boris F Krasnikov
1Red Anvil, LLC, Milwaukee, Wisconsin, USA.
Journal of Neurochemistry
|April 28, 2009
Summary
Transglutaminases (TGs) are enzymes implicated in neurodegenerative diseases like Alzheimer's. Inhibiting TG activity shows promise as a therapeutic strategy for these conditions.
Area of Science:
- Neurobiology
- Enzymology
Background:
- Transglutaminases (TGs) are calcium-dependent enzymes catalyzing modifications of glutaminyl residues.
- In the brain, TGs covalently attach compounds like polyamines and lysyl residues, regulating enzyme activity and substrate binding.
- Aberrant TG activity is linked to neurodegenerative diseases, including Alzheimer, Parkinson, and Huntington diseases.
Purpose of the Study:
- To review the role of transglutaminases in neurodegenerative diseases.
- To discuss the potential of selective TG inhibitors as therapeutic agents.
Main Methods:
- Literature review of studies on transglutaminases and neurodegenerative diseases.
- Analysis of therapeutic strategies targeting transglutaminase activity.
Main Results:
- Transglutaminase dysregulation is implicated in the pathogenesis of several neurodegenerative disorders.
- Intervention strategies targeting TGs have demonstrated efficacy in animal models of Huntington and Parkinson diseases.
Conclusions:
- Transglutaminases are significant contributors to neurodegeneration.
- Selective transglutaminase inhibitors represent a promising therapeutic avenue for treating neurodegenerative diseases.
