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Possible involvement of transglutaminase-catalyzed reactions in the physiopathology of neurodegenerative diseases

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Abstract

Transglutaminases are ubiquitous enzymes, which catalyze post-translational modifications of proteins. Recently, transglutaminases and tranglutaminase-catalyzed post-translational modification of proteins have been shown to be involved in the molecular mechanisms responsible for several human diseases. Transglutaminase activity has been hypothesized to be involved also in the pathogenetic mechanisms responsible for human neurodegenerative diseases. Neurodegenerative diseases, such as Alzheimer’s disease, Parkinson’s disease, supranuclear palsy, Huntington’s disease and other polyglutamine diseases, are characterized in part by aberrant cerebral transglutaminase activity and by increased cross-linked proteins in affected brains. In this review, we focus on the possible molecular mechanisms by which transglutaminase activity could be involved in the pathogenesis of neurodegenerative diseases, and on the possible therapeutic effects of selective transglutaminase inhibitors for the cure of patients with diseases characterized by aberrant transglutaminase activity.

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Acknowledgments

This work is supported by the Italian Education Department.

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The authors declare that they have no conflict of interest.

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Authors and Affiliations

  1. Department of Biochemistry and Biophysics, Second University of Naples, Via Costantinopoli 16, 80138, Naples, Italy

    Antonio Martin, Alessandro Giuliano, Domenico Collaro, Giulia De Vivo, Carla Sedia, Enrica Serretiello & Vittorio Gentile

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  1. Antonio Martin
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  2. Alessandro Giuliano
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  3. Domenico Collaro
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  4. Giulia De Vivo
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  5. Carla Sedia
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  7. Vittorio Gentile
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Correspondence to Vittorio Gentile.

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Martin, A., Giuliano, A., Collaro, D. et al. Possible involvement of transglutaminase-catalyzed reactions in the physiopathology of neurodegenerative diseases. Amino Acids 44, 111–118 (2013). https://doi.org/10.1007/s00726-011-1081-1

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  • DOI: https://doi.org/10.1007/s00726-011-1081-1

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