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

Authors
Type
Published Article
Journal
Amino Acids
0939-4451
Publisher
Springer-Verlag
Publication Date
Volume
44
Issue
1
Pages
111–118
Identifiers
DOI: 10.1007/s00726-011-1081-1
PMID: 21938398
Source
Medline

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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