Possible Physiopathological Roles of the Transglutaminase Activity in the Etiopathogenesis of Human Neurodegenerative Diseases

ISSN: 2212-3954 (Online)
ISSN: 1574-8898 (Print)


Volume 9, 3 Issues, 2014


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Editor-in-Chief:
Vincenzo Di Marzo
Istituto di Chimica Biomolecolare (I.C.B.)
Consiglio Nazionale delle Ricerche (C.N.R.)
Via Campi Flegrei 34
Pozzuoli, Napoli 80078
Italy


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Possible Physiopathological Roles of the Transglutaminase Activity in the Etiopathogenesis of Human Neurodegenerative Diseases

Author(s): Federica Titta, Martina Iannaccone, Antonio Martin and Vittorio Gentile

Affiliation: Department of Biochemistry, Biophysics and General Pathology, Second University of Naples, via Costantinopoli 16, 80138 Naples, Italy

Abstract

Transglutaminases are ubiquitous enzymes which catalyze post-translational modifications of proteins. The main activity of these enzymes is the cross-linking of glutaminyl residues of a protein/peptide substrate to lysyl residues of a protein/peptide co-substrate. In addition to lysyl residues, other second nucleophilic co-substrates may include monoamines or polyamines (to form mono- or bi-substituted /crosslinked adducts) or –OH groups (to form ester linkages). In the absence of co-substrates, the nucleophile may be water, resulting in the net deamidation of the glutaminyl residue. Transglutaminase activity has been suggested to be involved in molecular mechanisms responsible for both physiological or pathological processes. For example, 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. This review focuses on the possible molecular mechanisms responsible for such diseases and on the possible therapeutic effects of transglutaminase inhibitors for patients with diseases characterized by aberrant transglutaminase activity

Keywords: Cystamine, neurodegenerative diseases, post-translational modifications of proteins, protein aggregation, transglutaminase inhibitors, transglutaminases

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Article Details

Volume: 9
First Page: 1
Last Page: 9
Page Count: 9
DOI: 10.2174/1574889809666140613114850
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