Role of the transglutaminase enzymes in the nervous system and their possible involvement in neurodegenerative diseases

Current Medicinal Chemistry
G De VivoV Gentile

Abstract

Transglutaminases are a large family of related and ubiquitous enzymes which catalyze the cross linking of a glutaminyl residue of a protein/peptide substrate to a lysyl residue 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 absence of co-substrates, the nucleophile may be water, resulting in the net deamidation of the glutaminyl residue. These enzymes are also capable of catalyzing other reactions important for cell viability. The distribution and the physiological roles of human transglutaminases have been widely studied in numerous cell types and tissues and their roles in several diseases have begun to be identified. Recently, "tissue" transglutaminase (TG2) has been shown to be involved in the molecular mechanisms responsible for a very widespread human pathology, celiac disease (CD). Transglutaminase activity has also been hypothesized to be directly involved in the pathogenetic mechanisms responsible for several human neurodegenerative diseases, which are characterized in part by aberrant cerebral transglutaminase activity and by ...Continue Reading

Citations

May 4, 2012·Cellular and Molecular Neurobiology·Toshihiko SuzukiHiroyuki Ichikawa
Jul 10, 2010·Journal of Neuroinflammation·Shaheen E Lakhan, Annette Kirchgessner
Dec 15, 2010·Analytical Biochemistry·Johannes WolfThomas Mothes
Apr 21, 2011·Autism Research : Official Journal of the International Society for Autism Research·Allen RosenspireAnthony R Torres
Feb 5, 2014·Bioarchitecture·Yuyu Song, Scott T Brady
Jul 1, 2016·Somatosensory & Motor Research·Naoya HashimotoHiroyuki Ichikawa
Mar 17, 2020·World Journal of Microbiology & Biotechnology·N DotiM Ruvo

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