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Indexed/Abstracted in: EMBASE, Science Citation Index Expanded (SciSearch), Scopus
Impact Factor 0,246
Online ISSN 1827-160X
7th INTERNATIONAL CONFERENCE ON TRANSGLUTAMINASES AND PROTEIN CROSSLINKING REACTIONS
Ferrara (Italy), September 14-17, 2002
Johnson G. V. W., Bailey C. D., Tucholski J., Lesort M.
Department of Psychiatry, University of Alabama at Birmingham School of Medicine, Birmingham, AL, USA
Tissue transglutaminase (tTG), a multifunctional protein, is the most abundant transglutaminase in human brain, and likely to play a role in regulating neuronal function. Tissue TG post-translationally modifies proteins by transamidation of specific glutamine residues. This action results in the incorporation of polyamines into substrate proteins or the formation of protein crosslinks, modifications that likely have significant effects on neuronal function. Tissue TG is a unique member of the transglutaminase family as in addition to catalyzing the calcium-dependent transamidation reaction, it also binds and hydrolyzes GTP and may play a role in signal transduction. Further, binding of guanine nucleotides inhibits the transamidating activity of tTG. Several roles for tTG in neuronal function have been postulated, and there is evidence that tTG may also play a role in apoptosis. Recent findings have provided evidence that dysregulation of tTG may contribute to the pathogenesis of Alzheimer’s disease and Huntington’s disease, and perhaps other neurodegenerative conditions. In both Alzheimer’s and Huntington’s disease tTG and TG activity are elevated compared to age-matched controls. Further, immunohistochemical studies have demonstrated that there is an increase in tTG reactivity in affected neurons in both Alzheimer’s and Hunting-ton’s disease brain. Although intriguing, many questions remain to be addressed to definitively establish a role for tTG in these neurodegenerative diseases.