Abstract
Transglutaminases (TGs, E.C. 2.3.2.13) are 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. These enzymes are also capable of catalyzing other reactions which are important for cell life. To date, at least eight different human TGs have been identified. The distribution and the physiological roles of human TGs have been widely studied in numerous cell types and tissues and recently their roles in several diseases have begun to be identified. It has been hypothesized that transglutaminase activity is directly involved in the patho-genetic mechanisms responsible for several human diseases. In particular, TG2, a member of the TG enzyme family, has been shown to be involved in the molecular mechanisms responsible for a very widespread human pathology, Celiac Disease (CD), one of the most common food intolerances described in the western population. The main food agent that provokes the strong and diffuse clinical symptoms has been known for several years to be gliadin, a protein present in a very large number of human foods derived from vegetables. The aim of this review is to summarize the most recent findings concerning the relationships between the biochemical properties of the transglutaminase activity and the basic molecular mechanisms responsible for CD. In addition, we present some clinical associations of CD with other human diseases, with particular reference to neuropsychiatric disorders. Possible molecular links between biochemical activities of transglutaminase enzymes, CD and neuropsychiatric disorders are discussed.
Keywords: Celiac disease, enzyme inhibitors, gene expression, neuropsychiatric disorders, post-translational modifications of proteins, transglutaminases, glutaminyl residue, gliadin, transamidating activity, transglutaminase enzymes
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