Transglutaminase 2 and Cellular Functions

Dear Colleagues,

Transglutaminase type 2 (TG2) is a calcium-dependent enzyme, ubiquitously expressed belonging to the transglutaminase family (EC 2.3.2.13). TG2 catalyzes specific post-translational modifications of proteins through a transamidation reaction. It is also involved in various additional enzymatic activities, such as guanine nucleotide binding and hydrolysis, protein kinase, and disulfide isomerase activities.

TG2 is a widely studied enzyme and the greater the understanding of it the more new implications emerge. Since 2000, over 2400 papers have demonstrated that TG2 plays a central role in several biological mechanisms and cellular functions, such as cell proliferation, apoptosis, and differentiation in various cell types. The protein itself as well as its enzymatic activity are determining factors for the proliferation and invasion of tumor cells, and for the response of the tumor to chemotherapy. It was implicated in a growing variety of altered health states, not just celiac disease, but also neurodegenerative diseases, multiple sclerosis, and central nervous system injuries, among others.

The knowledge of the mechanisms through which TG2 participates in the various cellular functions, in particular those that trigger apoptosis or pathogenesis, could allow the design of future therapeutic applications. In this regard, the study of the biological effects of modulating molecules of the enzymatic activity of TG2 and/or of the effectors that are part of the cascade of events triggered arouses enormous interest. For example, biogenic polyamines, which act as natural substrates, have been shown to limit, and in some cases block, the enzymatic activity of TG2, resulting in possible use to reduce the onset of pathologies, such as senile cataracts.

Based on these premises, this monograph aims to broaden the knowledge of TG2 in health conditions and pathological states and the cellular functions in which it is involved. Studies that clarify the molecular mechanisms triggered by TG2, and also those focused on the identification of possible natural or synthetic modulators of the TG2 activity, are particularly welcome.

You may choose our Joint Special Issue in International Journal of Molecular Sciences.

Prof. Dr. Carlo Mischiati
Prof. Dr. Simone Beninati
Guest Editors

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