Transglutaminase Biology

Dear Colleagues,

Transglutaminases are a family of enzymes which catalyze the crosslinking of proteins, linking the epsilon group of a lysine residue in one protein to the carboxyl group of a glutamine residue in a second protein. Identified in plants, microbes and animals, transglutaminases are involved in a diverse range of biological functions. They find industrial usage in the food industry, with multiple applications as gelling and binding agents. In vivo, transglutaminase activity promotes formation of barriers, stabilises structures such as blood clots, and supports wound healing. Transglutaminases have also been shown to modify intracellular and extracellular proteins, and promote protein aggregate formation in a range of pathological states including neurodegenerative diseases, celiac disease and cancer. In recent years, transglutaminase inhibitors have progressed into clinical trials, with encouraging results - particularly in patients with celiac disease and kidney fibrosis - likely to support efforts to expand the potential of this approach into other conditions linked to aberrant transglutaminase activity. This special issue will focus on the biology of the transglutaminase enzyme family, and the potential in targeting these enzymes for the treatment of a diverse range of transglutaminase-linked conditions.

Guest Editor Dr. Nicholas Peake Sheffield Hallam University, UK