Abstract
Transglutaminases (TGs) expression and enzymatic activities in human saliva were investigated. Specific antibodies showed the co-existence of TG1, TG2, TG3 and TG4. TG2 and TG3 were found in native and multiple proteolytic forms. Our data indicate that TG1 and TG2 isoenzymes are highly active with the major activity attributed to TG1. These findings pave the way for future studies on the physiological role of TG in the oral cavity and the potential impact of their deregulation in TG-associated oral diseases.
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Acknowledgments
The authors gratefully acknowledge the financial support of the Marie Curie Action RTN program “Transglutaminase: role in pathogenesis, diagnosis and therapy” (TRACKS, MRTN-CT-2008-36032) and the Marie Curie Industry-Academia partnerships and pathways programme “TRANSCOM” (IAPP-251506) We knowledge Dr. Kiyotaka Hitomi for kindly providing the peptides pepT26(E), and pepK5(E) and Dr. Kim In-Gyu for the interesting discussion on saliva. We also thank all the participants in this study.
Conflict of interest
S. El Alaoui and V. Thomas have a financial relationship with the organization that sponsored this research. M. Perez Alea and G. Martin declare to not have financial relationship with the organization that sponsored the research. The authors declare that they have not conflict of interest.
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Perez Alea, M., Thomas, V., Martin, G. et al. Identification of human salivary transglutaminases. Amino Acids 44, 245–250 (2013). https://doi.org/10.1007/s00726-011-1142-5
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DOI: https://doi.org/10.1007/s00726-011-1142-5