Protein-peptide based assay for the characterization of human blood coagulation factor XIII-A isopeptidase activity

Csobán-Szabó, Zsuzsa; Fésüs, László; Király, Róbert

doi:10.1016/j.ab.2020.113699

Cited by 2 publications

(2 citation statements)

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“…Transglutaminases (TGs) comprise a family of nine multifunctional isoenzymes named TG1-7, blood coagulation factor XIII, and Band 4.2 [ 1 , 2 , 3 , 4 , 5 , 6 ]. First described by Waelsch in 1957, transglutaminase type 2 (TG2) is ubiquitously expressed and catalyzes calcium (Ca 2+ )-dependent post-translational protein transamidation.…”

Section: Introductionmentioning

confidence: 99%

“…Among the members of the TG family, TG2 is the most abundant and well-characterized transglutaminase in mammals [ 7 ] and is expressed in all cellular districts (nucleus, cytosol, and organelles), as well as in the extracellular environment [ 5 , 8 , 9 ]. While it retains strong sequence homology in its catalytic site [ 10 ] compared to other members of the transglutaminase family, TG2 has structural peculiarities that establish its uniqueness, making it a versatile protein [ 11 ] (see Figure 1 ).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The Role of Transglutaminase 2 in Cancer: An Update

Zaltron,

Vianello,

Ruzza

et al. 2024

IJMS

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Transglutaminase type 2 (TG2) is the most ubiquitously expressed and well characterized member of the transglutaminase family. It is a ubiquitous multifunctional enzyme implicated in the regulation of several cellular pathways that support the survival, death, and general homeostasis of eukaryotic cells. Due to its multiple localizations both inside and outside the cell, TG2 participates in the regulation of many crucial intracellular signaling cascades in a tissue- and cell-specific manner, making this enzyme an important player in disease development and progression. Moreover, TG2 is capable of modulating the tumor microenvironment, a process of dynamic tissue remodeling and biomechanical events, resulting in changes which influence tumor initiation, growth, and metastasis. Even if generally related to the Ca2+-dependent post-translational modification of proteins, a number of different biological functions have been ascribed to TG2, like those of a peptide isomerase, protein kinase, guanine nucleotide binder, and cytosolic–nuclear translocator. With respect to cancer, TG2′s role is controversial and highly debated; it has been described both as an anti- and pro-apoptotic factor and is linked to all the processes of tumorigenesis. However, numerous pieces of evidence support a tissue-specific role of TG2 so that it can assume both oncogenic and tumor-suppressive roles.

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