Transglutaminase 2 contributes to the blood clotting cascade

Abstract Cross-linking of fibrin and associated proteins via Nε-(γ-glutamyl)lysine bonds in clot formation is a well-established component of the hemodynamic mechanism, providing clot rigidity and reducing the rate of fibrinolysis. The latter effect occurs predominantly through the incorporation of fibrinolytic inhibitors. To date, this function has been attributed exclusively to Factor XIIIa, also known as plasma transglutaminase (TG), one of eight identified in mammals. In this report, we demonstrate that tissue transglutaminase (TG2), a ubiquitous enzyme abundantly present in erythrocytes, also contributed to clot stabilisation. We observed clear differences between whole thrombi isolated from TG2-deficient and wild-type mice. Similarly, human thrombi were more stable in the presence of TG2 than when TG2 activity is specifically inhibited, revealing a previously unrecognized role for this enzyme in haemostasis. Therefore, we propose TG2 as an additional factor involved in blood coagulation.

Authors

Institutions

Publication Details

Journal
Cell Death Discovery
Published
2026-10-17
DOI
https://doi.org/10.1038/s41420-026-03388-1
Primary Topic
Blood properties and coagulation
Type
article
Field-Weighted Citation Impact
0.00

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Transglutaminase 2 contributes to the blood clotting cascade

Nicola J. Mutch, Mauro Piacentini, Mara Mancini, Manuel Scimeca et al.
Cell Death Discovery
Blood properties and coagulation
article

Transglutaminase 2 contributes to the blood clotting cascade

Nicola J. Mutch, Mauro Piacentini, Mara Mancini, Manuel Scimeca, Gerry Melino, Martin Griffin, Eleonora Candi, Alessandro Mauriello, Valerio Da Ros, Zhuo Wang, Yufang Shi, Francesco Barilla’
article en

Abstract

Abstract Cross-linking of fibrin and associated proteins via Nε-(γ-glutamyl)lysine bonds in clot formation is a well-established component of the hemodynamic mechanism, providing clot rigidity and reducing the rate of fibrinolysis. The latter effect occurs predominantly through the incorporation of fibrinolytic inhibitors. To date, this function has been attributed exclusively to Factor XIIIa, also known as plasma transglutaminase (TG), one of eight identified in mammals. In this report, we demonstrate that tissue transglutaminase (TG2), a ubiquitous enzyme abundantly present in erythrocytes, also contributed to clot stabilisation. We observed clear differences between whole thrombi isolated from TG2-deficient and wild-type mice. Similarly, human thrombi were more stable in the presence of TG2 than when TG2 activity is specifically inhibited, revealing a previously unrecognized role for this enzyme in haemostasis. Therefore, we propose TG2 as an additional factor involved in blood coagulation.

Cell Death Discovery
University of Rome Tor Vergata (IT), Aston University (GB), University of Aberdeen (GB), Soochow University (CN), The Fourth Affiliated Hospital of Soochow University (Suzhou Dushu Lake Hospital)
European Commission, Associazione Italiana per la Ricerca sul Cancro, NextGenerationEU
Good health and well-being
Openalex Percentile: Top 12%
Blood properties and coagulation
DOIOpen Access PDFOpenAlex
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.