Evidence map›Paper›PMID 42555608›Full record

ArticlePloS one2026

The role of transglutaminase 2 in stabilizing fibrin clots and supporting hemostasis.

Paulina Stoklosa, Risa Suzuki, Murielle Golomingi, Bojun Li, Manfred Heller, Kiyotaka Hitomi, Elaissa Trybus Hardy, Wilbur A Lam, Verena Schroeder

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Article in PloS one, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Paulina StoklosaExperimental Haemostasis Research Group, Department for BioMedical Research (DBMR), University of Bern, Bern, Switzerland.
Risa SuzukiExperimental Haemostasis Research Group, Department for BioMedical Research (DBMR), University of Bern, Bern, Switzerland.ORCID https://orcid.org/0000-0001-5470-2815
Murielle GolomingiExperimental Haemostasis Research Group, Department for BioMedical Research (DBMR), University of Bern, Bern, Switzerland.
Bojun LiExperimental Haemostasis Research Group, Department for BioMedical Research (DBMR), University of Bern, Bern, Switzerland.
Manfred HellerProteomics & Mass Spectrometry Core Facility, Department for BioMedical Research (DBMR), University of Bern, Bern, Switzerland.
Kiyotaka HitomiLaboratory of Cellular Biochemistry, Department of Basic Medicinal Sciences, Graduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, Japan.
Elaissa Trybus HardyWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology, Atlanta, United States of America.
Wilbur A LamWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology, Atlanta, United States of America.
Verena SchroederExperimental Haemostasis Research Group, Department for BioMedical Research (DBMR), University of Bern, Bern, Switzerland.ORCID https://orcid.org/0000-0001-6508-3271

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transglutaminases are enzymes with pleiotropic functions in the human body, among them are the A-subunit of coagulation factor XIII (FXIII; FXIII-A) and tissue transglutaminase (TG2). FXIII has a crucial function in clot formation and stabilization. FXIII also contributes to extracellular matrix formation, wound healing and tissue regeneration, a function it shares with TG2. Whether TG2 may also have a role in hemostasis has never been studied in detail. The aim of our project was to study the role of TG2 in clot formation, stabilization and hemostasis. Here, with the use of a microfluidic endothelialized whole blood bleeding model, we detected TG2 and its crosslinking activity at the site of vessel injury, and the addition of exogenous TG2 resulted in its co-localization with the fibrin clot. In turbidimetric clot formation and lysis tests, TG2 delayed clot lysis. Finally, mass-spectrometry and proteomic analyses revealed differences in fibrin chain crosslinking patterns and protein composition of purified and plasma fibrin clots generated in the presence of either FXIII or TG2. Our data suggest that TG2 is present at the site of clot formation upon vessel injury and contributes to fibrin crosslinking and clot stabilization. Hence, TG2 may be able support hemostasis.

Indexed as

Blood CoagulationFibrinGTP-Binding ProteinsHemostasisTransglutaminasesFactor XIIIHumansProtein Glutamine gamma Glutamyltransferase 2Factor XIIIFibrinGTP-Binding ProteinsProtein Glutamine gamma Glutamyltransferase 2Transglutaminases

Identifiers

PMID42555608
PMCPMC13440824

What Socratic holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.