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The World of Transglutaminases: From Basic Biological and Medical Research to Applied Sciences 3.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (15 July 2023) | Viewed by 6953

Special Issue Editors

Dr. Ivana Caputo

E-Mail Website
Guest Editor
Department of Chemistry and Biology, University of Salerno, Via Giovanni Paolo II, 132, 84084 Fisciano, SA, Italy
Interests: tissue transglutaminase (tTG); anti-tTG antibodies and gliadin peptides in celiac disease; effects of pollutants; chemicals and bioactive compounds in cell and animal models
Special Issues, Collections and Topics in MDPI journals
Dr. Gaetana Paolella

E-Mail Website
Guest Editor
Department of Chemistry and Biology, University of Salerno, via Giovanni Paolo II 132, 84084 Fisciano, SA, Italy
Interests: transglutaminase and anti-tTG in celiac disease; interplay between transglutaminase and gliadin peptides in celiac disease; modulation of cell functions by environmental polluttants; phosphoproteomics; miRNA
Special Issues, Collections and Topics in MDPI journals
Dr. Stefania Martucciello

E-Mail Website
Guest Editor
Department of Chemistry and Biology, University of Salerno, via Giovanni Paolo II 132, 84084, Fisciano, SA, Italy
Interests: anti-tissue transglutaminase and angiogenesis in celiac disease; modulation of tTG function by autoantibodies; cell stress and human diseases; TBX1 gene function in angiogenesis and lymphangiogenesis in mouse models; molecular mechanisms of bioactive compounds from plants
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Transglutaminases are important protein-modifying enzymes that are distributed in all kingdoms of life. The post-translational modifications catalyzed by these enzymes produce stable networks in the extracellular matrix, in body fluids, and inside cells, thus contributing to the regulation of many aspects of cell life and death. Besides the cross-linking function, other enzymatic reactions and non-enzymatic functions can be attributed to some members of the transglutaminase family. In this regard, the ubiquitous multi-functional tissue transglutaminase has been nicknamed "the bete noire" of the family or "a molecular swiss army knife." Evidence on the involvement of transglutaminases in human diseases, such as cancer, fibrosis, and neurodegenerative and autoimmune diseases, is rapidly increasing. Moreover, transglutaminases have been successfully employed as biotechnological tools in several industrial fields.

The aim of this Special Issue is to collect original and review articles on all aspects of research on the transglutaminases family, from basic research to biomedical and biotechnological applications.

Suggested topics include, but are not limited to:

  • Transglutaminases in bacteria, plants, and other lower, non-mammalian organisms;
  • The discovery of novel transglutaminases;
  • Mammalian transglutaminases—new functions for old enzymes;
  • The thousand faces of the tissue transglutaminase;
  • Transglutaminases in human diseases;
  • Transglutaminases as therapeutic targets;
  • Transglutaminases as biotechnological tools.

Dr. Ivana Caputo
Dr. Gaetana Paolella
Dr. Stefania Martucciello
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

 

Related Special Issues

Published Papers (3 papers)

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Research

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11 pages, 2548 KiB  
Article
ATO Increases ROS Production and Apoptosis of Cells by Enhancing Calpain-Mediated Degradation of the Cancer Survival Protein TG2
by Károly Jambrovics, Szilárd Póliska, Beáta Scholtz, Iván P. Uray and Zoltán Balajthy
Int. J. Mol. Sci. 2023, 24(13), 10938; https://doi.org/10.3390/ijms241310938 - 30 Jun 2023
Cited by 2 | Viewed by 1256
Abstract
Transglutaminase 2 (TG2) is a critical cancer cell survival factor that activates several signalling pathways to foster drug resistance, cancer stem cell survival, metastasis, inflammation, epithelial-mesenchymal transition, and angiogenesis. All-trans retinoic acid (ATRA) and chemotherapy have been the standard treatments for acute promyelocytic [...] Read more.
Transglutaminase 2 (TG2) is a critical cancer cell survival factor that activates several signalling pathways to foster drug resistance, cancer stem cell survival, metastasis, inflammation, epithelial-mesenchymal transition, and angiogenesis. All-trans retinoic acid (ATRA) and chemotherapy have been the standard treatments for acute promyelocytic leukaemia (APL), but clinical studies have shown that arsenic trioxide (ATO), alone or in combination with ATRA, can improve outcomes. ATO exerts cytotoxic effects in a variety of ways by inducing oxidative stress, genotoxicity, altered signal transduction, and/or epigenetic modification. In the present study, we showed that ATO increased ROS production and apoptosis ratios in ATRA-differentiated NB4 leukaemia cells, and that these responses were enhanced when TG2 was deleted. The combined ATRA + ATO treatment also increased the amount of nuclear factor erythroid 2-related factor 2 (NRF2) transcription factor, an adaptive regulator of the cellular oxidative stress response, and calpain proteolytic activity, resulting in TG2 degradation and the reduced survival of WT leukaemia cells. We further showed that the induced TG2 protein expression was degraded in the MCF-7 epithelial cell line and primary peripheral blood mononuclear cells upon ATO treatment, thereby sensitising these cell types to apoptotic signals. Full article
(This article belongs to the Special Issue The World of Transglutaminases: From Basic Biological and Medical Research to Applied Sciences 3.0)
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14 pages, 2470 KiB  
Article
Inhibition of Transglutaminase 2 as a Therapeutic Strategy in Celiac Disease—In Vitro Studies in Intestinal Cells and Duodenal Biopsies
by Sebastian Stricker, Jan de Laffolie, Klaus-Peter Zimmer and Silvia Rudloff
Int. J. Mol. Sci. 2023, 24(5), 4795; https://doi.org/10.3390/ijms24054795 - 01 Mar 2023
Cited by 1 | Viewed by 1822
Abstract
Enzymatic modification of gliadin peptides by human transglutaminase 2 (TG2) is a key mechanism in the pathogenesis of celiac disease (CD) and represents a potential therapeutic target. Recently, we have identified the small oxidative molecule PX-12 as an effective inhibitor of TG2 in [...] Read more.
Enzymatic modification of gliadin peptides by human transglutaminase 2 (TG2) is a key mechanism in the pathogenesis of celiac disease (CD) and represents a potential therapeutic target. Recently, we have identified the small oxidative molecule PX-12 as an effective inhibitor of TG2 in vitro. In this study, we further investigated the effect of PX-12 and the established active-site directed inhibitor ERW1041 on TG2 activity and epithelial transport of gliadin peptides. We analyzed TG2 activity using immobilized TG2, Caco-2 cell lysates, confluent Caco-2 cell monolayers and duodenal biopsies from CD patients. TG2-mediated cross-linking of pepsin-/trypsin-digested gliadin (PTG) and 5BP (5-biotinamidopentylamine) was quantified by colorimetry, fluorometry and confocal microscopy. Cell viability was tested with a resazurin-based fluorometric assay. Epithelial transport of promofluor-conjugated gliadin peptides P31-43 and P56-88 was analyzed by fluorometry and confocal microscopy. PX-12 reduced TG2-mediated cross-linking of PTG and was significantly more effective than ERW1041 (10 µM, 15 ± 3 vs. 48 ± 8%, p < 0.001). In addition, PX-12 inhibited TG2 in cell lysates obtained from Caco-2 cells more than ERW1041 (10 µM; 12 ± 7% vs. 45 ± 19%, p < 0.05). Both substances inhibited TG2 comparably in the intestinal lamina propria of duodenal biopsies (100 µM, 25 ± 13% vs. 22 ± 11%). However, PX-12 did not inhibit TG2 in confluent Caco-2 cells, whereas ERW1041 showed a dose-dependent effect. Similarly, epithelial transport of P56-88 was inhibited by ERW1041, but not by PX-12. Cell viability was not negatively affected by either substance at concentrations up to 100 µM. PX-12 did not reduce TG2 activity or gliadin peptide transport in confluent Caco-2 cells. This could be caused by rapid inactivation or degradation of the substance in the Caco-2 cell culture. Still, our in vitro data underline the potential of the oxidative inhibition of TG2. The fact that the TG2-specific inhibitor ERW1041 reduced the epithelial uptake of P56-88 in Caco-2 cells further strengthens the therapeutic potential of TG2 inhibitors in CD. Full article
(This article belongs to the Special Issue The World of Transglutaminases: From Basic Biological and Medical Research to Applied Sciences 3.0)
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Review

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23 pages, 3542 KiB  
Review
Transglutaminase in Foods and Biotechnology
by Katja Vasić, Željko Knez and Maja Leitgeb
Int. J. Mol. Sci. 2023, 24(15), 12402; https://doi.org/10.3390/ijms241512402 - 03 Aug 2023
Cited by 5 | Viewed by 3243
Abstract
Stabilization and reusability of enzyme transglutaminase (TGM) are important goals for the enzymatic process since immobilizing TGM plays an important role in different technologies and industries. TGM can be used in many applications. In the food industry, it plays a role as a [...] Read more.
Stabilization and reusability of enzyme transglutaminase (TGM) are important goals for the enzymatic process since immobilizing TGM plays an important role in different technologies and industries. TGM can be used in many applications. In the food industry, it plays a role as a protein-modifying enzyme, while, in biotechnology and pharmaceutical applications, it is used in mediated bioconjugation due to its extraordinary crosslinking ability. TGMs (EC 2.3.2.13) are enzymes that catalyze the formation of a covalent bond between a free amino group of protein-bound or peptide-bound lysine, which acts as an acyl acceptor, and the γ-carboxamide group of protein-bound or peptide-bound glutamine, which acts as an acyl donor. This results in the modification of proteins through either intramolecular or intermolecular crosslinking, which improves the use of the respective proteins significantly. Full article
(This article belongs to the Special Issue The World of Transglutaminases: From Basic Biological and Medical Research to Applied Sciences 3.0)
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