ijms-logo

Journal Browser

Journal Browser

Special Issue "The World of Transglutaminases: From Basic Biological and Medical Research to Applied Sciences 2.0"

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

Deadline for manuscript submissions: 31 March 2022.

Special Issue Editors

Prof. 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
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
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.

Prof. 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 papers will be 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 Issue

Published Papers (2 papers)

Order results
Result details
Select all
Export citation of selected articles as:

Research

Article
Biochemical Characterisation of Human Transglutaminase 4
Int. J. Mol. Sci. 2021, 22(22), 12448; https://doi.org/10.3390/ijms222212448 - 18 Nov 2021
Viewed by 382
Abstract
Transglutaminases are protein-modifying enzymes involved in physiological and pathological processes with potent therapeutic possibilities. Human TG4, also called prostate transglutaminase, is involved in the development of autoimmune and tumour diseases. Although rodent TG4 is well characterised, biochemical characteristics of human TG4 that could [...] Read more.
Transglutaminases are protein-modifying enzymes involved in physiological and pathological processes with potent therapeutic possibilities. Human TG4, also called prostate transglutaminase, is involved in the development of autoimmune and tumour diseases. Although rodent TG4 is well characterised, biochemical characteristics of human TG4 that could help th e understanding of its way of action are not published. First, we analysed proteomics databases and found that TG4 protein is present in human tissues beyond the prostate. Then, we studied in vitro the transamidase activity of human TG4 and its regulation using the microtitre plate method. Human TG4 has low transamidase activity which prefers slightly acidic pH and a reducing environment. It is enhanced by submicellar concentrations of SDS suggesting that membrane proximity is an important regulatory event. Human TG4 does not bind GTP as tested by GTP-agarose and BODIPY-FL-GTPγS binding, and its proteolytic activation by dispase or when expressed in AD-293 cells was not observed either. We identified several potential human TG4 glutamine donor substrates in the AD-293 cell extract by biotin-pentylamine incorporation and mass spectrometry. Several of these potential substrates are involved in cell–cell interaction, adhesion and proliferation, suggesting that human TG4 could become an anticancer therapeutic target. Full article
Show Figures

Figure 1

Article
Transamidation Down-Regulates Intestinal Immunity of Recombinant α-Gliadin in HLA-DQ8 Transgenic Mice
Int. J. Mol. Sci. 2021, 22(13), 7019; https://doi.org/10.3390/ijms22137019 - 29 Jun 2021
Viewed by 810
Abstract
Enzymatic transamidation of gliadins by microbial transglutaminase (mTG) inhibits interferon-γ (IFN-γ) secretion by intestinal T cell lines in patients with celiac disease (CD). To gain insight into the cellular mechanisms underlying the down-regulatory effects of transamidation, we tested a single recombinant α-gliadin (r-gliadin) [...] Read more.
Enzymatic transamidation of gliadins by microbial transglutaminase (mTG) inhibits interferon-γ (IFN-γ) secretion by intestinal T cell lines in patients with celiac disease (CD). To gain insight into the cellular mechanisms underlying the down-regulatory effects of transamidation, we tested a single recombinant α-gliadin (r-gliadin) harbouring two immunodominant peptides, p13 (aa. 120–139) and p23 (aa. 220–239), in HLA-DQ8 transgenic mice, a model of gluten sensitivity. Mice were intranasally immunised with r-gliadin or r-gliadin transamidated by mTG (K-r-gliadin) along with cholera toxin, and the response of mesenteric lymph node cells was analysed by cytokine multiplex assay. An in vitro challenge with r-gliadin was characterised by secretion of specific cytokines featuring both innate immunity and the Th1/Th2/Th17 pattern of the adaptive response. Notably, transamidation specifically down-regulated the Th1 response. Structural studies performed on K-r-gliadin confirmed that specific glutamine residues in p13 and p23, previously found to be deamidated by tissue transglutaminase, were also transamidated by mTG. In silico analysis, simulating p13 and p23 peptide binding to HLA-DQ8 showed that these glutamines, in the form of glutamate, could interact by means of salt bridges with peculiar amino acids of the alpha chain of HLA-DQ8, suggesting that their transamidation may influence the HLA-restricted recognition of these peptides. Thus, the structural findings provided a rationale to explain the down-regulation of the r-gliadin-specific Th1 response following transamidation. Full article
Show Figures

Figure 1

Back to TopTop