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Biomolecules
Special Issues
Transglutaminases: Regulation, Imaging, and Applications
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Transglutaminases: Regulation, Imaging, and Applications

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Enzymology".

Deadline for manuscript submissions: 15 July 2024 | Viewed by 622

Special Issue Editor

Dr. Thomas M. Jeitner

E-Mail Website
Guest Editor
Department of Radiology, Weill Cornell Medicine, New York, NY 10065, USA
Interests: transglutaminase 2; protein-glutamine gamma-glutamyltransferase; metabolism; aging; protein structure and function

Special Issue Information

Dear Colleagues,

If form follows function, then transglutaminases are arguably some of the most important enzymes in biology. These enzymes contribute to the formation of the largest and most dynamic structures made by either single-cell or multicellular organisms. For example, transglutaminases crosslink the constituents of the cell walls encasing single cell creatures. Similar reactions result in the formation of the cornified envelope, bones, cartilage, and the extracellular matrix of multicellular organisms. The form of these structures profoundly affects the cells they encompass. And yet, this is just one aspect of the actions catalyzed by this remarkable group of enzymes. In the following Special Issue, we will review the current state-of-art concerning the role of transglutaminases in biological processes and how these might be imaged and regulated.

Dr. Thomas M. Jeitner
Guest Editor

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. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). 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.

Keywords

  • imaging
  • regulation
  • application
  • clinical translation

Published Papers (1 paper)

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Research

14 pages, 2283 KiB  
Article
Conformational Modulation of Tissue Transglutaminase via Active Site Thiol Alkylating Agents: Size Does Not Matter
by Pauline Navals, Alana M. M. Rangaswamy, Petr Kasyanchyk, Maxim V. Berezovski and Jeffrey W. Keillor
Biomolecules 2024, 14(4), 496; https://doi.org/10.3390/biom14040496 - 19 Apr 2024
Viewed by 437
Abstract
TG2 is a unique member of the transglutaminase family as it undergoes a dramatic conformational change, allowing its mutually exclusive function as either a cross-linking enzyme or a G-protein. The enzyme’s dysregulated activity has been implicated in a variety of pathologies (e.g., celiac [...] Read more.
TG2 is a unique member of the transglutaminase family as it undergoes a dramatic conformational change, allowing its mutually exclusive function as either a cross-linking enzyme or a G-protein. The enzyme’s dysregulated activity has been implicated in a variety of pathologies (e.g., celiac disease, fibrosis, cancer), leading to the development of a wide range of inhibitors. Our group has primarily focused on the development of peptidomimetic targeted covalent inhibitors, the nature and size of which were thought to be important features to abolish TG2’s conformational dynamism and ultimately inhibit both its activities. However, we recently demonstrated that the enzyme was unable to bind guanosine triphosphate (GTP) when catalytically inactivated by small molecule inhibitors. In this study, we designed a library of models targeting covalent inhibitors of progressively smaller sizes (15 to 4 atoms in length). We evaluated their ability to inactivate TG2 by measuring their respective kinetic parameters kinact and KI. Their impact on the enzyme’s ability to bind GTP was then evaluated and subsequently correlated to the conformational state of the enzyme, as determined via native PAGE and capillary electrophoresis. All irreversible inhibitors evaluated herein locked TG2 in its open conformation and precluded GTP binding. Therefore, we conclude that steric bulk and structural complexity are not necessary factors to consider when designing TG2 inhibitors to abolish G-protein activity. Full article
(This article belongs to the Special Issue Transglutaminases: Regulation, Imaging, and Applications)
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