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Galectins: Structure, Function and Therapeutic Inhibitors—2nd Edition
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Galectins: Structure, Function and Therapeutic Inhibitors—2nd Edition

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

Deadline for manuscript submissions: closed (20 July 2024) | Viewed by 2916

Special Issue Editors

Dr. EmiliaMaria Pedone

E-Mail Website
Guest Editor
Institute of Biostructures and Bioimaging, CNR, 80134 Naples, Italy
Interests: protein–protein interactions; protein structure–function relationship; cell–macromolecules interactions; biophysical characterization; thermophilic microorganisms; protein disulfide oxidoreductase
Special Issues, Collections and Topics in MDPI journals
Dr. Sonia Di Gaetano

E-Mail Website
Guest Editor
Institute of Biostructures and Bioimaging, CNR, 80134 Naples, Italy
Interests: molecular biology; cellular biology; biological chemistry; protein structure–function relationship; protein biophysical characterization
Special Issues, Collections and Topics in MDPI journals
Dr. Domenica Capasso

E-Mail Website
Guest Editor
Department of Physics "Ettore Pancini", University of Naples Federico II, Via Cintia, 80126 Napoli, Italy
Interests: organic chemistry synthesis; carbohydrate chemistry; protein–carbohydrate interaction; protein–peptide interaction; medicinal chemistry; cell biology; cytofluorimetry
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Galectins, β-galactoside-binding proteins, have been shown to participate in diverse and relevant biological functions via their interactions with β-galactoside-containing structures on the cell surface. More importantly, human galectins act as regulatory factors in many types of pathologies by either inhibiting or promoting them. Therefore, to identify selective ligands for human galectins provides not only a useful tool for dissecting how each galectin member interacts with specific glycan structures, but also a possible solution for the development of clinical therapeutics. In this regard, this Special Issue focuses on the characterization of different members belonging to this family, studying not only the interaction with newly selected inhibitors by different biophysical techniques, but also characterizing their potential biological activity. All researchers working in the field are cordially invited to contribute original research articles or reviews to this Special Issue.

Due to the success of the 1st edition, we would like to add more results and new insights from recent research projects.

https://www.mdpi.com/journal/ijms/special_issues/RYW7TH55V0

Dr. EmiliaMaria Pedone
Dr. Sonia Di Gaetano
Dr. Domenica Capasso
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.

Keywords

  • galectin
  • inhibitor
  • CRD
  • glyconiugates
  • glycomimetics
  • peptidic ligands
  • selectivity, binding constants
  • protein–ligand interaction
  • galectin–ligand structure

Related Special Issue

Published Papers (3 papers)

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Research

11 pages, 2433 KiB  
Communication
A Quantitative Human Red Blood Cell Agglutination Assay for Characterisation of Galectin Inhibitors
by Rhianna Gasson, James A. Roper and Robert J. Slack
Int. J. Mol. Sci. 2024, 25(12), 6756; https://doi.org/10.3390/ijms25126756 - 19 Jun 2024
Viewed by 519
Abstract
Galectins are a family of beta-galactoside-binding proteins that are characterised by their carbohydrate recognition domain (CRD) and include galectin-1 and galectin-3. These galectins have been implicated in numerous diseases due to their pleiotropic nature, including cancer and fibrosis, with therapeutic inhibitors being clinically [...] Read more.
Galectins are a family of beta-galactoside-binding proteins that are characterised by their carbohydrate recognition domain (CRD) and include galectin-1 and galectin-3. These galectins have been implicated in numerous diseases due to their pleiotropic nature, including cancer and fibrosis, with therapeutic inhibitors being clinically developed to block the CRD. One of the early methods developed to characterise these galectins was the hemagglutination of red blood cells. Although it is insightful, this approach has been hampered by a lack of sensitivity and accurate quantification of the agglutination observed. In this study, we aimed to validate a more precise and quantitative method to enable the further investigation of differences between galectins in respect to agglutination induction in different blood groups, as well as the characterisation of small molecule inhibitors. Quantification of hemagglutination was shown to be optimal using U-bottom plates imaged and analysed with FIJI ImageJ rather than flat-bottom plates read for absorbance on an optical density plate reader. Galectin-3-induced red blood cell agglutination efficacy increased significantly from blood group O to A to B. However, for both the galectin-1 monomer and concatemer, a more comparable effect was observed between blood group B and O, but with more potent effects than in blood group A. Inhibition assays for both galectin-3 and galectin-1 induced-hemagglutination were able to demonstrate clear concentration responses and expected selectivity profiles for a set of small-molecule glycomimetics, confirming the historical profiles obtained in biochemical binding and functional cellular assays. Full article
(This article belongs to the Special Issue Galectins: Structure, Function and Therapeutic Inhibitors—2nd Edition)
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10 pages, 2262 KiB  
Communication
Determining the Affinity and Kinetics of Small Molecule Inhibitors of Galectin-1 Using Surface Plasmon Resonance
by Henry Kim, Louis Kretz, Céline Ronin, Christina Starck, James A. Roper, Barbro Kahl-Knutson, Kristoffer Peterson, Hakon Leffler, Ulf J. Nilsson, Anders Pedersen, Fredrik R. Zetterberg and Robert J. Slack
Int. J. Mol. Sci. 2024, 25(12), 6704; https://doi.org/10.3390/ijms25126704 - 18 Jun 2024
Viewed by 1010
Abstract
The beta-galactoside-binding mammalian lectin galectin-1 can bind, via its carbohydrate recognition domain (CRD), to various cell surface glycoproteins and has been implicated in a range of cancers. As a consequence of binding to sugar residues on cell surface receptors, it has been shown [...] Read more.
The beta-galactoside-binding mammalian lectin galectin-1 can bind, via its carbohydrate recognition domain (CRD), to various cell surface glycoproteins and has been implicated in a range of cancers. As a consequence of binding to sugar residues on cell surface receptors, it has been shown to have a pleiotropic effect across many cell types and mechanisms, resulting in immune system modulation and cancer progression. As a result, it has started to become a therapeutic target for both small and large molecules. In previous studies, we used fluorescence polarization (FP) assays to determine KD values to screen and triage small molecule glycomimetics that bind to the galectin-1 CRD. In this study, surface plasmon resonance (SPR) was used to compare human and mouse galectin-1 affinity measures with FP, as SPR has not been applied for compound screening against this galectin. Binding affinities for a selection of mono- and di-saccharides covering a 1000-fold range correlated well between FP and SPR assay formats for both human and mouse galectin-1. It was shown that slower dissociation drove the increased affinity at human galectin-1, whilst faster association was responsible for the effects in mouse galectin-1. This study demonstrates that SPR is a sound alternative to FP for early drug discovery screening and determining affinity estimates. Consequently, it also allows association and dissociation constants to be measured in a high-throughput manner for small molecule galectin-1 inhibitors. Full article
(This article belongs to the Special Issue Galectins: Structure, Function and Therapeutic Inhibitors—2nd Edition)
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24 pages, 16535 KiB  
Article
Galectin-3 and Autophagy in Renal Acute Tubular Necrosis
by Suhail Al-Salam, Govindan S. Jagadeesh, Manjusha Sudhadevi and Javed Yasin
Int. J. Mol. Sci. 2024, 25(7), 3604; https://doi.org/10.3390/ijms25073604 - 22 Mar 2024
Viewed by 1057
Abstract
Acute kidney injury (AKI) is a public health burden with increasing morbidity and mortality rates and health care costs. Acute tubular necrosis (ATN) is the most common cause of AKI. Cisplatin (CIS) is a platinum-based chemotherapeutic agent used in the treatment of a [...] Read more.
Acute kidney injury (AKI) is a public health burden with increasing morbidity and mortality rates and health care costs. Acute tubular necrosis (ATN) is the most common cause of AKI. Cisplatin (CIS) is a platinum-based chemotherapeutic agent used in the treatment of a wide variety of malignancies such as lung, breast, ovary, testis, bladder, cervix, and head and neck cancers. Autophagy plays an important role in AKI. Galectin-3 (Gal-3) is significantly increased in renal tubules in AKI; however, its role in autophagy is not well understood. Male C57B6/J and B6.Cg-Lgals3 <tm 1 Poi>/J Gal-3 knockout (KO) mice were used to induce AKI using a CIS mouse model of ATN. Renal Gal-3 and autophagy proteins’ expression were measured using standard histologic, immunofluorescent, and enzyme-linked immunosorbent assay techniques. The data were presented as the mean ± S.E. Statistically significant differences (p < 0.05) were calculated between experimental groups and corresponding control groups by one-way analysis of variance. There was a significant increase in renal concentrations of Gal-3 in the Gal-3 wild-type CIS-treated mice when compared with sham control mice. There were significantly higher concentrations of renal LC3B, ATG13, Ulk-1, Beclin, ATG5, ATG12, ATG9A, and p-AMPK in the CIS-treated Gal-3 KO mice than in the Gal-3 wild-type CIS-treated mice. Further, there were significantly higher concentrations of mTOR, p- NF-κB, beta-catenin, and p62 in the kidneys of the Gal-3 wild-type CIS-treated mice than in the Gal-3 KO CIS-treated mice. Our findings affirm the connection between Gal-3 and autophagy, revealing its central role as a connector with prosurvival signaling proteins. Gal-3 plays a pivotal role in orchestrating cellular responses by interacting with prosurvival signal pathways and engaging with autophagy proteins. Notably, our observations highlight that the absence of Gal-3 can enhance autophagy in CIS-induced ATN. Full article
(This article belongs to the Special Issue Galectins: Structure, Function and Therapeutic Inhibitors—2nd Edition)
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