Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
9.4
4.8
Journals
Biomolecules
Special Issues
Cell Biology and Biomedical Application of Galectins
share announcement

Cell Biology and Biomedical Application of Galectins

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

Deadline for manuscript submissions: 31 December 2025 | Viewed by 10865

Special Issue Editor

Dr. Alexander Timoshenko

E-Mail Website
Guest Editor
Department of Biology, The University of Western Ontario, 1151 Richmond St. N., London, ON N6A 5B7, Canada
Interests: galectins; O-GlcNAc; cellular differentiation; glycobiology; cell aggregation; neutrophils
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Galectins are a family of soluble b-galactoside-binding proteins with diverse glycan-dependent and glycan-independent functions, both outside and inside the cell. Galectins play a role in many fundamental cellular processes, such as cell growth, differentiation, self-renewal, apoptosis, autophagy, phagocytosis, and cellular interactions. Changes in the expression of galectins are linked to diseases such as cancer, heart disease, and fibrosis, among others, which suggests that they are potential candidates for biomedical applications. However, current success in these directions is limited, primarily due to the complex network of interacting galectins in cells and their different modes of action. The functions of galectins depend on their localization in specific cellular compartments and organelles (cytosol, lipid droplets, cytoskeleton, mitochondria, nucleus, lysosomes, and plasma membrane) and related intracellular trafficking and secretion, which occurs through non-classical pathways. An integrated vision of galectin cell biology is still needed, and advanced studies of galectin trafficking, post-translational modifications, the transcriptional regulation of galectin gene expression, and galectin-mediated transmembrane signaling are highly warranted. This Special Issue covers recent progress in the fields of the cell biology of galectins and the biomedical aspects of these molecules as biomarkers and clinical targets in the context of human diseases.

Dr. Alexander Timoshenko
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

  • galectins
  • cell differentiation
  • stem cells
  • apoptosis
  • autophagy
  • cell adhesion
  • glycobiology
  • post-translational modifications
  • transmembrane signaling
  • protein trafficking
  • cancer
  • heart diseases
  • fibrosis
  • inflammation
  • targeted therapeutics
  • galectin inhibitors

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • Reprint: MDPI Books provides the opportunity to republish successful Special Issues in book format, both online and in print.

Further information on MDPI's Special Issue policies can be found here.

Related Special Issue

Published Papers (4 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

20 pages, 10279 KiB  
Article
Exploration into Galectin-3 Driven Endocytosis and Lattices
by Massiullah Shafaq-Zadah, Estelle Dransart, Satish Kailasam Mani, Julio Lopes Sampaio, Lydia Bouidghaghen, Ulf J. Nilsson, Hakon Leffler and Ludger Johannes
Biomolecules 2024, 14(9), 1169; https://doi.org/10.3390/biom14091169 - 18 Sep 2024
Cited by 1 | Viewed by 1757
Abstract
Essentially all plasma membrane proteins are glycosylated, and their activity is regulated by tuning their cell surface dynamics. This is achieved by glycan-binding proteins of the galectin family that either retain glycoproteins within lattices or drive their endocytic uptake via the clathrin-independent glycolipid-lectin [...] Read more.
Essentially all plasma membrane proteins are glycosylated, and their activity is regulated by tuning their cell surface dynamics. This is achieved by glycan-binding proteins of the galectin family that either retain glycoproteins within lattices or drive their endocytic uptake via the clathrin-independent glycolipid-lectin (GL-Lect) mechanism. Here, we have used immunofluorescence-based assays to analyze how lattice and GL-Lect mechanisms affect the internalization of the cell adhesion and migration glycoprotein α5β1 integrin. In retinal pigment epithelial (RPE-1) cells, internalized α5β1 integrin is found in small peripheral endosomes under unperturbed conditions. Pharmacological compounds were used to competitively inhibit one of the galectin family members, galectin-3 (Gal3), or to inhibit the expression of glycosphingolipids, both of which are the fabric of the GL-Lect mechanism. We found that under acute inhibition conditions, endocytic uptake of α5β1 integrin was strongly reduced, in agreement with previous studies on the GL-Lect driven internalization of the protein. In contrast, upon prolonged inhibitor treatment, the uptake of α5β1 integrin was increased, and the protein was now internalized by alternative pathways into large perinuclear endosomes. Our findings suggest that under these prolonged inhibitor treatment conditions, α5β1 integrin containing galectin lattices are dissociated, leading to an altered endocytic compartmentalization. Full article
(This article belongs to the Special Issue Cell Biology and Biomedical Application of Galectins)
►▼ Show Figures

Figure 1

12 pages, 2255 KiB  
Article
Galectin-9 as a Potential Modulator of Lymphocyte Adhesion to Endothelium via Binding to Blood Group H Glycan
by Eugenia M. Rapoport, Ivan M. Ryzhov, Ekaterina V. Slivka, Elena Yu. Korchagina, Inna S. Popova, Sergey V. Khaidukov, Sabine André, Herbert Kaltner, Hans-J. Gabius, Stephen Henry and Nicolai V. Bovin
Biomolecules 2023, 13(8), 1166; https://doi.org/10.3390/biom13081166 - 26 Jul 2023
Cited by 7 | Viewed by 1910
Abstract
The recruitment of leukocytes from blood is one of the most important cellular processes in response to tissue damage and inflammation. This multi-step process includes rolling leukocytes and their adhesion to endothelial cells (EC), culminating in crossing the EC barrier to reach the [...] Read more.
The recruitment of leukocytes from blood is one of the most important cellular processes in response to tissue damage and inflammation. This multi-step process includes rolling leukocytes and their adhesion to endothelial cells (EC), culminating in crossing the EC barrier to reach the inflamed tissue. Galectin-8 and galectin-9 expressed on the immune system cells are part of this process and can induce cell adhesion via binding to oligolactosamine glycans. Similarly, these galectins have an order of magnitude higher affinity towards glycans of the ABH blood group system, widely represented on ECs. However, the roles of gal-8 and gal-9 as mediators of adhesion to endothelial ABH antigens are practically unknown. In this work, we investigated whether H antigen–gal-9-mediated adhesion occurred between Jurkat cells (of lymphocytic origin and known to have gal-9) and EA.hy 926 cells (immortalized endothelial cells and known to have blood group H antigen). Baseline experiments showed that Jurkat cells adhered to EA.hy 926 cells; however when these EA.hy 926 cells were defucosylated (despite the unmasking of lactosamine chains), adherence was abolished. Restoration of fucosylation by insertion of synthetic glycolipids in the form of H (type 2) trisaccharide Fucα1-2Galβ1-4GlcNAc restored adhesion. The degree of lymphocyte adhesion to native and the “H-restored” (glycolipid-loaded) EA.hy 926 cells was comparable. If this gal-9/H (type 2) interaction is similar to processes that occur in vivo, this suggests that only the short (trisaccharide) H glycan on ECs is required. Full article
(This article belongs to the Special Issue Cell Biology and Biomedical Application of Galectins)
►▼ Show Figures

Figure 1

12 pages, 1668 KiB  
Article
Diffuse Myocardial Fibrosis on Cardiac Magnetic Resonance Imaging Is Related to Galectin-3 and Predicts Outcome in Heart Failure
by Elles M. Screever, Thomas M. Gorter, Tineke P. Willems, Joseph Pierre Aboumsallem, Navin Suthahar, Belend Mahmoud, Dirk J. van Veldhuisen, Rudolf A. de Boer and Wouter C. Meijers
Biomolecules 2023, 13(3), 410; https://doi.org/10.3390/biom13030410 - 22 Feb 2023
Cited by 6 | Viewed by 3193
Abstract
Aims: Ongoing adverse remodeling is a hallmark of heart failure (HF), which might be reflected by either focal or diffuse myocardial fibrosis. Therefore, in (pre)clinical settings, we used immunohistochemistry or cardiac magnetic resonance imaging (CMR) to investigate the association of (focal or diffuse) [...] Read more.
Aims: Ongoing adverse remodeling is a hallmark of heart failure (HF), which might be reflected by either focal or diffuse myocardial fibrosis. Therefore, in (pre)clinical settings, we used immunohistochemistry or cardiac magnetic resonance imaging (CMR) to investigate the association of (focal or diffuse) fibrosis with cardiac biomarkers and adverse events in HF. Methods and results: In C57Bl/6J mice, we determined the presence and extent of myocardial fibrosis 6 weeks post-myocardial infarction (MI). Furthermore, we studied 159 outpatient HF patients who underwent CMR, and determined focal and diffuse fibrosis by late gadolinium enhancement (LGE) and post-contrast T1 time of the non-LGE myocardium, respectively. HF patients were categorized based on the presence of LGE, and by the median post-contrast T1 time. Kaplan–Meier and Cox regression analyses were used to determine the association of fibrosis with HF hospitalization and all-cause mortality. LGE was detected in 61 (38%) patients. Cardiac biomarker levels were comparable between LGE-positive and LGE-negative patients. LGE-positive patients with a short T1 time had elevated levels of both NT-proBNP and galectin-3 (1611 vs. 453 ng/L, p = 0.026 and 20 vs. 15 μg/L, p = 0.004, respectively). This was not observed in LGE-negative patients. Furthermore, a short T1 time in LGE-positive patients was associated with a higher risk of adverse events (log-rank p = 0.01). Conclusion: This study implies that cardiac biomarkers reflect active remodeling of the non-infarcted myocardium of patients with focal myocardial scarring. Diffuse fibrosis, in contrast to focal scarring, might have a higher prognostic value regarding adverse outcomes in HF patients. Full article
(This article belongs to the Special Issue Cell Biology and Biomedical Application of Galectins)
►▼ Show Figures

Graphical abstract

18 pages, 2902 KiB  
Article
O-GlcNAc-Mediated Regulation of Galectin Expression and Secretion in Human Promyelocytic HL-60 Cells Undergoing Neutrophilic Differentiation
by Adam McTague, Rada Tazhitdinova and Alexander V. Timoshenko
Biomolecules 2022, 12(12), 1763; https://doi.org/10.3390/biom12121763 - 27 Nov 2022
Cited by 6 | Viewed by 2814
Abstract
In this study, we have tested the hypothesis that the expression and secretion of galectins are driven through mechanisms globally impacted by homeostatic regulation involving the post-translational modification of intracellular proteins with O-linked N-acetylglucosamine (O-GlcNAc). We showed that neutrophilic differentiation [...] Read more.
In this study, we have tested the hypothesis that the expression and secretion of galectins are driven through mechanisms globally impacted by homeostatic regulation involving the post-translational modification of intracellular proteins with O-linked N-acetylglucosamine (O-GlcNAc). We showed that neutrophilic differentiation of HL-60 cells induced by all-trans retinoic acid (ATRA) and 6-diazo-5-oxo-L-norleucine (DON) was associated with a significant drop of cellular O-GlcNAc levels in serum-contained and serum-free cell culture media. Galectin gene and protein expression profiles in HL-60 cells were specifically modified by ATRA and by inhibitors of O-GlcNAc cycle enzymes, however overall trends for each drug were similar between cells growing in the presence or absence of serum except for LGALS9 and LGALS12. The secretion of four galectins (-1, -3, -9, and -10) by HL-60 cells in a serum-free medium was stimulated by O-GlcNAc-reducing ATRA and DON while O-GlcNAc-elevating thiamet G (O-GlcNAcase inhibitor) failed to change the basal levels of extracellular galectins. Taken together, these results demonstrate that O-GlcNAc homeostasis is essential not only for regulation of galectin expression in cells but also for the secretion of multiple members of this protein family, which can be an important novel aspect of unconventional secretion mechanisms. Full article
(This article belongs to the Special Issue Cell Biology and Biomedical Application of Galectins)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-4
Back to TopTop