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Biomolecules
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Cell Biology of Galectins
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Cell Biology of Galectins

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

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 34281

Printed Edition Available!
A printed edition of this Special Issue is available here.

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 outside and inside the cell. There are sixteen recognized mammalian galectin genes and their expression profiles are very different between cell types, tissues, and species. Galectins are known to be involved in regulating multiple processes in cells under normal, stress, and pathological conditions, which suggest they are potential candidates for biomedical applications. However, current success in this direction is challenging, mostly, due to the complex network of interacting galectins in cells, different modes of their action, and association with diverse fundamental cellular functions such as cell growth, differentiation, stemness, apoptosis, autophagy, phagocytosis, and cellular interactions. Functions of galectins depend on their localization in specific cellular compartments and organelles (cytosol, cytoskeleton, mitochondria, nucleus, lysosomes, and plasma membrane) and related intracellular trafficking and secretion, which occurs through non-classical pathways. An integrated vision of the galectin cell biology is still warranted and advanced studies of galectin post-translational modifications, transcriptional regulation of galectin gene expression, and galectin-mediated transmembrane signaling are highly regarded. This Special Issue covers recent progress in the field of cell biology of galectins, relevant concepts of galectin regulatory mechanisms, and biomedical aspects of these unique multifunctional proteins.

Dr. Alexander V. Timoshenko
Guest Editor

Manuscript Submission Information

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Keywords

  • Galectins
  • Cell differentiation
  • Stem cells
  • Apoptosis
  • Autophagy
  • Cell adhesion
  • Glycobiology
  • Post-translational modifications
  • Transmembrane signaling
  • Protein trafficking

Related Special Issue

Published Papers (11 papers)

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Editorial

Jump to: Research, Review

3 pages, 205 KiB  
Editorial
Cell Biology of Galectins: Novel Aspects and Emerging Challenges
by Alexander V. Timoshenko
Biomolecules 2022, 12(6), 744; https://doi.org/10.3390/biom12060744 - 25 May 2022
Cited by 1 | Viewed by 1346
Abstract
Galectins are a family of soluble β-galactoside-binding proteins with diverse glycan-dependent and glycan-independent functions outside and inside the cell [...] Full article
(This article belongs to the Special Issue Cell Biology of Galectins)

Research

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14 pages, 2012 KiB  
Article
O-GlcNAcylation and Regulation of Galectin-3 in Extraembryonic Endoderm Differentiation
by Mohamed I. Gatie, Danielle M. Spice, Amritpal Garha, Adam McTague, Mariam Ahmer, Alexander V. Timoshenko and Gregory M. Kelly
Biomolecules 2022, 12(5), 623; https://doi.org/10.3390/biom12050623 - 22 Apr 2022
Cited by 5 | Viewed by 2305
Abstract
The regulation of proteins through the addition and removal of O-linked β-N-acetylglucosamine (O-GlcNAc) plays a role in many signaling events, specifically in stem cell pluripotency and the regulation of differentiation. However, these post-translational modifications have not been explored [...] Read more.
The regulation of proteins through the addition and removal of O-linked β-N-acetylglucosamine (O-GlcNAc) plays a role in many signaling events, specifically in stem cell pluripotency and the regulation of differentiation. However, these post-translational modifications have not been explored in extraembryonic endoderm (XEN) differentiation. Of the plethora of proteins regulated through O-GlcNAc, we explored galectin-3 as a candidate protein known to have various intracellular and extracellular functions. Based on other studies, we predicted a reduction in global O-GlcNAcylation levels and a distinct galectin expression profile in XEN cells relative to embryonic stem (ES) cells. By conducting dot blot analysis, XEN cells had decreased levels of global O-GlcNAc than ES cells, which reflected a disbalance in the expression of genes encoding O-GlcNAc cycle enzymes. Immunoassays (Western blot and ELISA) revealed that although XEN cells (low O-GlcNAc) had lower concentrations of both intracellular and extracellular galectin-3 than ES cells (high O-GlcNAc), the relative secretion of galectin-3 was significantly increased by XEN cells. Inducing ES cells toward XEN in the presence of an O-GlcNAcase inhibitor was not sufficient to inhibit XEN differentiation. However, global O-GlcNAcylation was found to decrease in differentiated cells and the extracellular localization of galectin-3 accompanies these changes. Inhibiting global O-GlcNAcylation status does not, however, impact pluripotency and the ability of ES cells to differentiate to the XEN lineage. Full article
(This article belongs to the Special Issue Cell Biology of Galectins)
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15 pages, 17762 KiB  
Article
Modulation of the Epithelial-Immune Cell Crosstalk and Related Galectin Secretion by DP3-5 Galacto-Oligosaccharides and β-3′Galactosyllactose
by Veronica Ayechu-Muruzabal, Melanie van de Kaa, Reshmi Mukherjee, Johan Garssen, Bernd Stahl, Roland J. Pieters, Belinda van’t Land, Aletta D. Kraneveld and Linette E. M. Willemsen
Biomolecules 2022, 12(3), 384; https://doi.org/10.3390/biom12030384 - 28 Feb 2022
Cited by 5 | Viewed by 2443
Abstract
Prebiotic galacto-oligosaccharides (GOS) were shown to support mucosal immune development by enhancing regulatory-type Th1 immune polarization induced by synthetic CpG oligodeoxynucleotides (TLR9 agonist mimicking a bacterial DNA trigger). Epithelial-derived galectin-9 was associated with these immunomodulatory effects. We aimed to identify the most active [...] Read more.
Prebiotic galacto-oligosaccharides (GOS) were shown to support mucosal immune development by enhancing regulatory-type Th1 immune polarization induced by synthetic CpG oligodeoxynucleotides (TLR9 agonist mimicking a bacterial DNA trigger). Epithelial-derived galectin-9 was associated with these immunomodulatory effects. We aimed to identify the most active fractions within GOS based on the degree of polymerization (DP), and to study the immunomodulatory capacities of DP3-sized β-3′galactosyllactose (β-3′GL) using a transwell co-culture model of human intestinal epithelial cells (IEC) and activated peripheral blood mononuclear cells (PBMC). IEC were apically exposed to different DP fractions of GOS or β-3′GL in the presence of CpG, and basolaterally co-cultured with αCD3/CD28-activated PBMC, washed, and incubated in fresh medium for IEC-derived galectin analysis. Only DP3-5 in the presence of CpG enhanced galectin-9 secretion. DP3-sized β-3′GL promoted a regulatory-type Th1 response by increasing IFNγ and IL-10 or galectin-9 concentrations as compared to CpG alone. In addition, IEC-derived galectin-3, -4, and -9 secretion was increased by β-3′GL when combined with CpG. Therefore, the GOS DP3-5 and most effectively DP3-sized β-3′GL supported the immunomodulatory properties induced by CpG by enhancing epithelial-derived galectin secretion, which, in turn, could support mucosal immunity. Full article
(This article belongs to the Special Issue Cell Biology of Galectins)
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15 pages, 3227 KiB  
Article
Expression, Regulation, and Functions of the Galectin-16 Gene in Human Cells and Tissues
by Jennifer D. Kaminker and Alexander V. Timoshenko
Biomolecules 2021, 11(12), 1909; https://doi.org/10.3390/biom11121909 - 20 Dec 2021
Cited by 15 | Viewed by 3127
Abstract
Galectins comprise a family of soluble β-galactoside-binding proteins, which regulate a variety of key biological processes including cell growth, differentiation, survival, and death. This paper aims to address the current knowledge on the unique properties, regulation, and expression of the galectin-16 gene ( [...] Read more.
Galectins comprise a family of soluble β-galactoside-binding proteins, which regulate a variety of key biological processes including cell growth, differentiation, survival, and death. This paper aims to address the current knowledge on the unique properties, regulation, and expression of the galectin-16 gene (LGALS16) in human cells and tissues. To date, there are limited studies on this galectin, with most focusing on its tissue specificity to the placenta. Here, we report the expression and 8-Br-cAMP-induced upregulation of LGALS16 in two placental cell lines (BeWo and JEG-3) in the context of trophoblastic differentiation. In addition, we provide the results of a bioinformatics search for LGALS16 using datasets available at GEO, Human Protein Atlas, and prediction tools for relevant transcription factors and miRNAs. Our findings indicate that LGALS16 is detected by microarrays in diverse human cells/tissues and alters expression in association with cancer, diabetes, and brain diseases. Molecular mechanisms of the transcriptional and post-transcriptional regulation of LGALS16 are also discussed based on the available bioinformatics resources. Full article
(This article belongs to the Special Issue Cell Biology of Galectins)
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16 pages, 15180 KiB  
Article
Structural Characterization of Rat Galectin-5, an N-Tailed Monomeric Proto-Type-like Galectin
by Federico M. Ruiz, Francisco J. Medrano, Anna-Kristin Ludwig, Herbert Kaltner, Nadezhda V. Shilova, Nicolai V. Bovin, Hans-Joachim Gabius and Antonio Romero
Biomolecules 2021, 11(12), 1854; https://doi.org/10.3390/biom11121854 - 09 Dec 2021
Cited by 1 | Viewed by 2234
Abstract
Galectins are multi-purpose effectors acting via interactions with distinct counterreceptors based on protein-glycan/protein recognition. These processes are emerging to involve several regions on the protein so that the availability of a detailed structural characterization of a full-length galectin is essential. We report here [...] Read more.
Galectins are multi-purpose effectors acting via interactions with distinct counterreceptors based on protein-glycan/protein recognition. These processes are emerging to involve several regions on the protein so that the availability of a detailed structural characterization of a full-length galectin is essential. We report here the first crystallographic information on the N-terminal extension of the carbohydrate recognition domain of rat galectin-5, which is precisely described as an N-tailed proto-type-like galectin. In the ligand-free protein, the three amino-acid stretch from Ser2 to Ser5 is revealed to form an extra β-strand (F0), and the residues from Thr6 to Asn12 are part of a loop protruding from strands S1 and F0. In the ligand-bound structure, amino acids Ser2–Tyr10 switch position and are aligned to the edge of the β-sandwich. Interestingly, the signal profile in our glycan array screening shows the sugar-binding site to preferentially accommodate the histo-blood-group B (type 2) tetrasaccharide and N-acetyllactosamine-based di- and oligomers. The crystal structures revealed the characteristically preformed structural organization around the central Trp77 of the CRD with involvement of the sequence signature’s amino acids in binding. Ligand binding was also characterized calorimetrically. The presented data shows that the N-terminal extension can adopt an ordered structure and shapes the hypothesis that a ligand-induced shift in the equilibrium between flexible and ordered conformers potentially acts as a molecular switch, enabling new contacts in this region. Full article
(This article belongs to the Special Issue Cell Biology of Galectins)
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19 pages, 2439 KiB  
Article
Galectin-1 Cooperates with Yersinia Outer Protein (Yop) P to Thwart Protective Immunity by Repressing Nitric Oxide Production
by Brenda Lucila Jofre, Ricardo Javier Eliçabe, Juan Eduardo Silva, Juan Manuel Pérez Sáez, Maria Daniela Paez, Eduardo Callegari, Karina Valeria Mariño, María Silvia Di Genaro, Gabriel Adrián Rabinovich and Roberto Carlos Davicino
Biomolecules 2021, 11(11), 1636; https://doi.org/10.3390/biom11111636 - 04 Nov 2021
Cited by 3 | Viewed by 1903
Abstract
Yersinia enterocolitica (Ye) inserts outer proteins (Yops) into cytoplasm to infect host cells. However, in spite of considerable progress, the mechanisms implicated in this process, including the association of Yops with host proteins, remain unclear. Here, we evaluated the functional role of Galectin-1 [...] Read more.
Yersinia enterocolitica (Ye) inserts outer proteins (Yops) into cytoplasm to infect host cells. However, in spite of considerable progress, the mechanisms implicated in this process, including the association of Yops with host proteins, remain unclear. Here, we evaluated the functional role of Galectin-1 (Gal1), an endogenous β-galactoside-binding protein, in modulating Yop interactions with host cells. Our results showed that Gal1 binds to Yops in a carbohydrate-dependent manner. Interestingly, Gal1 binding to Yops protects these virulence factors from trypsin digestion. Given that early control of Ye infection involves activation of macrophages, we evaluated the role of Gal1 and YopP in the modulation of macrophage function. Although Gal1 and YopP did not influence production of superoxide anion and/or TNF by Ye-infected macrophages, they coordinately inhibited nitric oxide (NO) production. Notably, recombinant Gal1 (rGal1) did not rescue NO increase observed in Lgals1−/− macrophages infected with the YopP mutant Ye ∆yopP. Whereas NO induced apoptosis in macrophages, no significant differences in cell death were detected between Gal1-deficient macrophages infected with Ye ∆yopP, and WT macrophages infected with Ye wt. Strikingly, increased NO production was found in WT macrophages treated with MAPK inhibitors and infected with Ye wt. Finally, rGal1 administration did not reverse the protective effect in Peyer Patches (PPs) of Lgals1−/− mice infected with Ye ∆yopP. Our study reveals a cooperative role of YopP and endogenous Gal1 during Ye infection. Full article
(This article belongs to the Special Issue Cell Biology of Galectins)
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Review

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32 pages, 2415 KiB  
Review
The Complex Biological Effects of Pectin: Galectin-3 Targeting as Potential Human Health Improvement?
by Lucas de Freitas Pedrosa, Avraham Raz and João Paulo Fabi
Biomolecules 2022, 12(2), 289; https://doi.org/10.3390/biom12020289 - 10 Feb 2022
Cited by 16 | Viewed by 5053
Abstract
Galectin-3 is the only chimeric representative of the galectin family. Although galectin-3 has ubiquitous regulatory and physiological effects, there is a great number of pathological environments where galectin-3 cooperatively participates. Pectin is composed of different chemical structures, such as homogalacturonans, rhamnogalacturonans, and side [...] Read more.
Galectin-3 is the only chimeric representative of the galectin family. Although galectin-3 has ubiquitous regulatory and physiological effects, there is a great number of pathological environments where galectin-3 cooperatively participates. Pectin is composed of different chemical structures, such as homogalacturonans, rhamnogalacturonans, and side chains. The study of pectin’s major structural aspects is fundamental to predicting the impact of pectin on human health, especially regarding distinct molecular modulation. One of the explored pectin’s biological activities is the possible galectin-3 protein regulation. The present review focuses on revealing the structure/function relationship of pectins, their fragments, and their biological effects. The discussion highlighted by this review shows different effects described within in vitro and in vivo experimental models, with interesting and sometimes contradictory results, especially regarding galectin-3 interaction. The review demonstrates that pectins are promissory food-derived molecules for different bioactive functions. However, galectin-3 inhibition by pectin had been stated in literature before, although it is not a fully understood, experimentally convincing, and commonly agreed issue. It is demonstrated that more studies focusing on structural analysis and its relation to the observed beneficial effects, as well as substantial propositions of cause and effect alongside robust data, are needed for different pectin molecules’ interactions with galectin-3. Full article
(This article belongs to the Special Issue Cell Biology of Galectins)
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22 pages, 1128 KiB  
Review
The Diagnostic and Therapeutic Potential of Galectin-3 in Cardiovascular Diseases
by Grażyna Sygitowicz, Agata Maciejak-Jastrzębska and Dariusz Sitkiewicz
Biomolecules 2022, 12(1), 46; https://doi.org/10.3390/biom12010046 - 29 Dec 2021
Cited by 27 | Viewed by 4230
Abstract
Galectin-3 plays a prominent role in chronic inflammation and has been implicated in the development of many disease conditions, including heart disease. Galectin-3, a regulatory protein, is elevated in both acute and chronic heart failure and is involved in the inflammatory pathway after [...] Read more.
Galectin-3 plays a prominent role in chronic inflammation and has been implicated in the development of many disease conditions, including heart disease. Galectin-3, a regulatory protein, is elevated in both acute and chronic heart failure and is involved in the inflammatory pathway after injury leading to myocardial tissue remodelling. We discussed the potential utility of galectin-3 as a diagnostic and disease severity/prognostic biomarker in different cardio/cerebrovascular diseases, such as acute ischemic stroke, acute coronary syndromes, heart failure and arrhythmogenic cardiomyopathy. Over the last decade there has been a marked increase in the understanding the role of galectin-3 in myocardial fibrosis and inflammation and as a therapeutic target for the treatment of heart failure and myocardial infarction. Full article
(This article belongs to the Special Issue Cell Biology of Galectins)
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25 pages, 9098 KiB  
Review
Functions and Inhibition of Galectin-7, an Emerging Target in Cellular Pathophysiology
by Nishant V. Sewgobind, Sanne Albers and Roland J. Pieters
Biomolecules 2021, 11(11), 1720; https://doi.org/10.3390/biom11111720 - 18 Nov 2021
Cited by 9 | Viewed by 2606
Abstract
Galectin-7 is a soluble unglycosylated lectin that is able to bind specifically to β-galactosides. It has been described to be involved in apoptosis, proliferation and differentiation, but also in cell adhesion and migration. Several disorders and diseases are discussed by covering the aforementioned [...] Read more.
Galectin-7 is a soluble unglycosylated lectin that is able to bind specifically to β-galactosides. It has been described to be involved in apoptosis, proliferation and differentiation, but also in cell adhesion and migration. Several disorders and diseases are discussed by covering the aforementioned biological processes. Structural features of galectin-7 are discussed as well as targeting the protein intracellularly or extracellularly. The exact molecular mechanisms that lie behind many biological processes involving galectin-7 are not known. It is therefore useful to come up with chemical probes or tools in order to obtain knowledge of the physiological processes. The objective of this review is to summarize the roles and functions of galectin-7 in the human body, providing reasons why it is necessary to design inhibitors for galectin-7, to give the reader structural insights and describe its current inhibitors. Full article
(This article belongs to the Special Issue Cell Biology of Galectins)
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15 pages, 2057 KiB  
Review
Galectins in Endothelial Cell Biology and Angiogenesis: The Basics
by Victor L. Thijssen
Biomolecules 2021, 11(9), 1386; https://doi.org/10.3390/biom11091386 - 20 Sep 2021
Cited by 18 | Viewed by 3616
Abstract
Angiogenesis, the growth of new blood vessels out of existing vessels, is a complex and tightly regulated process. It is executed by the cells that cover the inner surface of the vasculature, i.e., the endothelial cells. During angiogenesis, these cells adopt different phenotypes, [...] Read more.
Angiogenesis, the growth of new blood vessels out of existing vessels, is a complex and tightly regulated process. It is executed by the cells that cover the inner surface of the vasculature, i.e., the endothelial cells. During angiogenesis, these cells adopt different phenotypes, which allows them to proliferate and migrate, and to form tube-like structures that eventually result in the generation of a functional neovasculature. Multiple internal and external cues control these processes and the galectin protein family was found to be indispensable for proper execution of angiogenesis. Over the last three decades, several members of this glycan-binding protein family have been linked to endothelial cell functioning and to different steps of the angiogenesis cascade. This review provides a basic overview of our current knowledge regarding galectins in angiogenesis. It covers the main findings with regard to the endothelial expression of galectins and highlights their role in endothelial cell function and biology. Full article
(This article belongs to the Special Issue Cell Biology of Galectins)
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10 pages, 1277 KiB  
Review
Towards a Better Understanding of the Relationships between Galectin-7, p53 and MMP-9 during Cancer Progression
by Yves St-Pierre
Biomolecules 2021, 11(6), 879; https://doi.org/10.3390/biom11060879 - 14 Jun 2021
Cited by 11 | Viewed by 3335
Abstract
It has been almost 25 years since the discovery of galectin-7. This member of the galectin family has attracted interest from many working in the cancer field given its highly restricted expression profile in epithelial cells and the fact that cancers of epithelial [...] Read more.
It has been almost 25 years since the discovery of galectin-7. This member of the galectin family has attracted interest from many working in the cancer field given its highly restricted expression profile in epithelial cells and the fact that cancers of epithelial origin (carcinoma) are among the most frequent and deadly cancer subtypes. Initially described as a p53-induced gene and associated with apoptosis, galectin-7 is now recognized as having a protumorigenic role in many cancer types. Several studies have indeed shown that galectin-7 is associated with aggressive behavior of cancer cells and induces expression of MMP-9, a member of the matrix metalloproteinases (MMP) family known to confer invasive behavior to cancer cells. It is therefore not surprising that many studies have examined its relationships with p53 and MMP-9. However, the relationships between galectin-7 and p53 and MMP-9 are not always clear. This is largely because p53 is often mutated in cancer cells and such mutations drastically change its functions and, consequently, its association with galectin-7. In this review, we discuss the functional relationships between galectin-7, p53 and MMP-9 and reconcile some apparently contradictory observations. A better understanding of these relationships will help to develop a working hypothesis and model that will provide the basis for further research in the hope of establishing a new paradigm for tackling the role of galectin-7 in cancer. Full article
(This article belongs to the Special Issue Cell Biology of Galectins)
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