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13 pages, 2086 KiB

Open AccessArticle

Investigation of N-Acetyllactosamine and N,N-Diacetyllactosamine Residues of Seminal Plasma Prolactin-Induced Protein as Ligands Recognized by Galectin-3

by Anna Kałuża, Katarzyna Trzęsicka, Damian Drzyzga and Mirosława Ferens-Sieczkowska

Int. J. Mol. Sci. 2024, 25(24), 13432; https://doi.org/10.3390/ijms252413432 - 15 Dec 2024

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Abstract

Prolactin induced-protein (PIP) has been found to be rich in immunomodulatory epitopes, including N-acetyllactosamine (LacNAc) and N,N-diacetyllactosamine (LacdiNAc) residues, which may constitute ligands for galecin-3 (Gal-3). In the current study, we aimed to investigate the reactivity of galactose- and [...] Read more.

Prolactin induced-protein (PIP) has been found to be rich in immunomodulatory epitopes, including N-acetyllactosamine (LacNAc) and N,N-diacetyllactosamine (LacdiNAc) residues, which may constitute ligands for galecin-3 (Gal-3). In the current study, we aimed to investigate the reactivity of galactose- and N-acetylgalactosamine-specific lectins with human seminal plasma PIP. Subsequently, we examined the direct interaction between seminal plasma PIP and galectin-3, and next analyzed whether there are any differences in the interaction associated with impaired semen parameters. The reactivity of terminal galactose-presenting glycans in seminal plasma PIP with Ricinus communis agglutinin I in the asthenozoospermic group was significantly higher compared to the normozoospermic fertile subjects. Investigating the reactivity of Wisteria floribunda lectin with PIP glycans, we found likewise significantly higher relative reactivity in the normozoospermic infertile as well as the oligoasthenozoopermic group compared to the control group. These results are related to the expression of LacdiNAc epitopes in the oligosaccharide chain of PIP. Finally, we observed that PIP reactivity with Wisteria floribunda lectin correlates positively with the interaction between galectin-3 and PIP in the seminal plasma. This can suggest that LacdiNAc residues are engaged in the interaction between PIP and galectin-3. Full article

(This article belongs to the Special Issue Galectins (Gals))

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11 pages, 2572 KiB

Open AccessArticle

Galectin-7 Expression in the Placentas of Women with Gestational Diabetes Mellitus

by Christina Teresa Seifert, Laura Unverdorben, Julia Knabl, Stefan Hutter, Simon Keckstein, Elisa Schmoeckel, Mirjana Kessler, Udo Jeschke, Sven Mahner, Thomas Kolben and Franziska Ganster

Int. J. Mol. Sci. 2024, 25(18), 10186; https://doi.org/10.3390/ijms251810186 - 23 Sep 2024

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Abstract

Gestational diabetes mellitus (GDM) is a common condition during pregnancy. The prevalence of GDM is continuously increasing worldwide. Due to accessible diagnostic methods and a clear understanding of risk factors, GDM can be effectively diagnosed and managed. Galectins may influence immunomodulatory and inflammatory [...] Read more.

Gestational diabetes mellitus (GDM) is a common condition during pregnancy. The prevalence of GDM is continuously increasing worldwide. Due to accessible diagnostic methods and a clear understanding of risk factors, GDM can be effectively diagnosed and managed. Galectins may influence immunomodulatory and inflammatory processes. This study examines the expression of galectin-7 in the placentas of women with gestational diabetes (GDM), compares it to its expression in healthy pregnancies, and evaluates the associated clinical outcomes. The placentas of 40 healthy women and 40 GDM placentas were included in the cohort. The expression level of galecin-7 was measured in the syncytiotrophoblast (SCT) and in the decidua of the placenta by immunohistochemistry and double immunofluorescence staining. The evaluation was performed by an immunoreactivity score (IRS). The study results show an increased expression of galectin-7 in the SCT and the decidua of GDM placentas as compared to the placentas of the control group. Elevated levels of galectin-7 were observed in both the nucleus and the cytoplasm. This study investigated the hypothesis that galectins are involved in pathophysiological processes of gestational diabetes. Statistical analysis of gene expression patterns confirmed that galectin-7 is indeed upregulated in GDM placentas. Further studies are needed to show the correlation of galectin-7 and the development and maintenance of gestational diabetes mellitus. Full article

(This article belongs to the Special Issue Galectins (Gals))

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16 pages, 3269 KiB

Open AccessArticle

Galectin-8 Contributes to Human Trophoblast Cell Invasion

by Janko Legner, Milica Jovanović Krivokuća, Aleksandra Vilotić, Andrea Pirković, Mirjana Nacka-Aleksić and Žanka Bojić-Trbojević

Int. J. Mol. Sci. 2024, 25(18), 10096; https://doi.org/10.3390/ijms251810096 - 20 Sep 2024

Cited by 1 | Viewed by 1537

Abstract

Galectins are a class of lectins that are extensively expressed in all organisms. Galectins are involved in a range of functions, including early development, tissue regeneration, cancer and inflammation. It has been shown that galectin-8 is expressed in the villous and extravillous trophoblast [...] Read more.

Galectins are a class of lectins that are extensively expressed in all organisms. Galectins are involved in a range of functions, including early development, tissue regeneration, cancer and inflammation. It has been shown that galectin-8 is expressed in the villous and extravillous trophoblast (EVT) cells of the human placenta; however, its physiological role in pregnancy establishment has not been elucidated. Taking these factors into account, we investigated the functional role of galectin-8 in HTR-8/SVneo cells—a human EVT cell line—and human primary cytotrophoblast cells isolated from a first-trimester placenta. We analyzed the effects of recombinant human galectin-8 (rh galectin-8) on the adhesion, migration and invasion of HTR-8/SVneo cells. We used qPCR, cell-based ELISA (cELISA) and gelatin zymography to study the effects of galectin-8 on mediators of these processes, such as integrin subunits alpha-1 and beta-1 and matrix metalloproteinases (MMPs)-2 and -9, on the mRNA and protein levels. Further, we studied the effects of galectin-8 on primary cytotrophoblast cells’ invasion. Galectin-8 stimulated the adhesion, migration and invasion of HTR-8/SVneo cells, as well as the invasion of primary cytotrophoblasts. In addition, the MMP-2 and -9 levels were increased, while the expression of integrins alpha-1 and beta-1 was not affected. Galectin-8 has the ability to positively affect EVTs’ invasion, so it can be considered a significant factor in the trophoblast cell invasion process. Full article

(This article belongs to the Special Issue Galectins (Gals))

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15 pages, 2857 KiB

Open AccessArticle

Galectin-1 Attenuates PDGF-Mediated AKT Signaling in Retinal Pigment Epithelial Cells

by Martina Bizzotto, Annabella Ostermaier, Caspar Liesenhoff, Wenxiu Ma, Arie Geerlof, Siegfried G. Priglinger, Claudia S. Priglinger and Andreas Ohlmann

Int. J. Mol. Sci. 2024, 25(17), 9267; https://doi.org/10.3390/ijms25179267 - 27 Aug 2024

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Abstract

Galectins have the potential to interact with transmembrane glycoproteins to modulate their functions. Since galectin-1 interacts with PDGF-Rβ, we analyzed the effect of galectin-1 on PDGF-BB-mediated AKT signaling in primary human retinal pigment epithelial (RPE) cells and galectin-1-deficient immortalized human RPE cells (LGALS1 [...] Read more.

Galectins have the potential to interact with transmembrane glycoproteins to modulate their functions. Since galectin-1 interacts with PDGF-Rβ, we analyzed the effect of galectin-1 on PDGF-BB-mediated AKT signaling in primary human retinal pigment epithelial (RPE) cells and galectin-1-deficient immortalized human RPE cells (LGALS1^−/−/ARPE-19) following incubation with PDGF-BB and galectin-1. Expression and localization of galectin-1, PDGF-Rβ and pAKT were investigated using western blot analysis and immunohistochemical staining. Cell proliferation of RPE cells was analyzed using BrdU ELISA. Following treatment of human RPE cells with human recombinant (hr)-galectin-1 and PDGF-BB, an intense clustering of PDGF-Rβ and colocalization with galectin-1 were detected. By Western blot analysis and immunocytochemistry of human RPE cells, an enhanced PDGF-BB-mediated expression of pAKT was observed, which was substantially reduced by additional incubation with hr-galectin-1. Vice versa, in LGALS1^−/−/ARPE-19 cells, the PDGF-BB-induced pAKT signal was enhanced compared to wild-type cells. Furthermore, a decreased expression of PDGF-Rβ in human RPE cells was observed after treatment with PDGF-BB and hr-galectin-1, while in untreated LGALS1^−/−/ARPE-19 cells, its constitutive expression was increased. In addition, after treatment of RPE cells with hr-galectin-1, the PDGF-BB-induced proliferation was markedly reduced. In summary, galectin-1 has the distinct potential to reduce PDGF-mediated pAKT signaling and proliferation in human RPE cells—an effect that is most likely facilitated via a decreased expression of PDGF-Rβ. Full article

(This article belongs to the Special Issue Galectins (Gals))

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13 pages, 1985 KiB

Open AccessArticle

Galectin-2 Agglutinates Helicobacter pylori via Lipopolysaccharide Containing H Type I Under Weakly Acidic Conditions

by Takaharu Sasaki, Midori Oyama, Mao Kubota, Yasunori Isshiki, Tomoharu Takeuchi, Toru Tanaka, Takashi Tanikawa, Mayumi Tamura, Yoichiro Arata and Tomomi Hatanaka

Int. J. Mol. Sci. 2024, 25(16), 8725; https://doi.org/10.3390/ijms25168725 - 10 Aug 2024

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Abstract

Galectins are β-galactoside-binding animal lectins involved in various biological functions, such as host defense. Galectin-2 and -3 are members of the galectin family that are expressed in the stomach, including the gastric mucosa and surface mucous cells. Galectin-3 exhibits aggregation and bactericidal activity [...] Read more.

Galectins are β-galactoside-binding animal lectins involved in various biological functions, such as host defense. Galectin-2 and -3 are members of the galectin family that are expressed in the stomach, including the gastric mucosa and surface mucous cells. Galectin-3 exhibits aggregation and bactericidal activity against Helicobacter pylori in a β-galactoside-dependent manner. We previously reported that galectin-2 has the same activity under neutral pH conditions. In this study, the H. pylori aggregation activity of galectin-2 was examined under weakly acidic conditions, in which H. pylori survived. Galectin-2 agglutinated H. pylori even at pH 6.0, but not at pH 5.0, correlating with its structural stability, as determined using circular dichroism. Additionally, galectin-2 binding to the lipopolysaccharide (LPS) of H. pylori cultured under weakly acidic conditions was investigated using affinity chromatography and Western blotting. Galectin-2 could bind to H. pylori LPS containing H type I, a Lewis antigen, in a β-galactoside-dependent manner. In contrast, galectin-3 was structurally more stable than galectin-2 under acidic conditions and bound to H. pylori LPS containing H type I and Lewis X. In conclusion, galectin-2 and -3 might function cooperatively in the defense against H. pylori in the stomach under different pH conditions. Full article

(This article belongs to the Special Issue Galectins (Gals))

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16 pages, 2290 KiB

Open AccessArticle

Expression of Intracellular Galectin-8 and -9 in Endometrial Cancer

by Susanne Beyer, Maya Wehrmann, Sarah Meister, Fabian Trillsch, Franziska Ganster, Elisa Schmoeckel, Stefanie Corradini, Sven Mahner, Udo Jeschke, Mirjana Kessler, Alexander Burges and Thomas Kolben

Int. J. Mol. Sci. 2024, 25(13), 6907; https://doi.org/10.3390/ijms25136907 - 24 Jun 2024

Cited by 1 | Viewed by 1543

Abstract

Endometrial cancer (EC) is a common gynecological cancer worldwide. Treatment has been improved in recent years; however, in advanced stages, therapeutic options are still limited. The expression of galectins is increased in several tumor types and that they are involved in important cell [...] Read more.

Endometrial cancer (EC) is a common gynecological cancer worldwide. Treatment has been improved in recent years; however, in advanced stages, therapeutic options are still limited. The expression of galectins is increased in several tumor types and that they are involved in important cell processes. Large studies on endometrial cancer are still pending; Specimens of 225 patients with EC were immunohistochemically stained with antibodies for Gal-8 and Gal-9. Expression was correlated with histopathological variables. The cytosolic expression of both galectins is associated with grading and survival. Cytosolic Galectin-8 expression is a positive prognostic factor for overall survival (OS) and progression-free survival (PFS), while nuclear Gal-8 expression correlates only to OS. The cytosolic presence of Galectin-9 is correlated with a better prognosis regarding OS. Our results suggest that expression of both galectins is associated with OS and PFS in EC. Further studies are needed to understand the underlying molecular mechanisms. Full article

(This article belongs to the Special Issue Galectins (Gals))

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Review

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19 pages, 1386 KiB

Open AccessReview

Galectins and Liver Diseases

by Shima Mimura, Asahiro Morishita, Kyoko Oura, Kei Takuma, Mai Nakahara, Tomoko Tadokoro, Koji Fujita, Joji Tani and Hideki Kobara

Int. J. Mol. Sci. 2025, 26(2), 790; https://doi.org/10.3390/ijms26020790 - 18 Jan 2025

Cited by 1 | Viewed by 917

Abstract

Galectins are widely distributed throughout the animal kingdom, from marine sponges to mammals. Galectins are a family of soluble lectins that specifically recognize β-galactoside-containing glycans and are categorized into three subgroups based on the number and function of their carbohydrate recognition domains (CRDs). [...] Read more.

Galectins are widely distributed throughout the animal kingdom, from marine sponges to mammals. Galectins are a family of soluble lectins that specifically recognize β-galactoside-containing glycans and are categorized into three subgroups based on the number and function of their carbohydrate recognition domains (CRDs). The interaction of galectins with specific ligands mediates a wide range of biological activities, depending on the cell type, tissue context, expression levels of individual galectin, and receptor involvement. Galectins affect various immune cell processes through both intracellular and extracellular mechanisms and play roles in processes, such as apoptosis, angiogenesis, and fibrosis. Their importance has increased in recent years because they are recognized as biomarkers, therapeutic agents, and drug targets, with many other applications in conditions such as cardiovascular diseases and cancer. However, little is known about the involvement of galectins in liver diseases. Here, we review the functions of various galectins and evaluate their roles in liver diseases. Full article

(This article belongs to the Special Issue Galectins (Gals))

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17 pages, 1872 KiB

Open AccessReview

The Possible Effects of Galectin-3 on Mechanisms of Renal and Hepatocellular Injury Induced by Intravascular Hemolysis

by Mirjana Grujcic, Marija Milovanovic, Jelena Nedeljkovic, Danijela Jovanovic, Dragana Arsenijevic, Natalija Solovjova, Vesna Stankovic, Irena Tanaskovic, Aleksandar Arsenijevic and Jelena Milovanovic

Int. J. Mol. Sci. 2024, 25(15), 8129; https://doi.org/10.3390/ijms25158129 - 25 Jul 2024

Cited by 1 | Viewed by 1688

Abstract

Intravascular hemolysis is a central feature of congenital and acquired hemolytic anemias, complement disorders, infectious diseases, and toxemias. Massive and/or chronic hemolysis is followed by the induction of inflammation, very often with severe damage of organs, which enhances the morbidity and mortality of [...] Read more.

Intravascular hemolysis is a central feature of congenital and acquired hemolytic anemias, complement disorders, infectious diseases, and toxemias. Massive and/or chronic hemolysis is followed by the induction of inflammation, very often with severe damage of organs, which enhances the morbidity and mortality of hemolytic diseases. Galectin-3 (Gal-3) is a β-galactoside-binding lectin that modulates the functions of many immune cells, thus affecting inflammatory processes. Gal-3 is also one of the main regulators of fibrosis. The role of Gal-3 in the development of different kidney and liver diseases and the potential of therapeutic Gal-3 inhibition have been demonstrated. Therefore, the objective of this review is to discuss the possible effects of Gal-3 on the process of kidney and liver damage induced by intravascular hemolysis, as well as to shed light on the potential therapeutic targeting of Gal-3 in intravascular hemolysis. Full article

(This article belongs to the Special Issue Galectins (Gals))

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