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Galectins in Cancer and Translational Research 2.0
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Galectins in Cancer and Translational Research 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".

Deadline for manuscript submissions: closed (30 June 2020) | Viewed by 24979

Special Issue Editor

Prof. Dr. Armando Bartolazzi

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Guest Editor
Laboratory of Surgical and Experimental Pathology, St Andrea University Hospital, Rome, Italy
Interests: tumor pathology; molecular pathology; cell biology; thyroid cancer; melanoma; solid tumors; molecular targeted therapy; monoclonal antibodies; immunochemistry; immunohistochemistry; galectins; CD44; integrins, adhesion molecules; cell–ECM interactions
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The unexpected interest that accompanied the Special Issue entitled: Galectins in Cancer and Translational Medicine (IJMS 2018), has led us to launch a new proposal on the same subject with the aim of gathering further information on the role played by galectins in cancer and in a variety of human diseases. Galectins (S-type lectins) are an evolutionarily conserved family of endogenous lectins that bind carbohydrates with high specificity. These molecules are found both intracellularly and in the extracellular milieu and are functionally active in converting glycan-containing information into cell biological programs. As reported in the first Special Issue of IJMS, the galectin signature of human cells likely plays a key role in regulating biological processes that are critical for cell physiology as well as for tumour growth and progression. Furthermore, the interaction of specific galectins with sugar residues on lymphoid cells and cytokines is able to modulate the immune-response. Specific galectins have been detected in different cancer types and represent potential target molecules to be considered for improving cancer diagnosis and for exploring new therapeutic strategies. Diagnostic procedures based on the expression analysis of specific galectins have already been developed and validated for clinical use. For example, galectin-3 expression analysis is widely used in clinical practice for thyroid cancer diagnosis. Interestingly, structural and functional studies on the natural or synthetic molecules able to inhibit specific galectin–glycan interactions are presently being performed in different research laboratories. Clinical trials, spanning from immunology to clinical oncology, are ongoing and promise a large amount of relevant information for translational medicine. For this reason, we are launching this new Special Issue titled: Galectins in Cancer and Translational Medicine 2.0 just in time to collect in advance original preclinical and clinical studies that represent the frontier research in tumor therapy, immunology and translational medicine.

Prof. Dr. Armando Bartolazzi
Guest Editor

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Keywords

  • galectins
  • galectin-1
  • galectin-3
  • galectin-4
  • galectin-5
  • galectin-6
  • galectin-7
  • galectin-8
  • galectin-9
  • galectin-10
  • galectin-11
  • galectin-12
  • galectin-13
  • galectin-14
  • galectin-15
  • galectins in diagnosis
  • galectins in therapy
  • galectins and immunity
  • galectins and cancer
  • galectins and human diseases

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Published Papers (5 papers)

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Research

12 pages, 770 KiB  
Article
Galectin-3, N-terminal Propeptides of Type I and III Procollagen in Patients with Atrial Fibrillation and Metabolic Syndrome
by Valery A. Ionin, Elena I. Baranova, Ekaterina L. Zaslavskaya, Elena Yu. Petrishcheva, Aleksandr N. Morozov and Evgeny V. Shlyakhto
Int. J. Mol. Sci. 2020, 21(16), 5689; https://doi.org/10.3390/ijms21165689 - 8 Aug 2020
Cited by 11 | Viewed by 2720
Abstract
The aim of this study was to determine the concentration of galectin-3, PINP and PIIINP in patients with metabolic syndrome (MS) and atrial fibrillation (AF) with an assessment of the relationship with severity of left atrium fibrosis. A total of 480 subjects were [...] Read more.
The aim of this study was to determine the concentration of galectin-3, PINP and PIIINP in patients with metabolic syndrome (MS) and atrial fibrillation (AF) with an assessment of the relationship with severity of left atrium fibrosis. A total of 480 subjects were included in the case-control study: MS patients (n = 337), 176 of whom had AF, 72 patients with AF without MS and 71 healthy subjects. Galectin-3, PINP and PIIINP blood concentrations and metabolic parameters were compared with the severity of left atrium fibrosis, measured by CARTO3. Galectin-3 in AF and MS patients is higher than in MS without AF and in healthy subjects (10.3 (4.8–15.4), 5.1 (4.3–8.8), 3.2 (2.4–4.2) ng/mL, p < 0.0001). Galectin-3 serum concentration in AF patients with MS is higher than in patients without MS: 10.3 (4.8–15.4), 6.8 (5.2–8.1) ng/mL, p = 0.0001. PINP and PIIINP concentration were higher in patients with AF and MS than in MS without AF: 3499.1 (2299.2–4567.3), 2130.9 (1425.3–2861.8) pg/mL, p < 0.0001, 94.9 (64.8–123.5), 57.6 (40.5–86.9) ng/mL, p < 0.0001. Galectin-3 correlates with PINP (r = 0.496, p < 0.001) and PIIINP concentration (r = 0.451, p < 0.0001). The correlation between galectin-3, PINP and the severity of left atrium fibrosis was found (r = 0.410, p < 0.001; r = 0.623, p < 0.001). Galectin-3 higher than 12.6 ng/mL increased the risk of AF more than five-fold. High galectin-3, PINP and PIIINP concentrations were associated with heart remodeling in MS patients and increased the risk of AF. Full article
(This article belongs to the Special Issue Galectins in Cancer and Translational Research 2.0)
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12 pages, 4003 KiB  
Article
Galectin-2 Has Bactericidal Effects against Helicobacter pylori in a β-galactoside-Dependent Manner
by Takaharu Sasaki, Rei Saito, Midori Oyama, Tomoharu Takeuchi, Toru Tanaka, Hideshi Natsume, Mayumi Tamura, Yoichiro Arata and Tomomi Hatanaka
Int. J. Mol. Sci. 2020, 21(8), 2697; https://doi.org/10.3390/ijms21082697 - 13 Apr 2020
Cited by 10 | Viewed by 3117
Abstract
Helicobacter pylori is associated with the onset of gastritis, peptic ulcers, and gastric cancer. Galectins are a family of β-galactoside-binding proteins involved in diverse biological phenomena. Galectin-2 (Gal-2), a member of the galectin family, is predominantly expressed in the gastrointestinal tract. Although some [...] Read more.
Helicobacter pylori is associated with the onset of gastritis, peptic ulcers, and gastric cancer. Galectins are a family of β-galactoside-binding proteins involved in diverse biological phenomena. Galectin-2 (Gal-2), a member of the galectin family, is predominantly expressed in the gastrointestinal tract. Although some galectin family proteins are involved in immunoreaction, the role of Gal-2 against H. pylori infection remains unclear. In this study, the effects of Gal-2 on H. pylori morphology and survival were examined. Gal-2 induced H. pylori aggregation depending on β-galactoside and demonstrated a bactericidal effect. Immunohistochemical staining of the gastric tissue indicated that Gal-2 existed in the gastric mucus, as well as mucosa. These results suggested that Gal-2 plays a role in innate immunity against H. pylori infection in gastric mucus. Full article
(This article belongs to the Special Issue Galectins in Cancer and Translational Research 2.0)
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19 pages, 3625 KiB  
Article
SUSD2 Proteolytic Cleavage Requires the GDPH Sequence and Inter-Fragment Disulfide Bonds for Surface Presentation of Galectin-1 on Breast Cancer Cells
by Mitch E. Patrick and Kristi A. Egland
Int. J. Mol. Sci. 2019, 20(15), 3814; https://doi.org/10.3390/ijms20153814 - 5 Aug 2019
Cited by 11 | Viewed by 4694
Abstract
Galectin-1 (Gal-1) is a 14 kDa protein that has been well characterized for promoting cancer metastasis and tumor immune evasion. By localizing to the cancer cell surface, Gal-1 induces T cell apoptosis through binding T cell surface receptors. The transmembrane protein, Sushi Domain [...] Read more.
Galectin-1 (Gal-1) is a 14 kDa protein that has been well characterized for promoting cancer metastasis and tumor immune evasion. By localizing to the cancer cell surface, Gal-1 induces T cell apoptosis through binding T cell surface receptors. The transmembrane protein, Sushi Domain Containing 2 (SUSD2), has been previously shown to be required for Gal-1 surface presentation in breast cancer cells. Western immunoblot analysis revealed that SUSD2 is cleaved into two fragments. However, the significance of this cleavage for Gal-1 surface localization has not been investigated. To define the location of cleavage, a mutagenesis analysis of SUSD2 was performed. Our studies demonstrated that SUSD2 is cleaved at its glycine-aspartic acid-proline-histidine (GDPH) amino acid sequence. Generation of a noncleavable SUSD2 mutant (GDPH∆-SUSD2) showed that SUSD2 cleavage was required for SUSD2 and Gal-1 plasma membrane localization. Noncleavable cysteine mutants were also unable to present Gal-1 at the cell surface, further demonstrating that SUSD2 cleavage is required for Gal-1 surface presentation. Treatment with the serine protease inhibitor, Pefabloc SC, inhibited SUSD2 cleavage in a dose dependent manner, suggesting that SUSD2 is cleaved by a serine protease. Therefore, identification and inhibition of this protease may provide a new therapeutic tool for inhibiting SUSD2 and Gal-1′s combined tumorigenic function in breast cancer. Full article
(This article belongs to the Special Issue Galectins in Cancer and Translational Research 2.0)
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15 pages, 3682 KiB  
Article
Galectin-9 Induces Mitochondria-Mediated Apoptosis of Esophageal Cancer In Vitro and In Vivo in a Xenograft Mouse Model
by Taiga Chiyo, Koji Fujita, Hisakazu Iwama, Shintaro Fujihara, Tomoko Tadokoro, Kyoko Ohura, Takanori Matsui, Yasuhiro Goda, Nobuya Kobayashi, Noriko Nishiyama, Tatsuo Yachida, Asahiro Morishita, Hideki Kobara, Hirohito Mori, Toshiro Niki, Mitsuomi Hirashima, Takashi Himoto and Tsutomu Masaki
Int. J. Mol. Sci. 2019, 20(11), 2634; https://doi.org/10.3390/ijms20112634 - 29 May 2019
Cited by 25 | Viewed by 4450
Abstract
Galectin-9 (Gal-9) enhances tumor immunity mediated by T cells, macrophages, and dendritic cells. Its expression level in various cancers correlates with prognosis. Furthermore, Gal-9 directly induces apoptosis in various cancers; however, its mechanism of action and bioactivity has not been clarified. We evaluated [...] Read more.
Galectin-9 (Gal-9) enhances tumor immunity mediated by T cells, macrophages, and dendritic cells. Its expression level in various cancers correlates with prognosis. Furthermore, Gal-9 directly induces apoptosis in various cancers; however, its mechanism of action and bioactivity has not been clarified. We evaluated Gal-9 antitumor effect against esophageal squamous cell carcinoma (ESCC) to analyze the dynamics of apoptosis-related molecules, elucidate its mechanism of action, and identify relevant changes in miRNA expressions. KYSE-150 and KYSE-180 cells were treated with Gal-9 and their proliferation was evaluated. Gal-9 inhibited cell proliferation in a concentration-dependent manner. The xenograft mouse model established with KYSE-150 cells was administered with Gal-9 and significant suppression in the tumor growth observed. Gal-9 treatment of KYSE-150 cells increased the number of Annexin V-positive cells, activation of caspase-3, and collapse of mitochondrial potential, indicating apoptosis induction. c-Jun NH2-terminal kinase (JNK) and p38 mitogen-activated protein kinase (p38) phosphorylation were activated and could be involved in apoptosis. Therefore, Gal-9 induces mitochondria-mediated apoptosis of ESCC and inhibits cell proliferation in vitro and in vivo with JNK and p38 activation. Full article
(This article belongs to the Special Issue Galectins in Cancer and Translational Research 2.0)
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8 pages, 1055 KiB  
Communication
Predictive Biomarkers for Checkpoint Inhibitor-Based Immunotherapy: The Galectin-3 Signature in NSCLCs
by Carlo Capalbo, Giorgia Scafetta, Marco Filetti, Paolo Marchetti and Armando Bartolazzi
Int. J. Mol. Sci. 2019, 20(7), 1607; https://doi.org/10.3390/ijms20071607 - 31 Mar 2019
Cited by 44 | Viewed by 9520
Abstract
Checkpoint inhibitor-based immunotherapy is opening a promising scenario in oncology, with objective responses registered in multiple cancer types. However, reliable predictive markers of tumor responsiveness are still lacking. These markers need to be urgently identified for a better selection of patients that can [...] Read more.
Checkpoint inhibitor-based immunotherapy is opening a promising scenario in oncology, with objective responses registered in multiple cancer types. However, reliable predictive markers of tumor responsiveness are still lacking. These markers need to be urgently identified for a better selection of patients that can be candidates for immunotherapy. In this pilot study, a cohort of 34 consecutive patients bearing programmed death-ligand 1 (PD-L1)-positive non-small cell lung carcinoma (NSCLC), treated with pembrolizumab, was considered. The retrospective immuno-phenotypic analysis performed on the original tumor biopsies allowed for the identification of a specific “galectin signature”, which strongly correlated with tumor responsiveness to anti PD-1 immunotherapy. We observed that the large majority of patients (about 90%) with high galectin-3 tumor expression (score 3+) showed an early and dramatic progression of the disease after three cycles of treatments. In contrast, all patients with negative or low/intermediate expression of galectin-3 in tumor cells showed an early and durable objective response to pembrolizumab, indicating galectin-3 as an interesting predictive marker of tumor responsiveness. The galectin-3 signature, at least in NSCLCs, promises a better selection of patient candidates for immunotherapy, reducing unnecessary treatment exposures and social costs. A large multicenter study is ongoing to validate this finding. Full article
(This article belongs to the Special Issue Galectins in Cancer and Translational Research 2.0)
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