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Hypoxia‑induced galectin‑3 enhances RhoA function to activate the motility of tumor cells in non‑small cell lung cancer.

Galectin‑3 plays crucial roles in tumor progression. However, in non‑small cell lung cancer (NSCLC), it remains unclear whether the hypoxic tumor microenvironment enhances galectin‑3‑induced cell motility. We investigated galectin‑3 expression in NSCLC cells under hypoxia, and the possible molecular mechanisms by which galectin‑3 influences tumor aggressiveness. Galectin‑3 levels in NSCLC cell lines under hypoxia were assessed using reverse transcription PCR and western blotting. To clarify the role of endogenous galectin‑3, the effect of galectin‑3 knockdown in NSCLC cells was investigated using scratch and invasion assays. The expression and clinicopathological significance of galectin‑3 in 57 patients with pN0M0 invasive pulmonary adenocarcinoma were investigated by immunohistochemistry. Both mRNA and protein levels of galectin‑3 in the NSCLC cell lines A549 and LK‑2 were upregulated by hypoxia. As revealed by scratch and invasion assays, the cell migratory and invasive activities were significantly increased under hypoxia, but were reduced by galectin‑3 knockdown. Notably, addition of galectin‑3 to the media did not improve the cell motility impaired by galectin‑3 knockdown. To clarify the role of endogenous galectin‑3 in the enhancement of tumor cell motility under hypoxia, we focused on the function of RhoA. RhoA level in the plasma membrane, but not in the cytoplasm, was increased under hypoxia and decreased by galectin‑3 knockdown. RhoA activity was significantly enhanced under hypoxia and effectively inhibited by galectin‑3 knockdown. In patients with pN0M0 invasive pulmonary adenocarcinoma, higher galectin‑3 expression on tumor cells was significantly associated with tumor cell invasion into microvessels and tumor recurrence after surgery. These data demonstrate that in NSCLC cells under hypoxia, upregulated galectin‑3 levels increase the localization of RhoA to the plasma membrane, thus enhancing RhoA activity, which is associated with aggressive cell motility. In pN0M0 invasive pulmonary adenocarcinoma, galectin‑3 is a potential biomarker for predicting tumor recurrence after radical surgery.

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Histological investigation of human glaucomatous eyes: Extracellular fibrotic changes and galectin 3 expression in the trabecular meshwork and optic nerve head.

Glaucoma is a leading cause of irreversible vision loss and is associated with fibrotic changes in two ocular tissues-the optic nerve head (ONH) and trabecular meshwork (TM). We investigated the differences in extracellular matrix components (ECM) including collagen, elastin, transforming growth factor beta-2, type-II receptor (TGFβRII) and Galectin3 (Gal3) in the glaucomatous human eyes to quantify fibrotic changes in ONH and TM. Glaucomatous and control human donor eyes were prepared for chemical and immunological staining to quantify ECM protein expression in the TM and ONH. Chemical staining included: Trichrome (collagen), Vernhoeff-Van Giesen (elastin) and Sirius Red (collagen). Immunohistochemistry was used to determine levels of Gal3 and TGFβ2RII. Quantitative analyses were performed using Image J software. Student's t-test was used to compare groups and Pearson's test was used to determine correlations P-values of 0.05 (or less) were considered statistically significant. Deposition of ECM proteins was elevated in glaucomatous tissues. There was increased collagen (P = 0.0469), Gal3 (P < 0.0001) and TGFβ2RII (P = 0.0005) in the TM of glaucomatous eyes. Likewise, collagen (P = 0.0517) and Galectin3 (P = 0.041) were increased in the ONH glaucomatous eyes. There was a correlation of TGFβRII with Gal3 in the TM (P < 0.0001) and optic nerve (P = 0.0003). The TM and ONH of glaucomatous eyes showed increased expression of ECM proteins supporting a fibrotic pathology. Galectin3 and TGFβ-2R II showed a positive correlation in TM and optic nerve supporting co-localization and suggesting their potential role in the glaucoma fibrotic process. Clin. Anat. 31:1031-1049, 2018. © 2018 The Authors. Clinical Anatomy published by Wiley Periodicals, Inc. on behalf of American Association of Clinical Anatomists.

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Label-Free Graphene Oxide-Based Surface Plasmon Resonance Immunosensor for the Quantification of Galectin-3, a Novel Cardiac Biomarker.

We report the first optical biosensor for the novel and important cardiac biomarker, galectin-3 (Gal3), using the anti-Gal3 antibody as a biorecognition element and surface plasmon resonance (SPR) for transducing the bioaffinity event. The immunosensing platform was built at a thiolated Au surface modified by self-assembling four bilayers of poly(diallyldimethylammonium chloride) and graphene oxide (GO), followed by the covalent attachment of 3-aminephenylboronic acid (3ABA). The importance of GO, both as the anchoring point of the antibody and as a field enhancer for improving the biosensor sensitivity, was critically discussed. The advantages of using 3ABA to orientate the anti-Gal3 antibody through the selective link to the Fc region were also demonstrated. The new platform represents an interesting alternative for the label-free biosensing of Gal3 in the whole range of clinically relevant concentrations (linear range between 10.0 and 50.0 ng mL, detection limit of 2.0 ng mL) with successful application for Gal3 biosensing in enriched human serum samples.

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β3GnT8 Promotes Colorectal Cancer Cells Invasion via CD147/MMP2/Galectin3 Axis.

β1,3-N-acetylglucosaminyltransferase (β3GnT8) and β3GnT2 are key enzymes that catalyzes the formation of polylactosamine glycan structures by transferring GlcNAc to tetra-antennary β1-6-branched -glycan and it also has an important effect on the progression of various types of human cancer. They have been reported to participate in tumor invasion and metastasis by regulating the expression of matrix metalloproteinases (MMPs), CD147, and polylactosamine. However, whether β3GnT8 and β3GnT2 play a role in colorectal cancer and, if so, the underlying mechanisms remain unclear. In our study, we detected the expression of β3GnT8, CD147, MMP2, and galectin3 by immunohistochemistry on 90 paraffin-embedded slices. And β3GnT8, CD147, MMP2, and galectin3 were over-expressed in colorectal cancer tissues. We found that overexpression of β3GnT8 and β3GnT2 promoted invasion of colorectal cancer cells, whereas knockdown of β3GnT8 and β3GnT2 inhibited the invasive activity. Mechanistically, β3GnT8 and β3GnT2 regulated the expression of HG-CD147 and the level of polylactosamines in colorectal cancer cells. Together, these results illustrate that the novel role and the molecular mechanism of β3GnT8 and β3GnT2 in promotion of colorectal cancer invasion. These results suggest that the potential use of β3GnT8 as a tumor target for the therapy of colorectal cancer.

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Papillary carcinoma in thyroglossal duct cyst: Diagnosis by fine-needle aspiration cytology and immunocytochemistry.

Carcinoma associated with thyroglossal duct cyst (TDC) is extremely rare and when it occurs it is invariably papillary carcinoma. A 36-year-old man presented with a midline swelling in the upper part of neck, which was a cystic lesion with multiple septae in ultrasonogram, indicating a thyroglossal duct cyst. The CT scan findings also corroborated the ultrasound report. Fine needle aspiration (FNA) smears showed hemosiderin laden cyst macrophages and occasional papillary cluster of neoplastic cells with central psammoma body and rare intranuclear cytoplasmic inclusions. The neoplastic cells revealed positive reaction for thyroglobulin, galectin3, and CD44. FNA cytodiagnosis was thyroglossal duct cyst with cytologic features suggestive of papillary carcinoma. The histopathological diagnosis of the resected lesion, however, was metastatic papillary thyroid carcinoma in lymph node with cystic changes; there was positive reaction for thyroglobulin, galectin3, HBME1, and CK. Following this histopathology report, thyroidectomy was performed, which revealed lymphocytic thyroiditis and no evidence of papillary carcinoma. Review of paraffin sections of upper midline neck mass showed a cavity bound by thick fibrocollageneous wall and lined partly by epithelium consistent with papillary carcinoma. The cyst wall showed dense lymphomononuclear cell infiltration and germinal center formation. There were foci of papillary carcinoma in the cyst wall with frequent nuclear grooves, cerebriform nuclei and intranuclear cytoplasmic inclusions. The reviewed histopathological diagnosis was consistent with papillary carcinoma in thyroglossal duct cyst. Thus, the FNA cytodiagnosis of a rare case of papillary carcinoma in thyroglossal duct cyst, led to review and change in histopathological diagnosis achieving cyto-histopathological correlation.

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[Galectin3 Regulates Transforming Growth Factor-β-induced Epithelial-mesenchymal].

Objective To explore the role of Galectin3 in transforming growth factor-β(TGF-β)-induced epithelial-mesenchymal transition (EMT) in A549 cells. Methods Galectin3 was over-expressed in an A549 cell line. EMT was induced in lung cancer A549 cells by adding TGF-β. The expressions of Galectin3,E-cadherin,and vimentin were determined by Western blot. The protein expression of E-cadherin and the morphological changes of the cells were detected by immunofluorescence. Cellular proliferation was analyzed with cell counting kit-8,and the cellular migration and invasion was measured by scratches healing and Transwell assay,respectively.Results When only Galectin3 was over-expressed in A549 cell line,the expression levels of EMT-related proteins such as E-cadherin and vimentin were not changed,and the abilities of cellular proliferation,invasion,and migration were not changed either. When the EMT was induced by TGF-β in A549 cells,the E-cadherin expression was down-regulated and the vimentin expression was up-regulated in A549 cells with Galectin3 over-expression. There was no significant change in cellular proliferation,whereas the abilities of cellular invasion and migration were enhanced.Conclusion The TGF-β-induced EMT in A549 cells can be enhanced by Galectin3.

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Galectin-3 as a novel biomarker for disease diagnosis and a target for therapy (Review).

Galectin-3 is a member of the galectin family, which are β‑galactoside‑binding lectins with ≥1 evolutionary conserved carbohydrate‑recognition domain. It binds proteins in a carbohydrate‑dependent and ‑independent manner. Galectin‑3 is predominantly located in the cytoplasm; however, it shuttles into the nucleus and is secreted onto the cell surface and into biological fluids including serum and urine. It serves important functions in numerous biological activities including cell growth, apoptosis, pre‑mRNA splicing, differentiation, transformation, angiogenesis, inflammation, fibrosis and host defense. Numerous previous studies have indicated that galectin‑3 may be used as a diagnostic or prognostic biomarker for certain types of heart disease, kidney disease and cancer. With emerging evidence to support the function and application of galectin‑3, the current review aims to summarize the latest literature regarding the biomarker characteristics and potential therapeutic application of galectin‑3 in associated diseases.

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Lysosomotropism depends on glucose: a chloroquine resistance mechanism.

There has been long-standing interest in targeting pro-survival autophagy as a combinational cancer therapeutic strategy. Clinical trials are in progress testing chloroquine (CQ) or its derivatives in combination with chemo- or radiotherapy for solid and haematological cancers. Although CQ has shown efficacy in preclinical models, its mechanism of action remains equivocal. Here, we tested how effectively CQ sensitises metastatic breast cancer cells to further stress conditions such as ionising irradiation, doxorubicin, PI3K-Akt inhibition and serum withdrawal. Contrary to the conventional model, the cytotoxic effects of CQ were found to be autophagy-independent, as genetic targeting of ATG7 or the ULK1/2 complex could not sensitise cells, like CQ, to serum depletion. Interestingly, although CQ combined with serum starvation was robustly cytotoxic, further glucose starvation under these conditions led to a full rescue of cell viability. Inhibition of hexokinase using 2-deoxyglucose (2DG) similarly led to CQ resistance. As this form of cell death did not resemble classical caspase-dependent apoptosis, we hypothesised that CQ-mediated cytotoxicity was primarily via a lysosome-dependent mechanism. Indeed, CQ treatment led to marked lysosomal swelling and recruitment of Galectin3 to sites of membrane damage. Strikingly, glucose starvation or 2DG prevented CQ from inducing lysosomal damage and subsequent cell death. Importantly, we found that the related compound, amodiaquine, was more potent than CQ for cell killing and not susceptible to interference from glucose starvation. Taken together, our data indicate that CQ effectively targets the lysosome to sensitise towards cell death but is prone to a glucose-dependent resistance mechanism, thus providing rationale for the related compound amodiaquine (currently used in humans) as a better therapeutic option for cancer.

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Modified citrus pectin inhibits galectin-3 function to reduce atherosclerotic lesions in apoE-deficient mice.

Galectin-3 is a carbohydrate-binding lectin, which has been implicated in the modulation of atherosclerotic pathophysiology, and is highly expressed in monocytes, macrophages and endothelial cells within atherosclerotic plaques. Modified citrus pectin (MCP) is produced from citrus pectin via pH and temperature modifications, which break it into shorter, non‑branched, galactose‑rich carbohydrate chains. MCP is able to tightly bind with galectin‑3, via recognition of its carbohydrate recognition domain, and facilitates the modulation of galectin‑3‑induced bioactivity. The present study explored the effects of MCP on the initiation of atherosclerosis. Eight‑week‑old apolipoprotein E‑deficient mice were treated with 1% MCP and fed an atherogenic diet for 4 weeks. The effects of MCP on atherosclerotic initiation were determined by pathological analysis and scanning electron microscope (SEM) imaging. MCP treatment reduced the size of atherosclerotic lesion areas, which was accompanied by decreased numbers of macrophages and smooth muscle cells (SMCs). Furthermore, SEM examination of the surface of the atheroma‑prone vessel wall indicated that MCP treatment reduced endothelial injury. To analyze the effects of MCP on monocyte adhesion, firstly, oxidized‑low density lipoprotein and various concentrations of MCP (0.025, 0.05, 0.1 and 0.25%) were incubated with the human umbilical vein endothelial cells (HUVECs) for stimulation and following this, the U937 cells were plated onto the HUVECs. The results revealed that MCP reduced the adhesion of U937 monocytes to HUVECs, indicating the adhesion-inhibiting effects of MCP. In conclusion, the present study revealed that MCP, a galectin‑3 inhibitor, reduced the size of atherosclerotic lesions by inhibiting the adhesion of leucocytes to endothelial cells. Inhibition of galectin‑3 function may be a therapeutic strategy for the treatment of atherosclerosis.

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Galectin‑3 induces the phenotype transformation of human vascular smooth muscle cells via the canonical Wnt signaling.

Galectin‑3, a galactoside‑binding protein, is highly expressed in carotid plaques and plays an important role in the atherosclerotic lesions. The phenotype transformation of vascular smooth muscle cells is the basic pathological change of atherosclerosis. This study investigated the effects of exogenous galectin‑3 on the function and phenotype transformation of human umbilical vascular smooth muscle cells (HUSMC). In this study, we treated vascular smooth muscle cells with recombinant galectin‑3 and tested its effect on cell proliferation, migration, and phenotype transformation. Our results showed that exogenous galectin‑3 promoted human umbilical vascular smooth muscle cells (HUSMC) proliferation and migration. Exogenous galectin‑3 enhanced the expression of the smooth muscle synthetic protein osteopontin, smooth muscle contractile proteins calponin and smooth muscle α‑actin. The galectin‑3‑induced change in cell phenotype was associated with the activation of canonical Wnt signaling, as measured by β‑catenin axin2 and cyclin D1 expression. β‑catenin inhibition by small interfering RNA reduced cell proliferation, decreased cell motility, and blocked galectin‑3‑induced phenotype transformation of human umbilical vascular smooth muscle cells (HUSMC). Our data suggest galectin‑3 promotes the phenotype transformation of human umbilical vascular smooth muscle cells (HUSMC) by activating Wnt/β‑catenin signaling pathway.

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