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#28837152   2017/08/24 Save this To Up

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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#28560429   2017/05/31 Save this To Up

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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#28393190   2017/04/10 Save this To Up

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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#27728777   2016/10/11 Save this To Up

A TRIM16-Galactin3 Complex Mediates Autophagy of Damaged Endomembranes.

Selective autophagy, an essential process for maintaining intracellular homeostasis, depends on precise target recognition and local activation. Reporting in Developmental Cell, Chauhan et al. (2016) elegantly demonstrate that interaction between TRIM16 and Galectin3 orchestrates the recruitment of core autophagic factors and activates selective autophagy at the site of damaged endomembranes.

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#27035870   2016/04/28 Save this To Up

Knockdown of LI-cadherin alters expression of matrix metalloproteinase-2 and -9 and galectin-3.

Liver-intestine cadherin (LI-cadherin), a novel member of the cadherin family, has been associated with the ability of a tumor to acquire an aggressive phenotype in several types of cancer. However, the exact function of LI-cadherin in the process of tumor invasion and metastasis remains predominantly unknown. To explore the effect of LI-cadherin on the regulation of matrix metalloproteinase-2 (MMP-2), MMP-9 and galectin-3 in LoVo human colorectal cancer cells, a RNA interference technique was applied to suppress the expression of LI‑cadherin. Subsequently, the mRNA levels and activities of MMP-2 and -9 were analyzed by semi-quantitative reverse transcription-polymerase chain reaction and gelatin zymography, respectively. Additionally, the protein expression level of galectin-3 was determined by western blot analysis. The results of the present study demonstrated that short hairpin RNA (shRNA)-silencing of LI-cadherin significantly increased the mRNA levels and activities of MMP‑2 and ‑9, and significantly reduced the protein levels of galectin‑3 in LoVo cells compared with control shRNA (P<0.05). These data indicate that knockdown of LI‑cadherin facilitates the invasion of cancer cells by degrading extracellular matrix components via activation of MMP‑2 and ‑9, and increases cancer cell adhesion and migration via altered expression of galectin‑3. This suggests that LI‑cadherin serves an important role in the invasion and metastasis of colorectal cancer, and may be used as a potential therapeutic target.

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#26238776   2015/09/24 Save this To Up

Small interfering RNA-induced silencing of galectin-3 inhibits the malignant phenotypes of osteosarcoma in vitro.

Osteosarcoma (OS) is the most common malignant tumor of bone. It has recently been demonstrated that galectin-3, a multifunctional β-galactoside-binding, is significantly upregulated in OS tissues, and is correlated with its progression and metastasis. However, the detailed role of galectin‑3 in the regulation of cellular biological processes in OS cells has remained to be elucidated. The present study reported that the mRNA and protein levels of galectin‑3 were significantly increased in OS tissues compared to those in their matched normal adjacent tissues. Furthermore, galectin‑3 was upregulated in three OS cell lines, Saos‑2, MG63 and U2OS, when compared with that in the human osteoblast cell line hFOB1.19. Knockdown of galectin‑3 by galectin‑3‑specific small interfering RNA markedly inhibited OS‑cell proliferation and induced cell apoptosis. Furthermore, silencing of galectin‑3 expression significantly inhibited OS cell migration and invasion, accompanied with a marked decrease in the protein expression of matrix metalloproteinase 2 and ‑9. Mechanistic investigation suggested that the mitogen‑activated protein kinase kinase/extracellular signal‑regulated protein kinase signaling pathway may be involved in the galectin‑3‑mediated OS cell invasion. In conclusion, the present study was the first to report that silencing of galectin‑3 inhibited the malignant phenotypes of osteosarcoma in vitro. Therefore, galectin-3 may serve as a potential therapeutic target for OS.

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#26165519   2015/09/24 Save this To Up

Galectin-3-induced oxidized low-density lipoprotein promotes the phenotypic transformation of vascular smooth muscle cells.

Oxidized low-density lipoprotein (oxLDL) is involved in the pathological phenotypic transformation of vascular smooth muscle cells in atherosclerosis. Galectin‑3 also has an important role in atherosclerosis. However, little is currently known regarding the effects of galectin‑3 on the oxLDL‑induced phenotypic transformation of vascular smooth muscle cells. In the present study, primary culture human umbilical vascular smooth muscle cells were treated with various oxLDL concentrations (0‑50 µg/ml) for 72 h, and phenotypic changes were subsequently recorded. The results of the present study suggested that oxLDL increases the expression levels of galectin‑3, and induces the phenotypic transformation of vascular smooth muscle cells. The oxLDL‑induced cells exhibited increased expression levels of osteopontin, a smooth muscle synthetic protein, and calponin and α‑actin, smooth muscle contractile proteins. The oxLDL‑induced changes in cellular phenotype were associated with increased migration, proliferation, and phagocytosis. Concordant with these results, oxLDL‑treated smooth muscle cells exhibited activation of canonical Wnt signaling, as determined by an increase in the protein expression levels of β‑catenin. Silencing of galectin‑3 by small interfering RNA reversed the phenotypic transformation and functional changes observed in the oxLDL‑treated cells, suggesting these changes were dependent on the activation of galectin‑3. In addition, galectin‑3 knockdown decreased the protein expression levels of β‑catenin in both the cytoplasm and nucleus; however, the mRNA expression levels of β‑catenin remained unchanged. These results suggest that galectin‑3 is responsible for the phenotypic transformation of human umbilical vascular smooth muscle cells, and the canonical Wnt/β-catenin signaling pathway may be involved in this process.

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#25221953   2015/08/11 Save this To Up

A Pilot Study of Galectin-3, HBME-1, and p27 Triple Immunostaining Pattern for Diagnosis of Indeterminate Thyroid Nodules in Cytology With Correlation to Histology.

Indeterminate thyroid nodules form a heterogenous group of lesions that constitute 5% to 30% of thyroid cytology diagnoses. We introduce a triple immunostaining protocol for subtyping. Galectin-3, HBME-1, and p27 triple immunostaining, performed on destained cytology slides and formalin-fixed paraffin-embedded tissue, was developed and applied to 51 patients retrospectively with preoperative cytologic diagnoses of follicular lesion of undetermined significance (n=40), atypia of undetermined significance (n=6), and suspicious for follicular neoplasm (n=5). The malignant rate in this series was 43.1% (22/51). A hierarchal evaluation algorithm was generated based on digital image quantitation of triple-stained histologic sections, and applied to both cytology and histology specimens. Fifty of 51 cytology cases have triple staining validated by internal controls. In cytology specimens, the individual sensitivities and specificities of p27, Galectin3, and HBME1 for cancer with 95% confidence interval are: 86.2% (0.674, 0.955)/66.7% (0.431, 0.845); 77.3% (0.542, 0.913)/72.4% (0.525, 0.866); and 72.7% (0.496, 0.884)/93.1% (0.758, 0.988), respectively. Sensitivity is increased to 95.5% (0.751, 0.998), but specificity is decreased to 69.0% (0.490, 0.840), if Galectin3 and HBME1 are both used in combination as markers for malignancy. However, the level of specificity is increased to 86.2% (0.674, 0.955) and sensitivity remains high 100% (0.808, 1) if in addition, using the Galectin3/HBME1:p27 ratio (ratio ≥2 indicating malignancy) for 2 or 3 markers positive cases. Thus, the triple staining method on cytology slides and histology sections shows a similar sensitivity/specificity/positive predictive value/negative predictive value of 100.0%/86.2%/84.0%/100.0% and 95.5%/86.2%/84.0%/96.2%, respectively (P=0.92). Overall, p27 is the most frequent single positive marker (19/50, 38% in cytology), consistent with benign nature of most indeterminate thyroid nodules. Galectin-3 and HBME-1 colocalization (positive in the same cell) was demonstrated in thyroid cancer in 45.5% (10/22) of histology sections, but in none of the normal thyroid tissues and benign thyroid lesions. This supports the notion that synchronous activation of Galectin-3 and HBME-1 occurs in thyroid malignancy and is highly specific for malignancy. We have demonstrated the performance and pattern of triple immunostaining for subtyping indeterminate thyroid nodules. Further studies and validation in different larger populations are warranted.

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#23412777   2013/04/17 Save this To Up

Glioblastoma with oligodendroglial component represents a subgroup of glioblastoma with high prevalence of IDH1 mutation and association with younger age.

Glioblastoma with an oligodendroglial component (GBMO) is recognized as a subgroup of glioblastoma (GBM); however, the molecular and clinicopathological characteristics of GBMO are obscure. We evaluated the methylation status of MGMT, IDH1/2 mutation, deletions of 1p and 19q and expression of IDH1, p53, p16, CD151, and galectin3 proteins in 42 GBMOs (32 primary and 10 secondary tumors). Our aims were to correlate our molecular findings with clinicopathologic features, and to compare molecular-to-clinical correlations in the 42 GBMOs with the corresponding correlations in 45 GBMs. GBMO was subdivided into two subgroups according to the predominant cell component comprising >50 % of tumors: the astrocytic predominant type (GBMO-A) and oligodendroglioma predominant type (GBMO-O). Methylation of MGMT, IDH1/2 mutation, and co-deletion of 1p and 19q were found in 31.0, 26.2, and 17.9 % of patients with GBMO, respectively. Clinicopathological and molecular characteristics did not differ significantly between GBMO-A and GBMO-O. However, patients with GBMO-O experienced better outcomes than patients with GBMO-A (p = 0.007). On multivariate analysis the predominant cell type was an independent prognostic factor in overall survival [hazard ratio 4.2 (95 % confidence interval 1.4-12.8), p = 0.011]. When compared to patients with classic GBM, those with GBMO were younger (49.21 vs. 57.47, p = 0.003) and more frequently had tumors with IDH1 mutation (23.8 vs. 4.4 %, p = 0.009). Survival was similar in patients with GBMO and with classic GBM. Based on these results, GBMO may represent a subgroup of GBM that is associated with IDH1 mutation and younger age, although similar to classic GBM in prognosis.

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#19686089   2010/03/05 Save this To Up

Serum levels of galectin-3 and its ligand 90k/mac-2bp in colorectal cancer patients.

Galectin-3 is an endogenous lectin that binds glycan epitopes of cell membrane and some extracellular glycoproteins such as integrins and laminin. Galectin-3 is involved in several biological activities including regulation of cellular cycle, modulation of adhesion and tumor progression and metastasis. 90K/Mac-2BP glycoprotein is also a serum galectin-3 ligand. 90K is able to modulate the immune reaction against tumors and viruses and its level increases in sera of several neoplastic diseases. In our study, we have evaluated levels of both glycoproteins in sera of non metastatic colon cancer patients. Interestingly, galectin-3 ranged higher in cancer patients than in controls (p<0.0001), particularly in more differentiated tumors (p<0.04). Moreover, 90K mean values ranged higher in right-side than in left-side colon cancer. In conclusion, serum galectin3 might represent a useful biomarker to evaluate colon cancer transformation and, together with its ligand 90K, could contribute to the characterization of colon cancer.

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