• IMMUNE NETWORK
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• v.5 no.2
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• pp.105-109
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• 2005

Background: Dendritic cells (DCs) are the most potent APCs (antigen-presenting cells) and playa critical role in immune responses. Galectin-3 is a biological lectin with a beta-galactoside binding affinity. Recently, proteomic analysis revealed the presence of galectin-3 in the exosome of mature DCs. However, the expression and function of galectin-3 in DCs remains unclear yet. Methods: We used bone marrow-derived DCs of mouse and showed the expression of galectin-3 in DCs by using flow cytometry analysis and Western blot analysis. Results: Galectin-3 was determined as single band of 35 kDa in Western blot analysis. Flow cytometry analysis showed the major growth factor for DCs, granulocyte-macrophage colony stimulating factor (GM-CSF) and maturing agents, anti-CD40 monoclonal antibody (mAb) and lipopolysaccharide (LPS) consistently increased the intracellular expression of galectin-3 in DCs compared to medium alone. In addition, DCs treated with maturing agents did marginally express galectin-3 on their surface. Conclusion: This study suggests that galectin-3 in DCs may be regulated by critical factors for DC function.

• BMB Reports
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• v.53 no.4
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• pp.173-180
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• 2020

Galectin-3 is a carbohydrate-binding protein and regulates diverse functions, including cell proliferation and differentiation, mRNA splicing, apoptosis induction, immune surveillance and inflammation, cell adhesion, angiogenesis, and cancer-cell metastasis. Galectin-3 is also recommended as a diagnostic or prognostic biomarker of various diseases, including heart disease, kidney disease, and cancer. Galectin-3 exists as a cytosol, is secreted in extracellular spaces on cells, and is also detected in nuclei. It has been found that galectin-3 has different functions in cellular localization: (i) Extracellular galectin-3 mediates cell attachment and detachment. (ii) cytosolic galectin-3 regulates cell survival by blocking the intrinsic apoptotic pathway, and (iii) nuclear galectin-3 supports the ability of the transcriptional factor for target gene expression. In this review, we focused on the role of galectin-3 on translocation from cytosol to nucleus, because it happens in a way independent of carbohydrate recognition and accelerates cancer progression. We also suggested here that intracellular galecin-3 could be a potent therapeutic target in cancer therapy.

• Korean Journal of Veterinary Research
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• v.44 no.1
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• pp.83-88
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• 2004

Galectin family, endogenous ${\beta}$-galactoside-binding animal lectins, is known for the role in cell differentiation, morphogenesis, apoptosis and tumorigenesis. Galectin-3, one of family member, has been studied for its role in cell differentiation and tumor metastasis, and for its expression on epithelial cells of colon and mast cells but not in brain. Several reports, however, suggest its expression in brain including as a prion binding protein. In this report we explored possibility of galectin-3 expression in brain tissue. With Western blot and RT-PCR with rat brain tissues, we could detect galectin-3 that was not shown by conventional immunohistochemistry. Our results indicated galectin-3 was expressed in brain, and substantiate the previous report on galecin-3 as a prion-related protein in brain.

• Korean Journal of Veterinary Research
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• v.39 no.6
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• pp.1112-1118
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• 1999

Galectin-3 plays an important role in cell development, differentiation and cancer metastasis, including cell-cell/extracellular matrix (ECM) interactions and is supposed to have an effect of apoptosis on T-cells in thymic clonal selection. In this study, to know the effect of galectin-3 on thymocyte development, we used recombinant human galectin-3 (rHgal-3) from Escherichia coli, JM105, which was inserted with human gal-3 gene-transformed plasmid vector (prGal-3) to express human galectin-3. Expressed rHgal-3 was confirmed by western blot using the culture supernant of hybridoma (M3/38) producing monoclonal antibody to human galectin-3. Sepharose gel affinity chromatography was used to purify the expressed rHgal-3. Thymocytes and hepatocytes from 6-week-old male BALB/c mice were incubated with rHgal-3 and showed marked increase of apoptotic population on analysis using flow cytometry with 7-AAD in a dosedependent manner. However, rHgal-3 failed to induce apoptosis on hepatocytes. Interestingly, this apoptotic effect was not inhibited by lactose, a specific lectin domain inhibitor. From these results, we concluded that extrinsic -3 induces apoptosis on mouse thymocytes, and galectin-3 may have an apoptotic effect on T-cells in thymic clonal selection.

• Korean Journal of Veterinary Research
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• v.37 no.3
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• pp.547-554
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• 1997

Galectin-3 is known as an animal ${\beta}$-galactoside-binding lectin charicterized with S-type carbohydrate recognition domain. It plays a role in growth, adherence and movement of cells. It is, also, related to the cell transformation and metastasis of tumor cells. In this study, we have expressed and purified recombinant human galectin-3 (rHgalectin-3) using E coli system and asialofetuin affinity chromatography for the future development of monoclonal antibody to Hgalectin-3, which is suggested as the tumor marker for the gastric and thyroid gland cancers. Expressed protein was confirmed as the Hgalectin-3 by immunoblot with cross-reactive murine monoclonal antibody. Lectin activity and specificity of purified protein were, also, confirmed by the competitive inhibition with galectin-3 specific carbohydrate, lactose. Like physiological galectin-3, lectin activity of the molecule was not changed in nonreduced condition. Dimer formation, furthermore, was observed at high concentration of the protein even in the reduced condition, which is well known in physiological galectin-3. These results showed purified rHgalectin-3 has the same activity and molecular nature compared to the physiological galectin-3.

• Journal of Life Science
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• v.15 no.2 s.69
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• pp.186-191
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• 2005

Previous studies have demonstrated that expression of galectin-3, a member of family of beta-galactoside-binding animal lectin, is associated with pathological conditions including cancer, atherosclerosis, and viral infection. An increase of this lectin has been observed after infection by Kirsten murine sarcoma, human T lymphotropic virus-l (HTLV-l), and human immunodeficiency virus-l (HIV-l). Viral transactivation protein Tax of HTLV-l mediates the increase in the lectin. In case of HIV-1, there are evidences that Tat would be related with increase in galectin-3. We investigated whether Tat directly induced galectin-3 expression in cells. We found that HIV-l tat gene activated galectin-3 promoter in RAW264.7 cells. To demonstrate direct induction of galectin-3 by HIV-l tat, we transfected the tat into a rabbit smooth muscle cell line (Rb1) and obtained RblTatCl-2, a clone of cell stably transfected with tat gene. The Rb1TatCl-2 cells exhibited activation of LTR promoter and up-regulation of galectin-3 transcript as well as protein. Our results indicate that HIV-l tat alone is sufficient to induce the expression of galectin-3. The Rb1TatCl-2 cells could be valuable for study of the effect of HIV-1 tat on expression of cellular genes.

• Journal of Applied Biological Chemistry
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• v.43 no.3
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• pp.131-135
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• 2000

Human polymorphonuclear neutrophils undergo diaphoresis after a selectin-mediated rolling on the endothelial cells of the blood vessel wall. Extravasation is believed to be an integrin-mediated process. Galectin-1 is a small dimeric beta-galactoside-binding protein synthesized by the endotherial cells and present in the perivascular connective tissue. In this study we suggest the possible role of galectin-1 in extravasation of the activated neutrophils. MAL lectin binding study showed, that f-MetLeuPhe-activated neutrophils decrease surface sialylation and increase galectin-1 binding via exposure of new galectin-1 binding sites. Desialylated HL-60 cells also show the same decrease in MAL binding and increase in galectin-1 binding, an increase which was not observed in the presence of lactose. Galectin-1 blotting analysis detected two possible major ligands (approximately 120 and 160 kDa) of galectin-1 from the desialylated HL-60 cell lysates.

• Korean Journal of Veterinary Research
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• v.48 no.1
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• pp.1-8
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• 2008

The testis and epididymis are important organs of the male reproductive system; the functionis to produce, mature, transport, and store sperm. It is important to understand the localization and expressionof specific proteins based for the studies of its physiological processes. In this study, we investigated theexpression and distribution of galectin-3, one of beta-galactoside-binding proteins, in the testis andepididymis of mouse using western blot and imunohistochemistry. Western blot analysis revealed that theexpression of galectin-3, 29 kDa protein, was low in the testis. In the epididymis, high expression wasdetected in the body and tail part, but moderate expression in the head part. By immunohistochemicalanalysis, we found that positive localization of galectin-3 was detected in some myoid cells and Leydigin the epithelium of epididymis, especially in the epithelium of both body and tail of epididymis. Collectively,these results suggest that galectin-3 is constitutively expressed in the testis and epididymis of mouse withvarying intensity, and the role of galectin-3 in the male reproductive organ may be involved in the specificfunction of its structures.

• Journal of Pharmacopuncture
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• v.15 no.3
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• pp.19-30
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• 2012

Objectives: Many efforts have shown multi-oncologic roles of galectin-3 for cell proliferation, angiogenesis, and apoptosis. However, the mechanisms by which galectin-3 is involved in cell proliferation are not yet fully understood, especially in human colon cancer cells. Methods: To cluster genes showing positively or negatively correlated expression with galectin-3, we employed human colon cancer cell lines, SNU-61, SNU-81, SNU-769B, SNU-C4 and SNU-C5 in high-throughput gene expression profiling. Gene and protein expression levels were determined by using real-time quantitative polymerase chain reaction (PCR) and western blot analysis, respectively. The proliferation rate of human colon cancer cells was measured by using a 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide (MTT) assay. Results: Expression of ${\gamma}$-aminobutyric acid B receptor 1 (GABABR1) showed a positive correlation with galectin-3 at both the transcriptional and the translational levels. Down-regulation of galectin-3 decreased not only GABABR1 expression but also the proliferation rate of human colon cancer cells. However, Korean herbal extract, HangAmDan-B (HAD-B), decreased expression of GABABR1 without any expressional change of galectin-3, and offset ${\gamma}$-aminobutyric acid (GABA)-enhanced human colon cancer cell proliferation. Conclusions: Our present study confirmed that GABABR1 expression was regulated by galectin-3. HAD-B induced galectin-3-independent down-regulation of GABABR1, which resulted in a decreased proliferation of human colon cancer cells. The therapeutic effect of HAD-B for the treatment of human colon cancer needs to be further validated.

• Korean Journal of Veterinary Research
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• v.53 no.3
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• pp.159-162
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• 2013

Galectin-3 is a ${\beta}$-galactoside-binding lectin that plays a role in neuroinflammation through cell migration, proliferation, and apoptosis. In the present study, regulation of galectin-3 was examined in the brain of mice infected with the Daniel strain of Theiler's murine encephalomyelitis virus (TMEV) at days 7 and 81 post-infection by immunohistochemistry. Immunohistochemistry revealed that galectin-3 was mainly localized in ionized calcium-binding adapter 1-positive macrophages/activated microglia, but not in Iba-1-positive ramified microglia. Galectin-3 was also weakly detected in some astrocytes in the same encephalitic lesions, but not in neurons and oligodendrocytes. Collectively, the present findings suggest that galectin-3, mainly produced by activated microglia/macrophages, may be involved in the pathogenesis of virus induced acute inflammation in the early stage as well as the chronic demyelinating lesions in Daniel strain of TMEV induced demyelination model.