• IMMUNE NETWORK
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• 제5권2호
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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.

• Journal of Applied Biological Chemistry
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• 제43권3호
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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.

• 한국어병학회지
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• 제26권3호
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• pp.255-263
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• 2013

선천성 면역반응은 감염성 질병에 대한 저항력이 부족한 초기 발달단계의 자치어에게 중요하다. 특히 lectin은 선천성 면역반응에 많은 기여를 하고 있으며 종류 또한 다양하다. Lectin의 종류 중 하나인 galectin은 어류 점액 내에 존재하며 선천적으로 외부 병원체로부터 숙주를 보호하는 기능을 지니고 있다. 하지만 어류 galectin과 초기발생단계 시기와 관련된 연구들은 부족한 실정이다. 본 연구는 넙치에서 발현되는 galecin-1을 통하여 자치어의 초기발생단계별 그리고 성어의 조직별 발현을 조사하였다. 초기발생단계별 galectin 발현을 조사한 결과, 부화 전 수정란의 낭배기부터 galectin-1 유전자의 발현이 시작되었으며, 부화 후 25일까지 서서히 증가하였다. 부화 후 30~35일에 galectin-1 유전자의 발현량이 급격하게 증가하였고, 그 이후의 galecin-1 유전자의 발현량은 서서히 감소하였다. 성어 (5개월령, 29개월령)의 조직별 galectin 발현을 조사한 결과, 근육, 장, 지느러미, 위, 눈 조직 순서로 높게 발현하였고, 이외의 조직에서는 발현이 나타나지 않았다. 초기발생단계에서 galectin-1의 발현이 증가되는 것은 낭배기부터 넙치의 근육, 지느러미 그리고 눈 조직이 형성되고 galectin의 분비가 시작되어 기능을 나타내기 때문인 것으로 추측된다. 부화 후 30일부터 galectin의 발현량이 많이 증가하는 것은 장과 위 조직이 활성화됨에 따라 점액의 분비량이 증가하여 galectin의 발현량 또한 증가하는 것으로 판단된다. 이로써 넙치 초기발생단계 시기의 galectin-1 유전자의 발현패턴과 galectin이 점액 내에 다량 포함되어 있는 것을 확인하였으며, galectin의 발현은 선천적 면역반응으로 넙치의 초기발생단계 시기와 성어기에 중요할 것으로 판단된다.

• BMB Reports
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• 제53권4호
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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.

• 대한수의학회지
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• 제44권1호
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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.

• Asian-Australasian Journal of Animal Sciences
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• 제21권2호
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• pp.167-176
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• 2008

Galectins are a group of animal lectins consisting of galectin-type carbohydrate recognition domains (CRD) with relatively minor domains. The biological properties of galectins include the regulation of inflammation, intercellular adhesion, cell differentiation and cell death. The diverse kinds of galectin suggest variety in their biological roles. Galectin-1 is released during adipocyte differentiation and is associated with fat which is one of the important factors for meat quality. To verify expression level, a 0.5 kb clone of galectin-1 was obtained from cDNA prepared from back fat tissue of a Sancheong Berkshire pig with good quality meat, and the galectin-1 gene identified. The deduced amino acid sequence of the galectin-1 gene was compared with those obtained from other species. By using RT-PCR and Real time-PCR, an attempt was made to determine the expression level of galectin-1 and to compare with various tissues (tenderloin and back fat) taken from pigs in different groups. Grouping of pigs was based on growth-stage (weighing 60, 80, and 110 kg) and the sub-speciation (Yorkshire and Sancheong Berkshire pigs). We attempted to determine influences of pig species, growth stages and tissue variations on the expression level of the galectin-l gene and it was revealed that the expression pattern of the galectin-1 gene was significantly different (p<0.01 or p<0.05). Galectin-1 genes were expressed more highly in the back fat tissues of pigs weighing 110 kg than in those weighing 60 kg or 80 kg. However, the lowest expression was seen in the tenderloin tissues of pigs weighing 110 kg. Sancheong Berkshire pigs showed higher expression of the galectin-1 gene compared to Yorkshire pigs. Accordingly, it is considered that the expression pattern of the galectin-1 gene influences the growth of back fat tissues and the pig speciation relationship. Previous studies suggested that different expression of galectin-1 genes represents variety among the breeds and is closely related to fat tissue growth, conjugation and catabolism. Further, this study suggests that the expression of galectin-1 at a specific growth stage and tissue contributes significantly to the overall meat quality of Sancheong Berkshire pigs.

• 대한수의학회지
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• 제37권3호
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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.

• 생명과학회지
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• 제15권2호
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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.

• 대한수의학회지
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• 제39권6호
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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.

• 대한수의학회지
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• 제48권1호
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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.