Human Ecalectin, a Variant of Human Galectin-9, Is a Novel Eosinophil Chemoattractant Produced by T Lymphocytes

Matsumoto, Ryoji; Matsumoto, Hiroyuki; Seki, Masako; Hata, Mieko; Asano, Yusuke; Kanegasaki, Shiro; Stevens, Richard L; Hirashima, Mitsuomi

doi:10.1074/jbc.273.27.16976

Cited by 281 publications

(234 citation statements)

References 66 publications

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“…To date, 15 members of the galectin family have been identified (Gray et al, 2004). ) is a member of them, and it was first identified as an eosinophil chemoattractant and activation factor (Matsumoto et al, 1998;Matsushita et al, 2000; Zhao-Yang Zhang 1,2 , Jia-Hong Dong 2 *, Yong-Wei Chen 2 , Xian-Qiang Wang 2 , Chong-Hui Li 2 , Jian Wang 2 , Guo-Qiang Wang 2 , Hai-Lin Li 2 , Xue-Dong Wang 2 Matsumoto et al, 2002;Saita et al, 2002). Subsequent studies revealed that Gal-9, similar to other galectins, modulated a variety of biological functions, such as cell aggregation and adhesion, apoptosis of tumor cells, and others (Asakura et al, 2002;Hirashima et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Galectin-9 Acts as a Prognostic Factor with Antimetastatic Potential in Hepatocellular Carcinoma

Zhang¹,

Dong²,

Chen³

et al. 2012

Asian Pacific Journal of Cancer Prevention

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Considerable research has been conducted concerning galectin-9 and carcinomas, but little information is available about any relation with the hepatocellular carcinoma. In this study, we employed a small interfering RNA (siRNA) targeting galectin-9 to down-regulate the expression in HepG2 cells. As a result, after galectin-9 expression was reduced, cell aggregation was suppressed, while other behaviour such as the proliferation, adhesion and invasion to ECM, cell-endothelial adhesion and transendothelial invasion of the cells were markedly enhanced. When tumors of 200 patients with hepatocellular carcinoma were tested for galectin-9 expression by immunohistochemistry, binding levels demonstrated intimate correlations with the histopathologic grade, lymph node metastasis, vascular invasion and intrahepatic metastasis (P<0.05). Moreover, survival analysis indicated that patients with galectin-9 expression had much longer survival time than those with negative lesions, and the Log-rank test indicated that this difference was statistical significant (P<0.0001). The Cox proportional hazards model suggested that negative galectin-9 expression in hepatocellular carcinoma represented a significant risk factor for patient survival. We propose that galectin-9 might be a new prognostic factor with antimetastatic potential in patients with hepatocellular carcinoma.

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Section: Introductionmentioning

confidence: 99%

Galectin-9 Acts as a Prognostic Factor with Antimetastatic Potential in Hepatocellular Carcinoma

Zhang¹,

Dong²,

Chen³

et al. 2012

Asian Pacific Journal of Cancer Prevention

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“…Antibodies against galectin-1, -3, and -9 were raised in our laboratories by injecting recombinant galectins to rabbits (16,33).…”

Section: Methodsmentioning

confidence: 99%

“…Recent studies demonstrate that some galectins act as immunomodulators and cell adhesion modulators (25,(27)(28)(29)(30)(31)(32)(33)(34)(35). We recently found that galectin-3 binds to L. major through L. major-specific poly-␤-galactosyl epitope (Gal␤1-3) n (16).…”

mentioning

confidence: 99%

Specific Recognition of Leishmania major Poly-β-galactosyl Epitopes by Galectin-9

Pelletier

Hashidate

Urashima

et al. 2003

Journal of Biological Chemistry

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102

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Leishmania parasites are the causative agents of leishmaniasis, manifesting itself in a species-specific manner. The glycan epitopes on the parasite are suggested to be involved in the Leishmania pathogenesis. One of such established species-unique glycan structures is the poly-␤-galactosyl epitope (Gal␤1-3) n found on L. major, which can develop cutaneous infections with strong inflammatory responses. Interestingly, the polygalactosyl epitope is also suggested to be involved in the development of the parasites in its host vector, sand fly. Thus, the recognition of the galactosyl epitope by lectins expressed in host or sand fly should be implicated in the species-specific manifestations of leishmaniasis and in the parasite life cycle, respectively. We recently reported that one host ␤-galactoside-binding protein, galectin-3, can distinguish L. major from the other species through its binding to the poly-␤-galactosyl epitope, proposing a role for galectin-3 as an immunomodulator that could influence the L. major-specific immune responses in leishmaniasis. Here we report that galectin-9 can also recognize L. major by binding to the L. major-specific polygalactosyl epitope. Frontal affinity analysis with different lengths of poly-␤-galactosyllactose revealed that the galectin-9 affinity for polygalactose was enhanced in proportion to the number of Gal␤1-3 units present. Even though both galectins have comparable affinities toward the polygalactosyl epitopes, only galectin-9 can promote the interaction between L. major and macrophages, suggesting distinctive roles for the galectins in the L. major-specific development of leishmaniasis in the host.

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“…3 Galectin-9 is a tandem-repeat type galectin, and has been shown to be involved in a variety of cellular functions, such as cell adhesion, proliferation, and apoptosis. [4][5][6][7][8][9][10] Moreover, recent studies have indentified anti-cancer properties of galectin-9 against several cancers. [11][12][13][14][15] In this study, we show the anti-multiple myeloma (MM) activity of a recombinant mutant form of human galectin-9 (hGal9) through the activation of c-Jun NH 2 -terminal kinase (JNK) and p38 mitogen-activated protein kinase (MAPK) signaling pathways, those share crucial roles in the survival and death of myeloma cells.…”

Section: Introductionmentioning

confidence: 99%

Galectin-9 exhibits anti-myeloma activity through JNK and p38 MAP kinase pathways

et al. 2010

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Galectins constitute a family of lectins that specifically exhibit the affinity for b-galactosides and modulate various biological events. Galectin-9 is a tandem-repeat type galectin with two carbohydrate recognition domains and has recently been shown to have an anti-proliferative effect on cancer cells. We investigated the effect of recombinant protease-resistant galectin-9 (hGal9) on multiple myeloma (MM). In vitro, hGal9 inhibited the cell proliferation of five myeloma cell lines examined, including a bortezomib-resistant subcell line, with IC 50 between 75.1 and 280.0 nM, and this effect was mediated by the induction of apoptosis with the activation of caspase-8, -9, and -3. hGal9-activated Jun NH 2 -terminal kinase (JNK) and p38 MAPK signaling pathways followed by H2AX phosphorylation. Importantly, the inhibition of either JNK or p38 MAPK partly inhibited the anti-proliferative effect of hGal9, indicating the crucial role of these pathways in the anti-MM effect of hGal9. hGal9 also induced cell death in patient-derived myeloma cells, some with poor-risk factors, such as chromosomal deletion of 13q or translocation t(4;14)(p16;q32). Finally, hGal9 potently inhibited the growth of human myeloma cells xenografted in nude mice. These suggest that hGal9 is a new therapeutic target for MM that may overcome resistance to conventional chemotherapy.

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Human Ecalectin, a Variant of Human Galectin-9, Is a Novel Eosinophil Chemoattractant Produced by T Lymphocytes

Cited by 281 publications

References 66 publications

Galectin-9 Acts as a Prognostic Factor with Antimetastatic Potential in Hepatocellular Carcinoma

Galectin-9 Acts as a Prognostic Factor with Antimetastatic Potential in Hepatocellular Carcinoma

Specific Recognition of Leishmania major Poly-β-galactosyl Epitopes by Galectin-9

Galectin-9 exhibits anti-myeloma activity through JNK and p38 MAP kinase pathways

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