Selective Eosinophil Adhesion to Fibroblast Via IFN-γ-Induced Galectin-9

Asakura, Hirofumi; Kashio, Yumiko; Nakamura, Kazuhiro; Seki, Masako; Dai, Shuyan; Shirato, Yukako; Abedin, Mohammad J.; Yoshida, Naoko; Nishi, Nozomu; Imaizumi, Tadaatsu; Saita, Naoki; Toyama, Yoshihiro; Takashima, Hitoshi; Nakamura, Takanori; Ohkawa, Motoomi; Hirashima, Mitsuomi

doi:10.4049/jimmunol.169.10.5912

Cited by 132 publications

(90 citation statements)

References 42 publications

(31 reference statements)

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“…These results are reasonable because Gal-9 expression in endothelial cells and fibroblasts can be up-regulated by interferon-␥ (IFN␥) (31,32), and the levels of IFN␥ are usually higher in RA ST than in OA ST (33). The fact that approximately one-third of vimentin-positive cells (probably synovial fibroblasts) had immunoreactive Gal-9 in the cytoplasm (Figure 2) is consistent with our finding that RA ST had 31.8% Gal-9-positive cells (Figure 3).…”

Section: Discussionmentioning

confidence: 75%

Beneficial effect of galectin 9 on rheumatoid arthritis by induction of apoptosis of synovial fibroblasts

Seki¹,

Sakata²,

Oomizu³

et al. 2007

Arthritis & Rheumatism

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103

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Objective. To compare the expression of galectin 9 (Gal-9) in synovial tissue (ST) from rheumatoid arthritis (RA) patients and osteoarthritis (OA) patients and to evaluate the effects of Gal-9 on fibroblast-like synoviocytes (FLS) in these patients.Methods. The expression of Gal-9 in ST and FLS was compared using immunohistochemical techniques. Apoptotic cells in RA and OA ST samples were detected by TUNEL assay. Apoptosis of FLS was analyzed by the sub-G 1 method in vitro. The in vivo suppressive effects of Gal-9 on collagen-induced arthritis (CIA) in a mouse model were also elucidated.Results. The percentage of Gal-9-positive cells in ST samples and the amount of Gal-9 in synovial fluid samples were significantly higher in patients with RA than in patients with OA, suggesting the involvement of Gal-9 in the development of RA. Compared with the 2 wild-type Gal-9 forms, stable Gal-9, a mutant protein resistant to proteolysis, significantly induced apoptosis of FLS from RA patients. In contrast, other galectins, such as Gal-1, Gal-3, and Gal-8, did not induce apoptosis or suppress the proliferation of human RA FLS. Stable Gal-9 preferentially induced apoptosis and suppressed the proliferation of RA FLS in vitro. It also induced apoptosis of cells in RA ST implanted into SCID mice in vivo. In a mouse model of CIA, apoptotic cells were detected in the joints of stable Gal-9-treated mice, but not phosphate buffered saline-treated mice, and suppressed CIA characterized by pannus formation with inflammatory cell infiltration and bone/cartilage destruction.Conclusion. Gal-9-induced apoptosis of hyperproliferative RA FLS may play a critical role in the suppression of RA.

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Section: Discussionmentioning

confidence: 75%

Beneficial effect of galectin 9 on rheumatoid arthritis by induction of apoptosis of synovial fibroblasts

Seki¹,

Sakata²,

Oomizu³

et al. 2007

Arthritis & Rheumatism

Self Cite

103

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“…In the case of galectin-9, our data suggest that galectin-9 acts as a L. major-specific tagging protein or an adhesion molecule so that macrophages can recognize L. major more efficiently. It has been known that some galectins, which can cross-link different cells expressing their oligosaccharide ligands (28,34,35), act as adhesion molecules even though galectins are soluble proteins (32,63,64). Galectin-9 contains two CRDs linked by a peptide linker and is thus intrinsically divalent (33,46,65).…”

Section: Discussionmentioning

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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“…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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Selective Eosinophil Adhesion to Fibroblast Via IFN-γ-Induced Galectin-9

Cited by 132 publications

References 42 publications

Beneficial effect of galectin 9 on rheumatoid arthritis by induction of apoptosis of synovial fibroblasts

Beneficial effect of galectin 9 on rheumatoid arthritis by induction of apoptosis of synovial fibroblasts

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

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

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