Potential roles of galectins in myeloid differentiation into three different lineages

Abedin, Mohammad J.; Kashio, Yumiko; Seki, Masako; Nakamura, Kazuhiro; Hirashima, Mitsuomi

doi:10.1189/jlb.0402163

Cited by 52 publications

(49 citation statements)

References 43 publications

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“…Gal are also implicated in myeloid differentiation (17). We have thus shown that Gal-9 expression gradually decreases, whereas Gal-10 expression increases during eosinophil differentiation and that Gal-9 expression decreases, whereas Gal-3 expression increases during monocyte differentiation.…”

Section: G Alectins (Gal)mentioning

confidence: 78%

Galectin-9 Induces Maturation of Human Monocyte-Derived Dendritic Cells

Dai

Nakagawa

Itoh³

et al. 2005

The Journal of Immunology

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Maturation of dendritic cells (DCs) is critical for initiation of immune responses and is regulated by various stimulatory signals. We assessed the role of galectin (Gal)-9 in DC maturation. Culture of immature DCs with exogenous Gal-9 markedly increased the surface expression of CD40, CD54, CD80, CD83, CD86, and HLA-DR in a dose-dependent manner, although Gal-9 had no or little effect on differentiation of human monocytes into immature DCs. Gal-9-treated DCs secreted IL-12 but not IL-10, and they elicited the production of Th1 cytokines (IFN-γ and IL-2) but not that of the Th2 cytokines (IL-4 and IL-5) by allogeneic CD4+ T cells. These effects of Gal-9 on immature DCs were not essentially dependent on its lectin properties, given that they were inhibited only slightly by lactose. We further found that a Gal-9 mutant that lacks β-galactoside binding activity reproduced the above activities and that an anti-Gal-9 mAb suppressed them. Gal-9 induced phosphorylation of the MAPK p38 and ERK1/2 in DCs, and an inhibitor of p38 signaling, but not inhibitors of signaling by either ERK1/2 or PI3K, blocked Gal-9-induced up-regulation of costimulatory molecule expression and IL-12 production. These findings suggest that Gal-9 plays a role not only in innate immunity but also in acquired immunity by inducing DC maturation and promoting Th1 immune responses.

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Section: G Alectins (Gal)mentioning

confidence: 78%

Galectin-9 Induces Maturation of Human Monocyte-Derived Dendritic Cells

Dai

Nakagawa

Itoh³

et al. 2005

The Journal of Immunology

Self Cite

189

126

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“…The cells' reactivity was particularly strong toward members of the proto-type subfamily at the late stages of the cell death program. Despite sharing sequence homology, their expression and activity patterns, for example, in vitro and in vivo or with respect to caspase activation in human T cell apoptosis, differ so that they should not be considered to exert fully overlapping functions (46)(47)(48)(49). Having herewith identified human galectins as sensors for apoptosis/necrosis-associated cell surface changes, the next step will be to define a functional significance of this interplay.…”

Section: Discussionmentioning

confidence: 99%

Human galectins as sensors for apoptosis/necrosis‐associated surface changes of granulocytes and lymphocytes

et al. 2008

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Changes in the glycomic profile can significantly affect the cells' communication with the environment. Plant lectins have so far been used to address the issue as to whether the courses of apoptosis or necrosis are associated with such alterations. We, here, initiate the study of members of the family of functionally pleiotropic human galectins in this respect. Established protocols for the induction of apoptosis/necrosis of blood cells and for flow cytometry using annexin V/propidium iodide were combined with cell surface staining using biotinylated galectins at a nontoxic concentration. The galectin panel covered members from all three subfamilies. Flow cytometry revealed specific binding of galectins to viable control cells and conspicuous staining differences when testing apoptotic or necrotic cells. Onset and especially progression of cell death led to pronounced reactivity with the proto-type galectins-1, -2, and -7 and tandem-repeattype galectin-4. Extent of staining depended on the nature and stage of cell death, type of dying cell, and type of galectin. Galectins act as sensors for cell-death-associated surface changes. Staining of late-apoptotic polymorphonuclear cells was particularly strong. Examining the functional significance of this result may reveal a new aspect within the surveillance system to protect against autoinflammation. ' 2008 International Society for Analytical Cytology Key terms apoptosis; flow cytometry; galectin; glycosylation; lectin; necrosis; phagocytosis; sialylation THE safe disposal of apoptotic and necrotic cell material will limit the hazard to develop autoimmunity (1). In its initial phase, endogenous safeguard systems trace biochemical deviations on the cell surface, which signal the onset of cell death. Consecutive steps toward late stages are accompanied by further surface alterations. They are supposed to mark dying cells for elimination but their biochemical nature is not yet fully characterized. To explain efficient clearance, probing into distinct surface characteristics is a means to delineate operative routes of dying-self recognition. That said that the analysis of cell surface glycans is an obvious choice, because the glycomic profile is known to undergo disease-associated changes and to present a large panel of sugar-encoded signals to the environment (2-4). Using plant lectins as marker for glycan determinants (5), the hypothesis that their profile and/or mode of presentation are altered by cell death was already tested, and changes of lectin binding to dying and dead leukemic cells had been reported (6-9). These results obtained with plant proteins support the concept that glycan recognition by endogenous receptors can figure as a way to identify and clear nonviable cells. Focusing on spatially accessible branch-end determinants of glycan antennae, case studies with hepatic, and macrophage C-type asialoglycoprotein receptors already illustrated their

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“…10 Galectin-3 is a differentiation marker for human monocytes or promyelocytic cell line HL-60, which can be differentiated into macrophage-like cells by phorbol ester treatment. 11 Galectin-3 is considered as macrophage activation marker as it is overexpressed in phagocytic macrophages. 12 Galectin-3 level is also increased in myelin-activated microglia and macrophages.…”

Section: Introductionmentioning

confidence: 99%

Galectin-3 and Inflammation

Wan

Liu

2016

Glycobiology Insights

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ABSTRACT:Galectins are a family of β-galactoside-binding proteins that share a consensus sequence in the carbohydrate recognition domain (CRD). Galectin-3 is the most widely studied family member and can be found in the cellular cytoplasm and nucleus, as well as extracellularly in various tissues. The 30-kDa molecule contains an N-terminal proline-rich domain that is important for its oligomerization and a C-terminal CRD for carbohydrate-binding activity. Many studies have shown that galectin-3 may regulate inflammation through a variety of mechanisms. Endogenous galectin-3 has been shown to be involved in the pathogenesis of various diseases, such as fibrosis in the lung, liver, and heart, diabetes mellitus, coronary artery disease, and allergic diseases. In this review, we briefly discuss the pro-or anti-inflammatory roles, as well as potential clinical implications of galectin-3 in these disorders.

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Potential roles of galectins in myeloid differentiation into three different lineages

Cited by 52 publications

References 43 publications

Galectin-9 Induces Maturation of Human Monocyte-Derived Dendritic Cells

Galectin-9 Induces Maturation of Human Monocyte-Derived Dendritic Cells

Human galectins as sensors for apoptosis/necrosis‐associated surface changes of granulocytes and lymphocytes

Galectin-3 and Inflammation

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