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Interferon-γ stimulates the expression of galectin-9 in cultured human endothelial cells

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TLDR
IFN‐γ‐induced production of galectin‐9 by endothelial cells may play an important role in immune responses by regulating interactions between the vascular wall and eosinophils.
Abstract
Galectin-9 is a member of the galectin family and has been identified as an eosinophil chemoattractant produced by activated T lymphocytes. Vascular endothelial cells play an important role in the initial step of eosinophil recruitment and activation in immune and inflammatory responses. We have addressed the stimulation of galectin-9 expression in endothelial cells. Galectin-9 was detected in membrane and cytosolic fractions of human umbilical vein endothelial cells stimulated with interferon-gamma (IFN-gamma). IFN-gamma also enhanced the adhesion of human eosinophilic leukemia-1 cells to endothelial monolayers, and it was inhibited by the presence of lactose. Interleukin-4, which induces eotaxin expression, did not affect the expression of galectin-9. The in situ endothelium from patients with inflammatory diseases was found to express galectin-9. IFN-gamma-induced production of galectin-9 by endothelial cells may play an important role in immune responses by regulating interactions between the vascular wall and eosinophils.

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Citations
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Journal ArticleDOI

The Tim-3 ligand galectin-9 negatively regulates T helper type 1 immunity

TL;DR: The data suggest that the Tim-3–galectin-9 pathway may have evolved to ensure effective termination of effector TH1 cells.
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Promotion of tissue inflammation by the immune receptor Tim-3 expressed on innate immune cells.

TL;DR: It is found that Tim-3 is constitutively expressed on cells of the innate immune system in both mice and humans, and that it can synergize with Toll-like receptors and can either promote or terminate TH1 immunity.
Journal ArticleDOI

Galectins in innate immunity: dual functions of host soluble β‐galactoside‐binding lectins as damage‐associated molecular patterns (DAMPs) and as receptors for pathogen‐associated molecular patterns (PAMPs)

TL;DR: The glycocalyx is a glycan layer found on the surfaces of host cells as well as microorganisms and enveloped virus, which contains various structurally different glycans, which provide cell‐ or microorganism‐specific ‘glycoinformation’ and is decoded by host glycan‐binding proteins, lectins.
References
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Journal ArticleDOI

How cells respond to interferons

TL;DR: The Janus kinases and signal transducers and activators of transcription, and many of the interferon-induced proteins, play important alternative roles in cells, raising interesting questions as to how the responses to the interFERons intersect with more general aspects of cellular physiology and how the specificity of cytokine responses is maintained.
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Endothelial cell interactions with granulocytes: tethering and signaling molecules

TL;DR: The adhesion of granulocytes to endothelial cells requires regulated expression of molecules on both the endothelial cell and the granulocyte, which act either to tether the two cells together or as signals that induce activation-dependent adhesion events.
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Human eotaxin is a specific chemoattractant for eosinophil cells and provides a new mechanism to explain tissue eosinophilia.

TL;DR: It is demonstrated that human eotaxin is an early response gene of cytokine–stimulated epithelial and endothelial cells, and is induced in peripheral blood eosinophils by interleukin–3, and an eOTaxin antagonist may be a novel therapy for certain human diseases characterized by tissue eOSinophilia.
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Biochemical characterization of a gamma interferon-inducible cytokine (IP-10).

TL;DR: Using polyclonal monospecific antisera to recombinant protein and synthetic peptides, it is demonstrated that the IP-10 protein is associated, in vivo, with a delayed-type hypersensitivity response.
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The family of metazoan metal-independent β-galactoside-binding lectins: structure, function and molecular evolution

TL;DR: It appears that beta-galactoside-binding lectins and some non-lectin proteins form a superfamily whose members are widely distributed from vertebrates to invertebrates and a consideration of molecular evolution suggests that lectins belonging to this family probably existed in the Precambrian era.
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