Immunoelectron microscopic localization of galectin‐3, an IgE binding protein, in human mast cells and basophils

Craig, Shirley S.; Krishnaswamy, Priya; Irani, Anne-Marie; Kepley, Christopher L.; Liu, Fu‐Tong; Schwartz, Lawrence B.

doi:10.1002/ar.1092420210

Cited by 44 publications

(33 citation statements)

References 47 publications

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“…Galectin-1, expressed in abundance in muscle, can induce T-cells to undergo apoptosis (60). Galectin-3 has been localized in macrophages, basophils (61), eosinophils (62), and mast cells (61). Immunoelectron microscopic studies have indicated that much of the galectin-3 found in a mast cell is granule-associated.…”

Section: Bioactivity Of Recombinant Ecalectin In Vitro and In Vivo-mentioning

confidence: 99%

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

Matsumoto¹,

Matsumoto²,

Seki³

et al. 1998

Journal of Biological Chemistry

281

230

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A 1.6-kilobase pair cDNA was isolated from a human T-cell-derived expression library that encodes a novel eosinophil chemoattractant (designated ecalectin) expressed during allergic and parasitic responses. Based on its deduced amino acid sequence, ecalectin is a 36-kDa protein consisting of 323 amino acids. Although ecalectin lacks a hydrophobic signal peptide, it is secreted from mammalian cells. Ecalectin is not related to any known cytokine or chemokine but rather is a variant of human galectin-9, a member of the large family of animal lectins that have affinity for ␤-galactosides. Recombinant ecalectin, expressed in COS cells and insect cells, exhibited potent eosinophil chemoattractant activity and attracted eosinophils in vitro and in vivo in a dose-dependent manner but not neutrophils, lymphocytes, or monocytes. The finding that the ecalectin transcript is present in abundance in various lymphatic tissues and that its expression increases substantially in antigen-activated peripheral blood mononuclear cells suggests that ecalectin is an important T-cell-derived regulator of eosinophil recruitment in tissues during inflammatory reactions. We believe that this is the first report of the expression of an immunoregulatory galectin expressed by a T-cell line that is selective for eosinophils.

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Section: Bioactivity Of Recombinant Ecalectin In Vitro and In Vivo-mentioning

confidence: 99%

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

Matsumoto¹,

Matsumoto²,

Seki³

et al. 1998

Journal of Biological Chemistry

281

230

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“…Furthermore, expression of Gal-1 in endothelial cells can be modulated by several inflammatory agents, supporting its role in inflammatory incidences (Baum et al 1995b). Gal-3 is expressed by virtually all immune cell types, including endothelial cells, lymphocytes (Lotan et al 1994, Baum et al 1995b, neutrophils (Truong et al 1993), monocytes and macrophages , mast cells (Craig et al 1995) and dendritic cells (Flotte et al 1983). Gal-3 expression has been found to be increased in neutrophils upon adhesion to the endothelium (Gil et al 2006b), which also coincided with a relocalisation of Gal-3 to the plasma membrane in endothelial cells (Gil et al 2006b).…”

mentioning

confidence: 99%

Endogenous galectins and the control of the host inflammatory response

Norling¹,

Perretti²,

Cooper³

2009

Journal of Endocrinology

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A new era of research is being devoted to deciphering endogenous mediators and mechanisms that are in place to resolve the inflammatory response. Accruing evidence indicates that galectins fall into this category of immunoregulatory mediators signifying their use as prospective novel anti-inflammatory agents. The focus of this review is to depict the immunoregulatory bioactivities of three members of the galectin superfamily, Galectin (Gal)-1, Gal-3 and Gal-9.Emphasis is given to the studies investigating the properties of these endogenous lectins. Gal-1, Gal-3 and Gal-9 are emerging as pertinent players in the modulation of acute and chronic inflammatory diseases, autoimmunity and cancer, and thus being increasingly recognised as molecular targets for innovative drug discovery.

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“…Galectin-3 is a member of the galectin family, which comprises soluble mammalian lectins with conserved peptide sequence elements of carbohydrate recognition domain (30 -32). Galectin-3 is found in most cells involved in the immune response, including macrophages, mast cells, and paranchyma cells (endothelial/epithelial cells) and can be released in the extracellular environment by inflammatory cells, such as macrophages, or by damaged cells (33)(34)(35)(36)(37)(38)(39)(40)(41).…”

mentioning

confidence: 99%

Role of Galectin-3 in Leukocyte Recruitment in a Murine Model of Lung Infection by Streptococcus pneumoniae

Nieminen

St-Pierre

Bhaumik

et al. 2008

The Journal of Immunology

105

119

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Pneumonia can be caused by a variety of pathogens, among which Streptococcus pneumoniae causes one of the most common forms of community-acquired pneumonia. Depending on the invading pathogen, the elements of the immune response triggered will vary. For most pathogens, such as Escherichia coli, neutrophil recruitment involves a well-described family of adhesion molecules, β2-integrins. In the case of streptococcal pneumonia, however, neutrophil recruitment occurs mainly through a β2-integrin-independent pathway. Despite decades of research on this issue, the adhesion molecules involved in neutrophil recruitment during lung infection by S. pneumoniae have not been identified. We have previously shown that galectin-3, a soluble mammalian lectin, can be found in lungs infected by S. pneumoniae, but not by E. coli, and can mediate the adhesion of neutrophils on the endothelial cell layer, implying its role in the recruitment of neutrophils to lungs infected with S. pneumoniae. In this study, using galectin-3 null mice, we report further evidence of the involvement of this soluble lectin in the recruitment of neutrophils to S. pneumonia-infected lungs. Indeed, in the absence of galectin-3, lower numbers of leukocytes, mainly neutrophils, were recruited to the infected lungs during infection by S. pneumoniae. In the case of β2-integrin-dependent recruitment induced by lung infection with E. coli, the number of recruited neutrophils was not reduced. Thus, taken together, our data suggest that galectin-3 plays a role as a soluble adhesion molecule in the recruitment of neutrophils to lungs infected by S. pneumoniae, which induces β2-integrin-independent migration.

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Immunoelectron microscopic localization of galectin‐3, an IgE binding protein, in human mast cells and basophils

Cited by 44 publications

References 47 publications

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

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

Endogenous galectins and the control of the host inflammatory response

Role of Galectin-3 in Leukocyte Recruitment in a Murine Model of Lung Infection by Streptococcus pneumoniae

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