Oligosaccharide specificity of galectins: a search by frontal affinity chromatography.

A soluble lactose-binding lectin with subunit Mr of 14,500 is believed to function by interacting with extracellular glycoconjugates, because it has been detected extracellularly by immunohistochemistry. This localization has been questioned, however, since the lectin lacks a secretion signal sequence, which challenges the contention that it is secreted. We have demonstrated externalization of this lectin from C2 mouse muscle cells by both immunoprecipitation of metabolically labeled protein and immunohistochemical localization. We further show that externalization of the lectin is a developmentally regulated process that accompanies myoblast differentiation and that the lectin codistributes with laminin in myotube extracellular matrix. Immunohistochemical localization during intermediate stages of externalization suggests that the lectin becomes concentrated in evaginations of plasma membrane, which pinch off to form labile lectin-rich extracellular vesicles. This suggests a possible mechanism for lectin export from the cytosol to the extracellular matrix.

/pdf/evidence-for-export-of-a-muscle-lectin-from-cytosol-to-1sescb6cvw.pdf

Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism.

Identification and Characterization of Galectin-9, a Novel β-Galactoside-binding Mammalian Lectin

Galectin-9, a beta-galactoside binding lectin, has recently been isolated from murine embryonic kidney In this study, its biological functions and expression in embryonic, newborn, and adult mice tissues were investigated By Northern blot analyses, it was found widely distributed and its expression was developmentally regulated In situ hybridization studies revealed an accentuated expression of galectin-9 in liver and thymus of embryonic mice In postnatal mice, antigalectin-9 immunoreactivity was observed in various tissues, including thymic epithelial cells The high expression of galectin-9 in the thymus led us to investigate its role in the clonal deletion of thymocytes Fusion proteins were generated, which retained lactose-binding activity like the endogenous galectin-9 Galectin-9, at 25 microM concentration, induced apoptosis in approximately 30% of the thymocytes, as assessed by terminal deoxytransferase-mediated dUTP nick end labeling method The apoptotic effect was dose dependent and lactose inhibitable At higher concentrations, it induced homotypic aggregation of the thymocytes Electron microscopy revealed approximately 60% of the thymocytes undergoing apoptosis in the presence of galectin-9 By immunofluorescence microscopy, some of the thymocytes undergoing apoptosis had plasmalemmal bound galectin-9 Galectin-9 failed to induce apoptosis in hepatocytes Taken together, these findings indicate that galectin-9, a developmentally regulated lectin, plays a role in thymocyte-epithelial interactions relevant to the biology of the thymus

/pdf/developmental-regulation-expression-and-apoptotic-potential-4i20dclz12.pdf

Developmental regulation, expression, and apoptotic potential of galectin-9, a beta-galactoside binding lectin.

Identification of an autocrine negative growth factor: Mouse β-galactoside-binding protein is a cytostatic factor and cell growth regulator

Molecular cloning, characterization, and expression of a human 14-kDa lectin.

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Molecular cloning, characterization, and expression of a human 14-kDa lectin.