Galectin-3 Guides Intracellular Trafficking of Some Human Serotransferrin Glycoforms

Carlsson, Michael C.; Bengtson, Per; Cucak, Helena; Leffler, Hakon

doi:10.1074/jbc.m113.487793

Cited by 25 publications

(32 citation statements)

References 51 publications

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“…Carlsson and colleagues determined that Transferrin uptake and intracellular trafficking was mediated in part by Galectin 3 (140). While Clathrin-dependent endocytosis of transferrin was well established, this new Galectin 3 mediated mechanism was important to demonstrate that iron transport by this molecule was more complex than originally envisioned.…”

Section: Novel Function Of Galectin 3 In Regulation Of Glycoprotein Ementioning

confidence: 94%

“…Importantly, the glycan moiety on Transferrin (which does not affect iron binding) was found to (140). Indeed, endocytosis of another important cancer associated receptor (CD44) was found to be mediated by Galectin 3.…”

Section: Novel Function Of Galectin 3 In Regulation Of Glycoprotein Ementioning

confidence: 97%

“…The ability of Galectin 3 to form lattices with glycoproteins and glycolipids has been implicated in regulating cell adhesion, metastasis, endocytosis, and other biological processes (26,63,71,72,140,141). Carlsson and colleagues determined that Transferrin uptake and intracellular trafficking was mediated in part by Galectin 3 (140).…”

Section: Novel Function Of Galectin 3 In Regulation Of Glycoprotein Ementioning

confidence: 97%

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Galectin 3 as a guardian of the tumor microenvironment

Ruvolo

2016

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

175

165

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Galectin 3 is a member of a family of β-galactoside binding proteins and has emerged as an important regulator of diverse functions critical in cancer biology including apoptosis, metastasis, immune surveillance, molecular trafficking, mRNA splicing, gene expression, and inflammation. Galectin 3's ability to support cancer cell survival by intra-cellular and extra-cellular mechanisms suggests this molecule is an important component of the tumor microenvironment that potentially could be targeted for therapy. Data is emerging that Galectin 3 is elevated in many cancers including solid tumors and the cancers of the blood. Galectin 3 also appears to be a key molecule produced by tumor microenvironment support cells including mesenchymal stromal cells (MSC) to suppress immune surveillance by killing T cells and interfering with NK cell function and by supporting metastasis. Levels of Galectin 3 increase in the MSC of aging mice and perhaps this contributes to the development of cancer in the elderly. Galectin 3 modulates surface protein expression of a diverse set of glycoproteins including CD44 by regulating endocytosis of these proteins. In addition, Galectin 3 binding to receptor kinases such as CD45 and the T cell receptor is critical in the regulation of their function. In this review I will examine the various mechanisms how Galectin 3 supports chemoresistance and metastasis in solid tumors and in leukemia and lymphoma. I will also discuss possible therapeutic strategies to target this Galectin for cancer therapy. This article is part of a Special Issue entitled: Tumor Microenvironment Regulation of Cancer Cell Survival, Metastasis, Inflammation, and Immune Surveillance edited by Peter Ruvolo and Gregg L. Semenza.

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Section: Novel Function Of Galectin 3 In Regulation Of Glycoprotein Ementioning

confidence: 94%

Section: Novel Function Of Galectin 3 In Regulation Of Glycoprotein Ementioning

confidence: 97%

Section: Novel Function Of Galectin 3 In Regulation Of Glycoprotein Ementioning

confidence: 97%

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Galectin 3 as a guardian of the tumor microenvironment

Ruvolo

2016

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

175

165

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“…Among the galectin-3 binding partners LPH and p75 NTR contain both N-and O-glycans (Naim and Lentze, 1992;Yeaman et al, 1997), whereas gp114 is only N-glycosylated (Le Bivic et al, 1993). Both glycan-variants could be involved in galectin-3 mediated apical sorting since galectin-3 binds to ␤-galactosides of N- (Carlsson et al, 2013) and in principle also of O-glycans. Nevertheless, galectin-1 and -3 bind nearly exclusively to complex N-glycans on the surface of CHO cells (Patnaik et al, 2006).…”

Section: Participation Of Galectin-3 In Apical Traffickingmentioning

confidence: 99%

Recycling of galectin-3 in epithelial cells

Hönig

Schneider

Jacob

2015

European Journal of Cell Biology

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“…The fifth mechanism was that rs4644 and rs4652 regulate LGALS3, affecting immunoglobulin binding. This gene encodes a member of the galectin family of carbohydrate-binding proteins and plays roles in numerous cellular functions including apoptosis, innate immunity, cell adhesion, and t-cell regulation [33]. In the nucleus, LGALS3 acts as a pre-mRNA splicing factor, and is involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes and macrophages, opsonization of apoptotic neutrophils, and activation of mast cells [33].…”

Section: Discussionmentioning

confidence: 99%

Genome-wide pathway analysis in glioma

Lee¹,

Song²

2015

neo

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The aim of this study was to identify candidate single-nucleotide polymorphisms (SNPs) that may play a role in the susceptibility to glioma, to elucidate their potential mechanisms, and to generate SNP-to-gene-to-pathway hypotheses.A genome-wide association study (GWAS) dataset of glioma including 509,345 SNPs from 1,856 glioma patients and 4,955 control subjects of European descent was used in this study. Identify candidate Causal SNPs and Pathways (ICSNPathway) analysis was applied to the GWAS dataset.ICSNPathway analysis identified 6 candidate SNPs, 5 genes, and 9 pathways, which revealed 5 hypothetical biological mechanisms. The hypothetical mechanisms, beginning with the strongest, are summarized as follows: (i) rs667128 alters the role of taste receptor, type 2, member 8 (TAS2R8) in taste receptor activity and taste transduction pathways (p < 0.001, false discovery rate (FDR) < 0.001; p = 0.001, FDR = 0.012, respectively), (ii) rs619381 modulates the effect of taste receptor, type 2, member 7 (TAS2R7) on taste receptor activity and taste transduction (p < 0.001, FDR Using the ICSNPathway to analyze glioma GWAS data, 6 candidate SNPs, 5 genes (TAS2R8, TAS2R7, DLL1, LBP, and LGALS3), and 9 pathways that may contribute to the susceptibility of glioma were identified.

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Galectin-3 Guides Intracellular Trafficking of Some Human Serotransferrin Glycoforms

Cited by 25 publications

References 51 publications

Galectin 3 as a guardian of the tumor microenvironment

Galectin 3 as a guardian of the tumor microenvironment

Recycling of galectin-3 in epithelial cells

Genome-wide pathway analysis in glioma

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