Loss of galectin-3 impairs membrane polarisation of mouse enterocytes in vivo

Delacour, Delphine; Koch, Annett; Ackermann, Waltraud; Parco, Isabelle Eude-Le; Elsässer, Hans–Peter; Poirier, Françoise; Jacob, Ralf

doi:10.1242/jcs.020800

Cited by 68 publications

(53 citation statements)

References 38 publications

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“…Galectin-3 is required for intracellular sorting and correct targeting of glycoproteins to the apical plasma membrane (Delacour et al 2006). In accordance with this, an analysis of galectin-3 knockout mice showed that actin and villin abundant in the brush border become abnormally distributed along baso-lateral membranes (Delacour et al 2008). Interaction of galectins, including galectin-3, with actin (Chiu et al 1992;Joubert et al 1992), cytokeratins (Goletz et al 1997), and possibly tubulin (Ozaki et al 2004) has been indicated.…”

Section: Discussionmentioning

confidence: 87%

Immunohistochemical Localization of Six Galectin Subtypes in the Mouse Digestive Tract

Nio‐Kobayashi

Takahashi-Iwanaga

Iwanaga

2008

J Histochem Cytochem.

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S U M M A R Y Galectin, an animal lectin that recognizes b-galactoside of glycoconjugates, is abundant in the gut. This IHC study showed the subtype-specific localization of galectin in the mouse digestive tract. Mucosal epithelium showed region/cell-specific localization of each galectin subtype. Gastric mucous cells exhibited intense immunoreactions for galectin-2 and galectin-4/6 with a limited localization of galectin-3 at the surface of the gastric mucosa. Electron microscopically, galectin-3 immunoreactivity coated indigenous bacteria on the gastric surface mucous cells. Epithelial cells in the small intestine showed characteristic localizations of galectin-2 and galectin-4/6 in the cytoplasm of goblet cells and the baso-lateral membrane of enterocytes in association with maturation, respectively. Galectin-3 expressed only at the villus tips was concentrated at the myosin-rich terminal web of fully matured enterocytes. Epithelial cells of the large intestine contained intense immunoreactions for galectin-3 and galectin-4/6 but not for galectin-2. The stratified squamous epithelium of the forestomach was immunoreactive for galectin-3 and galectin-7, but the basal layer lacked galectin-3 immunoreactivity. Outside the epithelium, only galectin-1 was localized in the connective tissue, smooth muscles, and neuronal cell bodies. The subtype-specific localization of galectin suggests its important roles in host-pathogen interaction and epithelial homeostasis such as membrane polarization and trafficking in the gut. GALECTIN is a b-galactoside-binding lectin, which to date consists of 15 members (galectin-1 to galectin-15) in mammals and is broadly distributed in a variety of cells and tissues (Leffler et al. 2004). Galectin is likely secreted extracellularly through a non-classical unknown pathway because it lacks a signal sequence essential for insertion into the endoplasmic reticulum (Hughes 1999). Extracellular galectin may mediate cell-cell or cell-matrix adhesion by recognizing cell surface glycoproteins and glycolipids or glycosylated extracellular matrix (Hughes 2001). It also seems capable of regulating cell signaling and membrane trafficking by cross-linking the cell surface receptors (Rabinovich et al. 2007a). A special type of galectin (galectin-3) is involved in host-pathogen interaction through the recognition of a surface carbohydrate of microorganisms (Sato and Nieminen 2004). In contrast, the predominant localization of galectin in the cytoplasm has been frequently observed, suggesting an additional possibility that galectin operates intracellularly to cell proliferation, differentiation, and apoptosis (Hsu and Liu 2004).In the mouse, nine subtypes of galectin (galectin-1, -2, -3, -4, -6, -7, -8, -9, and -12) have been reported to be expressed in a tissue/cell-specific manner. The digestive tract is one of the organs rich in galectin; we previously showed at the mRNA level that at least six subtypes of galectin (galectin-2, -3, -4, -6, -7, and -9) were intensely and continuously expressed from t...

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Section: Discussionmentioning

confidence: 87%

Immunohistochemical Localization of Six Galectin Subtypes in the Mouse Digestive Tract

Nio‐Kobayashi

Takahashi-Iwanaga

Iwanaga

2008

J Histochem Cytochem.

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“…Similarly, in the absence of the basolateral sorting adaptor AP-1B, Gal4 promotes transcytosis and apical sorting of the transferrin receptor through apical recycling endosomes (Perez Bay et al, 2014). Gal3, Gal4, Gal7 and Gal9 have all been shown to be determinants of apical sorting, and are required for epithelial morphogenesis and polarity, the development of the apical lumen and ciliogenesis (Delacour et al, 2006(Delacour et al, , 2008Mishra et al, 2010;Mo et al, 2012;Rondanino et al, 2011;Stechly et al, 2009;Torkko et al, 2008). Gal3 trafficking, therefore, involves non-classical secretion from the cytoplasm and glycan-dependent raft endocytosis to recycling endosomes, where it and other galectins play roles in post-Golgi sorting (see poster).…”

Section: Galectin Traffickingmentioning

confidence: 99%

The galectin lattice at a glance

Nabi

Shankar

Dennis

2015

Journal of Cell Science

272

230

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Galectins are a family of widely expressed β-galactoside-binding lectins in metazoans. The 15 mammalian galectins have either one or two conserved carbohydrate recognition domains (CRDs), with galectin-3 being able to pentamerize; they form complexes that crosslink glycosylated ligands to form a dynamic lattice. The galectin lattice regulates the diffusion, compartmentalization and endocytosis of plasma membrane glycoproteins and glycolipids. The galectin lattice also regulates the selection, activation and arrest of T cells, receptor kinase signaling and the functionality of membrane receptors, including the glucagon receptor, glucose and amino acid transporters, cadherins and integrins. The affinity of transmembrane glycoproteins to the galectin lattice is proportional to the number and branching of their N-glycans; with branching being mediated by Golgi N-acetylglucosaminyltransferasebranching enzymes and the supply of UDP-GlcNAc through metabolite flux through the hexosamine biosynthesis pathway. The relative affinities of glycoproteins for the galectin lattice depend on the activities of the Golgi enzymes that generate the epitopes of their ligands and, thus, provide a means to analyze biological function of lectins and of the 'glycome' more broadly.

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“…Galectins are cytosolic proteins that are released from cells via a nonclassical secretion mechanism that then bind to cell-surface proteins and can be internalized into endosomal compartments (Hughes, 2004). Knockdown or knockout of the apically secreted galectin-3 inhibits the delivery of the raftindependent protein p75 (Delacour et al, 2006;Delacour et al, 2008;Lindstedt et al, 1993), whereas knockdown of galectin-4 in intestinal cells inhibits lipid-raft association of raft-associated proteins [the GPI-APs carcinoembryonic antigen (CEA) and CD59, and the transmembrane protein dipeptidyl peptidase IV (DPPIV)] and prevents their apical delivery (Delacour et al, 2005;Stechly et al, 2009). Interestingly, the apical addition of galectin-4 to intestinal cells depleted of this protein reconstituted apical delivery of DPPIV, which otherwise was accumulated in a postGolgi endosomal compartment .…”

Section: Carbohydrates As Apical Sorting Determinantsmentioning

confidence: 99%

“…Clustering is also required for correct apical sorting of raftindependent apical proteins, a process that might involve galectin-3 (Delacour et al, 2006;Delacour et al, 2007;Delacour et al, 2008). Whereas galectin-4 is believed to meet apical proteins in a post- Golgi endosomal compartment , the exact site where galectin-3 meets apical cargo has not been established.…”

Section: Clustering and Apical Traffickingmentioning

confidence: 99%

Apical trafficking in epithelial cells: signals, clusters and motors

Weisz

Rodríguez-Boulan

2009

Journal of Cell Science

284

281

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In the early days of epithelial cell biology, researchers working with kidney and/or intestinal epithelial cell lines and with hepatocytes described the biosynthetic and recycling routes followed by apical and basolateral plasma membrane (PM) proteins. They identified the trans-Golgi network and recycling endosomes as the compartments that carried out apical-basolateral sorting. They described complex apical sorting signals that promoted association with lipid rafts, and simpler basolateral sorting signals resembling clathrin-coated-pit endocytic motifs. They also noticed that different epithelial cell types routed their apical PM proteins very differently, using either a vectorial (direct) route or a transcytotic (indirect) route. Although these original observations have generally held up, recent studies have revealed interesting complexities in the routes taken by apically destined proteins and have extended our understanding of the machinery required to sustain these elaborate sorting pathways. Here, we critically review the current status of apical trafficking mechanisms and discuss a model in which clustering is required to recruit apical trafficking machineries. Uncovering the mechanisms responsible for polarized trafficking and their epithelial-specific variations will help understand how epithelial functional diversity is generated and the pathogenesis of many human diseases.

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Loss of galectin-3 impairs membrane polarisation of mouse enterocytes in vivo

Cited by 68 publications

References 38 publications

Immunohistochemical Localization of Six Galectin Subtypes in the Mouse Digestive Tract

Immunohistochemical Localization of Six Galectin Subtypes in the Mouse Digestive Tract

The galectin lattice at a glance

Apical trafficking in epithelial cells: signals, clusters and motors

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