Glycosylation pattern of brush border-associated glycoproteins in enterocyte-like cells: involvement of complex-type <i>N</i>-glycans in apical trafficking

Morelle, Willy; Stechly, Laurence; André, Sabine; Seuningen, Isabelle Van; Porchet, Nicole; Gabius, Hans‐Joachim; Huet, Guillemette

doi:10.1515/bc.2009.075

Cited by 41 publications

(27 citation statements)

References 56 publications

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“…Of note, galectin-based sorting of distinct glycoproteins with complex-type N-glycans such as dipeptidyl peptidase IV, carcinoembryonic antigen, or mucin-like membrane MUC1 through the endocytic/recycling pathway has been recently described for galectin-4 in the apical biosynthetic pathway in enterocyte-like cells. 51,52 It is therefore tempting to speculate that galectin-5 in rat or EDA in rabbit might facilitate down-regulation of the expression of specific target glycoconjugates during erythropoiesis. This would be in agreement with the progressive decrease in galactosidecontaining components from the cell surface of rabbit erythroid cells during differentiation of erythroblasts into mature erythrocytes.…”

Section: Discussionmentioning

confidence: 99%

Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages

Barrès

Blanc

Bette‐Bobillo

et al. 2010

Blood

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Reticulocytes release small membrane vesicles termed exosomes during their maturation into erythrocytes. Exosomes are intraluminal vesicles of multivesicular endosomes released into the extracellular medium by fusion of these endosomal compartments with the plasma membrane. This secretion pathway contributes to reticulocyte plasma membrane remodeling by eliminating certain membrane glycoproteins. We show in this study that galectin-5, although mainly cytosolic, is also present on the cell surface of rat reticulocytes and erythrocytes. In addition, in reticulocytes, it resides in the endosomal compartment. We document galectin-5 translocation from the cytosol into the endosome lumen, leading to its secretion in association with exosomes. Galectin-5 bound onto the vesicle surface may function in sorting galactosebearing glycoconjugates. Fittingly, we found that Lamp2, a major cellular glycoprotein presenting galectin-reactive poly-N-acetylactosamine chains, is lost during reticulocyte maturation. It is associated with released exosomes, suggestive of binding to galectin-5. Finally, we reveal that the uptake of rat reticulocyte exosomes by macrophages is dependent on temperature and the mechanoenzyme dynamin and that exosome uptake is decreased by adding galectin-5. These data imply galectin-5 functionality in the exosomal sorting pathway during rat reticulocyte maturation. (Blood. 2010;115: 696-705) IntroductionExosomes are membrane vesicles secreted by various cells and represent intraluminal vesicles of multivesicular endosomes (MVEs) released into the extracellular medium upon fusion of MVE with the plasma membrane. 1 Exosomal release during reticulocyte maturation is part of a cellular program resulting in remodeling of the plasma membrane by removal of a distinct set of (glyco)proteins. 2 We have previously shown that exosomal segregation of internalized membrane (glyco)proteins can occur by different routes, such as a natural enrichment in membrane domains (eg, lipid rafts), 3 antibody-or lectin-induced clustering on the cell surface, 4 or via the endosomal sorting complex required for transport (ie, ESCRT) cytosolic machinery. 5 During an earlier stage of mammalian erythroid differentiation, ie, when the erythroblast expels its nucleus, some components of the erythroblast plasma membrane are already specifically sorted to either the nascent reticulocyte or the expelled nucleus. For example, it has been shown by the use of mouse erythroblasts that proteins such as erythroblast-macrophage protein and ␤1-integrin partitioned predominantly to the plasma membrane surrounding the expelled nucleus, whereas glycophorin A localized to the plasma membrane of the nascent reticulocyte. 6 Both erythroblastmacrophage protein and ␤1-integrin have been identified as adhesion molecules involved in erythroblast retention by central macrophages within erythroblastic islands. [7][8][9] Thus, it has been suggested that their segregation to expelled nuclei favors their engulfment by macrophages while enabling reticulocytes to de...

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Section: Discussionmentioning

confidence: 99%

Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages

Barrès

Blanc

Bette‐Bobillo

et al. 2010

Blood

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250

211

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“…The presented biodistribution data, also covering isomers of triantennary N-glycans, provide a guideline for rational glycoengineering of glycosylated pharmaproteins. Owing to the potency of tissue lectins as elicitors of signaling in concert with particular glycoprotein targets, such as the a 5 b 1 -integrin or CD7 or as glycoprotein-specific transport vehicles (Rappl et al, 2002;Villalobo et al, 2006;André et al, 2007b;Morelle et al, 2009), even a low overall frequency of physiological substitution hitting these functionally important sites will be effective. Structural changes mapped by glycophenotyping, e.g., by glycoproteomics as a current approach in the quest to define new cancer biomarkers, can thus hereby reach a functional meaning.…”

Section: Discussionmentioning

confidence: 99%

From structural to functional glycomics: core substitutions as molecular switches for shape and lectin affinity of N-glycans

André

Kožár²,

Kojima³

et al. 2009

BCHM

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Glycan epitopes of cellular glycoconjugates act as versatile biochemical signals (sugar coding). Here, we test the hypothesis that the common N-glycan modifications by core fucosylation and introduction of the bisecting Nacetylglucosamine moiety have long-range effects with functional consequences. Molecular dynamics simulations indicate a shift in conformational equilibria between linear extension or backfolding of the glycan antennae upon substitution. We also present a new fingerprint-like mode of presentation for this multi-parameter system. In order to delineate definite structure-function relationships, we strategically combined chemoenzymatic synthesis with bioassaying cell binding and the distribution of radioiodinated neoglycoproteins in vivo. Of clinical relevance, tailoring the core region affects serum clearance markedly, e.g., prolonging circulation time for the neoglycoprotein presenting the N-glycan with both substitutions. a2,3-Sialylation is another means toward this end, similarly seen for type II branching in triantennary N-glycans. This discovery signifies that rational glycoengineering along the given lines is an attractive perspective to optimize pharmacokinetic behavior of glycosylated pharmaproteins. Of general importance for the concept of the sugar code, the presented results teach the fundamental lesson that N-glycan core substitutions convey distinct characteristics to the concerned oligosaccharide relevant for cis and trans biorecognition processes. These modifications are thus molecular switches.

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“…Because annexin A2 is strongly localized to the terminal web region of the brush border where endocytosis and exocytosis occur (54), it is a likely candidate for regulating vesicle trafficking to and from the brush border. Galectins have also been shown to play important roles in the apical trafficking of membrane proteins (20); indeed, knockdown of just one galectin, galectin-4, in HT-29 cells resulted in a dramatic reduction in the delivery of all glycosylated proteins to the apical surface (63). The importance of annexins and galectins in apical transport is underscored by findings suggesting that changes in their expression levels are contributing factors to a number of gastrointestinal diseases ranging from inflammation to cancer (21,81).…”

Section: Peripheral Membrane Bindingmentioning

confidence: 99%

Proteomic analysis of the enterocyte brush border

McConnell

Benesh²,

Mao³

et al. 2011

American Journal of Physiology-Gastrointestinal and Liver Physi

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The brush border domain at the apex of intestinal epithelial cells is the primary site of nutrient absorption in the intestinal tract and the primary surface of interaction with microbes that reside in the lumen. Because the brush border is positioned at such a critical physiological interface, we set out to create a comprehensive list of the proteins that reside in this domain using shotgun mass spectrometry. The resulting proteome contains 646 proteins with diverse functions. In addition to the expected collection of nutrient processing and transport components, we also identified molecules expected to function in the regulation of actin dynamics, membrane bending, and extracellular adhesion. These results provide a foundation for future studies aimed at defining the molecular mechanisms underpinning brush border assembly and function.

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Glycosylation pattern of brush border-associated glycoproteins in enterocyte-like cells: involvement of complex-type N-glycans in apical trafficking

Cited by 41 publications

References 56 publications

Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages

Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages

From structural to functional glycomics: core substitutions as molecular switches for shape and lectin affinity of N-glycans

Proteomic analysis of the enterocyte brush border

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