Sweet preferences of MGL: carbohydrate specificity and function

Vliet, Sandra J. van; Saeland, Eiríkur; Kooyk, Yvette van

doi:10.1016/j.it.2007.10.010

Cited by 150 publications

(143 citation statements)

References 72 publications

Supporting

Mentioning

139

Contrasting

Unclassified

Order By: Relevance

“…MMR and DC-SIGN bind both mannose and fucose residues, whereas CLEC10A specifically recognizes a-and b-linked N-acetylgalactosamine. [26][27][28] Each of these carbohydrate structures is present in FX, 29 providing a rationale for a potential interaction between FX and these receptors. However, despite their evident expression in THP1 macrophages (supplemental Figure 1), no colocalization was found when assessed via Duolink-PLA analysis (Figure 2).…”

Section: Discussionmentioning

confidence: 99%

Macrophage receptor SR-AI is crucial to maintain normal plasma levels of coagulation factor X

Muczynski

Bazaa

Loubière

et al. 2016

Blood

View full text Add to dashboard Cite

Key Points• SR-AI is the major receptor of FX at the macrophage surface.• Macrophages use SR-AI to control FX circulatory levels.Beside its classical role in the coagulation cascade, coagulation factor X (FX) is involved in several major biological processes including inflammation and enhancement of virusinduced immune responses. We recently reported that the long circulatory half-life of FX is linked to its interaction with liver-resident macrophages. Importantly, we now observed that macrophages, but not undifferentiated monocytes, support this interaction. Using cell biology approaches with primary and THP1-derived macrophages as well as transfected cells, we further identified the scavenger receptor type A member I (SR-AI) to be a macrophage-specific receptor for FX. This result was confirmed using SR-AI-deficient mice, which exhibit reduced circulating levels of FX in vivo and loss of FX-macrophage interactions in vitro. Binding studies using purified proteins revealed that FX binds specifically (half-maximal binding, 3 mg/mL) to the extracellular domain of SR-AI. Altogether, we demonstrate that macrophages regulate FX plasma levels in an SR-AI-dependent manner. (Blood. 2016;127(6):778-786)

show abstract

Section: Discussionmentioning

confidence: 99%

Macrophage receptor SR-AI is crucial to maintain normal plasma levels of coagulation factor X

Muczynski

Bazaa

Loubière

et al. 2016

Blood

View full text Add to dashboard Cite

show abstract

“…Because uptake of PKH67-labeled exosomes was markedly decreased when incubation with macrophages was carried out in the presence of EDTA (supplemental Figure 5), binding of exosomes to macrophages could be mediated by their C-type lectin receptor. 53 In the red-cell maturation setting, galectin-5 would, besides its putative exosomal segregation/sorting function, thus be involved in limiting interactions between glycoproteins presenting galactosidecontaining determinants on the surface of red cells with C-type lectin receptors on phagocytic cells. The competition of 2 different lectins for the same epitopes would then attain functional relevance.…”

Section: Discussionmentioning

confidence: 99%

“…However, the size of exosomes (60-80 nm) compared with the size of cells (6-8 m) likely allows (1) a greater density of N-acetyllactosamine-bearing glycoconjugates per membrane surface unit and (2) the possibility of being taken up through endocytosis, the average size of clathrin coated pits being around 0.3 m, eg via macrophage C-type asialoglycoprotein receptors. 16,53 This study suggests that the secretion of galectin-5 has a direct impact on the biogenesis and fate of rat reticulocyte exosomes. …”

mentioning

confidence: 81%

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

254

211

View full text Add to dashboard Cite

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...

show abstract

“…Guided by the reported binding characteristics of MR, MGL, and DC-SIGN, the Lewis X elements present on both IPSE/alpha-1 and omega-1 are potential ligands for DC-SIGN (41), and they may also confer MR binding (42,43). In contrast, kappa-5 is a candidate ligand for MGL that binds to ␣-and ␤-linked GalNAc residues (44). Another special property of kappa-5 is that it is recognized by IgE as well as IgG antibodies in sera from S. mansoni infected individuals but not from uninfected individuals, whereas no other SEA components are as strongly reactive with IgE (18).…”

Section: Kappa-5-reactive Ige Antibodies In Human Infectionmentioning

confidence: 99%

Targeted Glycoproteomic Analysis Reveals That Kappa-5 is a Major, Uniquely Glycosylated Component of Schistosoma mansoni Egg Antigens

Meevissen

Balog

Koeleman

et al. 2011

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

Glycans present on glycoproteins from the eggs of the parasite Schistosoma mansoni are mediators of various immune responses of the human host, including T-cell modulation and granuloma formation, and they are the target of glycan-specific antibodies. Here we have analyzed the glycosylation of kappa-5, a major glycoprotein antigen from S. mansoni eggs using a targeted approach of lectin purification followed by mass spectrometry of glycopeptides as well as released glycans. We demonstrate that kappa-5 has four fully occupied N-glycosylation sites carrying unique triantennary glycans composed of a difucosylated and xylosylated core region, and immunogenic GalNAc␤1-4GlcNAc (LDN) termini. Furthermore, we show that the kappa-5 specific IgE antibodies in sera of S. mansoni-infected individuals are directed against the core region of the kappa-5 glycans. Whereas two previously analyzed immunomodulatory egg glycoproteins, IPSE/alpha-1 and omega-1, both express diantennary N-glycans with a difucosylated core and one or two Gal␤1-4(Fuc␣1-3)GlcNAc (Lewis X) antennae, the kappa-5 glycosylation appears unique among the major soluble egg antigens of S. mansoni. The distinct structural and antigenic properties of kappa-5 glycans suggest a specific role for kappa-5 in schistosome egg immunogenicity.

show abstract

Sweet preferences of MGL: carbohydrate specificity and function

Cited by 150 publications

References 72 publications

Macrophage receptor SR-AI is crucial to maintain normal plasma levels of coagulation factor X

Macrophage receptor SR-AI is crucial to maintain normal plasma levels of coagulation factor X

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

Targeted Glycoproteomic Analysis Reveals That Kappa-5 is a Major, Uniquely Glycosylated Component of Schistosoma mansoni Egg Antigens

Contact Info

Product

Resources

About