Chai, W.

Combarnous, Yves

Feizi, T.

Jankovic, M.

Leteux, C.

Loveless, R.W.

Maric, S.C.

Milusovin, Z.

Nussenzweig, M.C.

Uhlin-Hansen, L.

Yuen, C.T.

PubMed

HAL Université de Tours

The cysteine-rich domain of the macrophage mannose receptor is a multispecific lectin that recognizes chondroitin sulfates A and B and sulfated oligosaccharrides of blood group Lewis a and Lewis x types in addition to the sulfated N-glycans of lutropin

A cysteine-rich domain of the “mannose” receptor mediates

A functional soluble form of the murine mannose receptor is produced by macrophages in vitro and is present in mouse serum.

A hepatic reticuloendothelial cell receptor specific for SO4-4-GalNAcb1,4GlcNAcb1,2Mana that mediates rapid clearance of lutropin.

A modified uronic acid carbazole reaction.

Biotinyl-l-3-(2-naphthyl)-alanine hydrazide derivatives of N-glycans: versatile solid-phase probes for carbohydrate-recognition studies.

Cell-specific glycoforms of sialoadhesin and CD45 are counter-receptors for the cysteine-rich domain of the mannose receptor.

Chondroitin sulphate composition and structure in alternatively spliced CD44 fusion proteins.

Crystal structure of the cysteine-rich domain of mannose receptor complexed with a sulfated carbohydrate ligand.

Demonstration by monoclonal antibodies that carbohydrate structures of glycoproteins and glycolipids are onco-developmental antigens.

Dendritic cells use macropinocytosis and the mannose receptor to concentrate macromolecules in the major histocompatibility complex class II compartment: downregulation by cytokines and bacterial products.

Densitometric assay of nanogram quantities of proteoglycans precipitated on nitrocellulose membrane with safranin O.

Equine lutropin and chorionic gonadotropin bear oligosaccharides terminating with SO4-4-GalNAc and Siaa2,3Gal, respectively.

Fc chimeric protein containing the cysteine-rich domain of the murine mannose receptor binds to macrophages from splenic marginal zone and lymph node subcapsular sinus and to germinal centers.

First synthesis of the 39-sulfated Lewisa pentasaccharide, the most potent human E-selectin ligand so far.

Generation and structural characterization of a range of unmodified chondroitin sulfate oligosaccharide fragments.

Hydrazinolysis of asparagine-linked sugar chains to produce free oligosaccharides. Methods Enzymol.

Influence of oligosaccharide presentation on the interactions of carbohydrate sequence-specific antibodies and the selectins. Observations with biotinylated oligosaccharides.

Isolation of the SO4-1125 Leteux et al. 4-GalNAcb1,4GlcNAcb1,2Mana-specific receptor from rat liver.

Molecular characterization of the human macrophage mannose receptor: demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeast in Cos-1 cells.

Monoclonal antibody 91.9H raised against sulfated mucins is specific for the 39-sulfated Lewisa tetrasaccharide sequence.

Multiple interactions between pituitary hormones and the mannose receptor.

Neoglycolipids: probes of oligosaccharide structure, antigenicity, and function. Methods Enzymol.

NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.

Novel sulfated ligands for the cell adhesion molecule E-selectin revealed by the neoglycolipid technology among O-linked oligosaccharides on an ovarian cystadenoma glycoprotein.

Oligosaccharides that mediate mammalian cell-cell adhesion.

Optimal procedure for combined high performance thin-layer chromatography/high sensitivity liquid secondary ion mass spectrometry.

Porcine lutropin and its subunits. Isolation and characterization.

Potential role of the mannose receptor in antigen transport.

Preparation of neoglycolipids for structure and function assignments of oligosaccharides.

Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains.

Proteoglycans in cell regulation.

Proteoglycans in haemopoietic cells.

Reaction of unsaturated uronic acid residues with mercuric salts. Cleavage of the hyaluronic acid disaccharide 2-acetamido-2-deoxy-3-O-(b-d-gluco-4-enepyranosyluronic acid)-d-glucose.

Serglycin expression during monocytic differentiation of U937-1 cells.

Serglycin secreted by leukocytes is efficiently eliminated from the circulation by sinusoidal scavanger endothelial cells in the liver.

Small proteoglycans.

Structural characterisation of two hexasaccharides and an octasaccharide from chondroitin sulfate C containing the unusual sequence (4-sulfo)-N-acetylgalactosamine-b1-4-(2-sulfo)-glucuronic acid-b-1-3-(6-sulfo)-N-acetylgalactosamine.

Structural requirements for high affinity binding of complex ligands by the macrophage mannose receptor.

Syntheses of sulfated derivatives as sialyl Lewisa and sialyl Lewisx analogues.

Synthetic studies on sialoglycoconjugates. 40. Stereocontrolled synthesis of sialyl Lewis X epitope and its ceramide derivative.

The chondroitin sulfate form of invariant chain can enhance stimulation of T cell responses through interaction with CD44.

The glycosaminoglycans in cultures of stimulated rat peritoneal macrophages. 1. Pattern and biosynthesis of glycosaminoglycans.

The macrophage/endothelial cell mannose receptor cDNA encodes a protein that binds oligosaccharides terminating with SO4-4-GalNAcb1,4GlcNAcb or Man at independent sites.

The mannose receptor delivers lipoglycan antigens to endosomes for presentation to T cells by CD1b molecules.

The mannose receptor is a pattern recognition receptor involved in host defence.

The receptor DEC-205 expressed by dendritic cells and thymic epithelial cells is involved in antigen processing.

Valency dependent patterns of binding of human L-selectin towards sialyl and sulfated oligosaccharides of Lea and Lex types: relevance to anti-adhesion therapeutics.

Widespread expression of chondroitin sulfate-type serglycins with CD44 binding ability in hematopoietic cells.

http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2193175

The cysteine-rich domain of the macrophage mannose receptor is a multispecific lectin that recognizes chondroitin sulfates A and B and sulfated oligosaccharrides of blood group Lewis a and Lewis x types in addition to the sulfated N-glycans of lutropin

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