Novel Sulfated Lymphocyte Homing Receptors and Their Control by a Core1 Extension β1,3-N-Acetylglucosaminyltransferase

  title={Novel Sulfated Lymphocyte Homing Receptors and Their Control by a Core1 Extension $\beta$1,3-N-Acetylglucosaminyltransferase},
  author={Jiunn‐chern Yeh and Nobuyoshi Hiraoka and Bronislawa Petryniak and Jun Nakayama and Lesley G. Ellies and David Rabuka and Ole Hindsgaul and Jamey D Marth and John B. Lowe and Minoru Fukuda},

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Core 2 Branching β1,6-N-Acetylglucosaminyltransferase and High Endothelial Venule-restricted Sulfotransferase Collaboratively Control Lymphocyte Homing*

It is suggested that LSST and Core2GlcNAcT cooperatively synthesize HEV-specific L-selectin ligands required for lymphocyte homing and play a critical role in lymphocyte trafficking during chronic inflammation.

N-acetylglucosamine-6-O-sulfotransferases 1 and 2 cooperatively control lymphocyte homing through L-selectin ligand biosynthesis in high endothelial venules

The essential function of GlcNAc6ST-1 and Glcnac6 ST-2 in L-selectin ligand biosynthesis in high endothelial venules and their importance in immune surveillance are demonstrated.

N-Acetylglucosamine 6-O-Sulfotransferase-1 Regulates Expression of L-Selectin Ligands and Lymphocyte Homing*

It is demonstrated that GlcNAc6ST-1 is involved in lymphocyte homing in vivo, and it is indicated that Gl cNAc 6-O-sulfotransferases -2 and -2 play complementary roles, which is particularly high-lighted by its involvement in lymphocytes homing to Peyer's patches where Glc NAc6 ST-2 expression is undetectable.

Model Glycosulfopeptides from P-selectin Glycoprotein Ligand-1 Require Tyrosine Sulfation and a Core 2-branched O-Glycan to Bind to L-selectin*

It is demonstrated that L-selectin binds with high affinity to the N-terminal region of PSGL-1 through cooperative interactions with three sulfated tyrosine residues and an appropriately positioned C2-O-sLex O-glycan.

Critical functions of N-glycans in L-selectin-mediated lymphocyte homing and recruitment

The results demonstrate the critical function of N-glycan-linked 6-sulfo sialyl Lewis X in L-selectin-dependent lymphocyte homing and recruitment in wild-type and mutant mice.

Impaired selectin-ligand biosynthesis and reduced inflammatory responses in beta-1,4-galactosyltransferase-I-deficient mice.

It is demonstrated that beta4GalT-I is a major galactosyltransferase responsible for selectin-ligand biosynthesis and that inflammatory responses of beta4 galactose residues in beta-1,4 linkage-deficient mice are impaired because of the defect in selectIn-ligands biosynthesis.

Endoglycan, a Member of the CD34 Family, Functions as an L-selectin Ligand through Modification with Tyrosine Sulfation and Sialyl Lewis x*

Endoglycan employs a different binding mechanism, interacting with L-selectin through sulfation on two tyrosine residues and O-linked sLex structures that are presented within its highly acidic amino-terminal region, suggesting several potential settings for endoglycan-mediated adhesion events.

Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.

KSST competes with FucT-VII for the same acceptor substrate and downregulates the synthesis of L-selectin ligand by inhibiting alpha1,3-fucosylation, which suggests that KSST downregulate the synthesized structures of oligosaccharides containing 6'-sulfated Gal are almost identical to those synthesized by keratan sulfate sulfotransferase.



Sulfotransferases of Two Specificities Function in the Reconstitution of High Endothelial Cell Ligands for L-selectin

L-selectin, a lectin-like receptor, mediates rolling of lymphocytes on high endothelial venules (HEVs) in secondary lymphoid organs by interacting with HEV ligands, candidates for which are glycosylation- dependent cell adhesion molecule 1 (GlyCAM-1), CD34, and podocalyxin.

L-Selectin Ligands That Are O-glycoprotease Resistant and Distinct from MECA-79 Antigen are Sufficient for Tethering and Rolling of Lymphocytes on Human High Endothelial Venules

A pool of O-glycoprotease-resistant sLex-like L-selectin ligands exist on human HEV that is distinct from the mucin-associated moieties recognized by MECA-79 mAb and it is postulate that these ligands may participate in lymphocyte binding to HEV.

Sulfation-dependent recognition of high endothelial venules (HEV)- ligands by L-selectin and MECA 79, and adhesion-blocking monoclonal antibody

This study compares the requirements for the binding of MECA 79 and LEC-IgG to HEV-ligands and identifies Sgp200, an independent molecule of approximately 200 kD in a sulfate-dependent manner that is an additional ligand for L-selectin.

Structure of the O-Glycans in GlyCAM-1, an Endothelial-derived Ligand for L-selectin

The complete structure of β-eliminated chains of GlyCAM-1 is defined using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography.

Minimal Sulfated Carbohydrates for Recognition by L-selectin and the MECA-79 Antibody*

Surprisingly, 6′,6-disulfolactose was poorly recognized by MECA-79, a carbohydrate- and sulfate-dependent monoclonal antibody that binds competitively to L-selectin ligands, and bound preferentially to 6-sulfolactorose.

Sulphation requirement for GlyCAM-1, an endothelial ligand for L-selectin

It is reported here that GlyCAM-1 has an additional requirement for sulphate, a high endothelial venule-associated, mucin-like glycoprotein containing predominantly O-linked carbohydrate chains.

L-selectin-mediated lymphocyte rolling on MAdCAM-1

The mucosal vascular addressin MAdCAM-1, a mucosal endothelial adhesion molecule with immunoglobulin- and mucin-like domains, is a facultative ligand for L-selectin and may be uniquely adapted to support both selectin-mediated lymphocyte rolling and integrin-mediated adhesion and arrest in vivo.