scholarly journals Selectin glycoprotein ligands.

2000 ◽  
Vol 47 (2) ◽  
pp. 393-412 ◽  
Author(s):  
I Zak ◽  
E Lewandowska ◽  
W Gnyp
Keyword(s):  
Biosynthetic Pathway ◽  
Structure And Function ◽  
Cell Interactions ◽  
Sialyl Lewis X ◽  
Lewis X ◽  
Sialyl Lewis ◽  
Selectin Ligands ◽  
The Common ◽  
And Function ◽  
Lymphatic Organs

Lectin selectins and their counter-receptors participate in discontinuous cell-cell interactions concurrent with leukocyte tethering and rolling on endothelium, which, in consequence, leads to leukocyte penetration to lymphatic organs and generation of inflammation sites. Counter-receptors are glycoproteins in which carbohydrate units, the direct selectin ligands, are built into the polypeptide framework. In this review, the distribution, structure and function of the main ligands and counter-receptors for P-, L- and E-selectins known so far, have been discussed. The common biosynthetic pathway of sialyl-Lewis x and sulpho-sialyl-Lewis x determinants of selectin ligands has been described.

scholarly journals Mycobacterium tuberculosis Infection Up-Regulates Sialyl Lewis X Expression in the Lung Epithelium

2021 ◽  
Vol 9 (1) ◽  
pp. 99
Author(s):  
Rita Matos ◽  
Kaori L. Fonseca ◽  
Stefan Mereiter ◽  
Ana Raquel Maceiras ◽  
Joana Gomes ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Biosynthetic Pathway ◽  
Molecular Mechanisms ◽  
Tuberculosis Infection ◽  
Host Susceptibility ◽  
Sialyl Lewis X ◽  
Lung Pathology ◽  
Lung Epithelium ◽  
Lewis X ◽  
Sialyl Lewis

Glycans display increasingly recognized roles in pathological contexts, however, their impact in the host-pathogen interplay in many infectious diseases remains largely unknown. This is the case for tuberculosis (TB), one of the ten most fatal diseases worldwide, caused by infection of the bacteria Mycobacterium tuberculosis. We have recently reported that perturbing the core-2 O-glycans biosynthetic pathway increases the host susceptibility to M. tuberculosis infection, by disrupting the neutrophil homeostasis and enhancing lung pathology. In the present study, we show an increased expression of the sialylated glycan structure Sialyl-Lewis X (SLeX) in the lung epithelium upon M. tuberculosis infection. This increase in SLeX glycan epitope is accompanied by an altered lung tissue transcriptomic signature, with up-regulation of genes codifying enzymes that are involved in the SLeX core-2 O-glycans biosynthetic pathway. This study provides novel insights into previously unappreciated molecular mechanisms involving glycosylation, which modulate the host response to M. tuberculosis infection, possibly contributing to shape TB disease outcome.

scholarly journals Selectin Ligands Sialyl-Lewis a and Sialyl-Lewis x in Gastrointestinal Cancers

Biology ◽  
2017 ◽  
Vol 6 (4) ◽  
pp. 16 ◽  
Author(s):  
Marco Trinchera ◽  
Adele Aronica ◽  
Fabio Dall’Olio
Keyword(s):  
Sialyl Lewis X ◽  
Gastrointestinal Cancers ◽  
Lewis X ◽  
Sialyl Lewis ◽  
Selectin Ligands ◽  
Sialyl Lewis A ◽  
Lewis A

Biosynthesis of L-Selectin Ligands:  Sulfation of Sialyl Lewis x-Related Oligosaccharides by a Family of GlcNAc-6-sulfotransferases†

Biochemistry ◽  
2001 ◽  
Vol 40 (18) ◽  
pp. 5382-5391 ◽  
Author(s):  
Kendra G. Bowman ◽  
Brian N. Cook ◽  
Christopher L. de Graffenried ◽  
Carolyn R. Bertozzi
Keyword(s):  
Sialyl Lewis X ◽  
Lewis X ◽  
Sialyl Lewis ◽  
Selectin Ligands

scholarly journals 6-sulfo sialyl Lewis X is the common receptor determinant recognized by H5, H6, H7 and H9 influenza viruses of terrestrial poultry

2008 ◽  
Vol 5 (1) ◽  
pp. 85 ◽  
Author(s):  
Alexandra S Gambaryan ◽  
Alexander B Tuzikov ◽  
Galina V Pazynina ◽  
Julia A Desheva ◽  
Nicolai V Bovin ◽  
...  
Keyword(s):  
Influenza Viruses ◽  
Sialyl Lewis X ◽  
Lewis X ◽  
Sialyl Lewis ◽  
Common Receptor ◽  
The Common

L-selectin ligands in rat high endothelium: multivalent sialyl Lewis x glycans are high-affinity inhibitors of lymphocyte adhesion

1997 ◽  
Vol 27 (6) ◽  
pp. 1360-1365 ◽  
Author(s):  
Sanna Toppila ◽  
Jouni Lauronen ◽  
Pirkko Mattila ◽  
Juha Pekka Turunen ◽  
Leena Penttilä ◽  
...  
Keyword(s):  
Sialyl Lewis X ◽  
Lewis X ◽  
Lymphocyte Adhesion ◽  
High Affinity ◽  
Sialyl Lewis ◽  
Selectin Ligands

scholarly journals N-glycans of core2 β(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of α(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding

2005 ◽  
Vol 391 (3) ◽  
pp. 491-502 ◽  
Author(s):  
Maëlle Prorok-Hamon ◽  
Frédéric Notel ◽  
Sylvie Mathieu ◽  
Claire Langlet ◽  
Minoru Fukuda ◽  
...  
Keyword(s):  
Drug Targets ◽  
Sialyl Lewis X ◽  
Lewis X ◽  
Sialyl Lewis ◽  
Selectin Ligands ◽  
Glycosylation Sites ◽  
Glycan Chain ◽  
Golgi Compartment ◽  
Selectin Binding

C2GnT-I [core2 β(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [α(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins. In the present study, we examined the importance of N-glycosylation for the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1). We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present. All combined, our results show a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII and disclose that a strongly reduced FucT-VII activity retains the ability to fucosylate PSGL-1 on the core2-based binding site(s) for the three selectins.

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