Ligand recognition by E-selectin: analysis of conformation and activity of synthetic monomeric and bivalent sialyl Lewis X analogs

1993 ◽  
Vol 115 (16) ◽  
pp. 7549-7550 ◽  
Author(s):  
Shawn A. DeFrees ◽  
Federico C. A. Gaeta ◽  
Ying Chih Lin ◽  
Yoshitaka Ichikawa ◽  
Chi Huey Wong
Keyword(s):  
Sialyl Lewis X ◽  
Ligand Recognition ◽  
Lewis X ◽  
Sialyl Lewis

Ligand Recognition by E-Selectin: Synthesis, Inhibitory Activity and Conformational Analysis of Bivalent Sialyl Lewis x Analogs

1995 ◽  
Vol 117 (1) ◽  
pp. 66-79 ◽  
Author(s):  
Shawn A. DeFrees ◽  
Winfried Kosch ◽  
William Way ◽  
James C. Paulson ◽  
Subramanian Sabesan ◽  
...  
Keyword(s):  
Conformational Analysis ◽  
Inhibitory Activity ◽  
Sialyl Lewis X ◽  
Ligand Recognition ◽  
Lewis X ◽  
Sialyl Lewis

Persistent HIV Transcription Induces Sialyl-Lewis-X Glyco-Antigen Cell-Surface Expression

2020 ◽  
Author(s):  
Florent Colomb ◽  
Leila B. Giron ◽  
Leticia Kuri Cervantes ◽  
Tongcui Ma ◽  
Samson Adeniji ◽  
...  
Keyword(s):  
Cell Surface ◽  
Surface Expression ◽  
Sialyl Lewis X ◽  
Cell Surface Expression ◽  
Lewis X ◽  
Hiv Transcription ◽  
Sialyl Lewis

scholarly journals Sialyl Lewis X mimics derived from a pharmacophore search are selectin inhibitors with anti-inflammatory activity.

1994 ◽  
Vol 269 (31) ◽  
pp. 19663-19666
Author(s):  
B.N. Rao ◽  
M.B. Anderson ◽  
J.H. Musser ◽  
J.H. Gilbert ◽  
M.E. Schaefer ◽  
...  
Keyword(s):  
Inflammatory Activity ◽  
Sialyl Lewis X ◽  
Lewis X ◽  
Sialyl Lewis ◽  
Anti Inflammatory

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.

Sulfated Sialyl Lewis X, the Putative L-Selectin Ligand, Detected on Endothelial Cells of High Endothelial Venules by a Distinct Set of Anti-Sialyl Lewis X Antibodies

1997 ◽  
Vol 230 (3) ◽  
pp. 546-551 ◽  
Author(s):  
Chikako Mitsuoka ◽  
Naoko Kawakami-Kimura ◽  
Mikiko Kasugai-Sawada ◽  
Nozomu Hiraiwa ◽  
Ken'ichi Toda ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Sialyl Lewis X ◽  
Lewis X ◽  
High Endothelial Venules ◽  
Sialyl Lewis ◽  
Selectin Ligand
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