scholarly journals A Atractylodes lancea polysaccharide inhibits metastasis of human osteosarcoma U‐2 OS cells by blocking sialyl Lewis X (sLe x )/E‐selectin binding

2020 ◽  
Vol 24 (21) ◽  
pp. 12789-12798
Author(s):  
Kaihua Zhong ◽  
Shuxin Fan ◽  
Shujun Yao ◽  
Haibin Xu ◽  
Suping Bai
Keyword(s):  
Sialyl Lewis X ◽  
Lewis X ◽  
Human Osteosarcoma ◽  
Atractylodes Lancea ◽  
Sialyl Lewis ◽  
Selectin Binding

Studies on Selectin Blockers. 4. Structure−Function Relationships of Sulfated Sialyl Lewis X Hexasaccharide Ceramides toward E-, P-, and L-Selectin Binding

1997 ◽  
Vol 40 (4) ◽  
pp. 455-462 ◽  
Author(s):  
Kohichiro Yoshino ◽  
Hiroshi Ohmoto ◽  
Noriko Kondo ◽  
Hideki Tsujishita ◽  
Yasuyuki Hiramatsu ◽  
...  
Keyword(s):  
Structure Function ◽  
Sialyl Lewis X ◽  
Lewis X ◽  
Sialyl Lewis ◽  
Selectin Binding

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.

scholarly journals Glycoforms of human endothelial CD34 that bind L-selectin carry sulfated sialyl Lewis x capped O- and N-glycans

Blood ◽  
2009 ◽  
Vol 114 (3) ◽  
pp. 733-741 ◽  
Author(s):  
Gerard Hernandez Mir ◽  
Jari Helin ◽  
Kari-Pekka Skarp ◽  
Richard D. Cummings ◽  
Antti Mäkitie ◽  
...  
Keyword(s):  
Sialyl Lewis X ◽  
Affinity Binding ◽  
Lewis X ◽  
High Affinity ◽  
Human Cd34 ◽  
Sialyl Lewis ◽  
Selectin Ligand ◽  
Sulfated Carbohydrate ◽  
A Minor ◽  
Selectin Binding

Abstract Endothelial sialomucin CD34 functions as an L-selectin ligand mediating lymphocyte extravasation only when properly glycosylated to express a sulfated carbohydrate epitope, 6-sulfo sialyl Lewis x (6-sulfo SLex). It is thought that multivalent 6-sulfo SLex expression promotes high-affinity binding to L-selectin by enhancing avidity. However, the reported low amount of 6-sulfo SLex in total human CD34 is inconsistent with this model and prompted us to re-evaluate CD34 glycosylation. We separated CD34 into 2 glycoforms, the L-selectin–binding and nonbinding glycoforms, L-B-CD34 and L-NB-CD34, respectively, and analyzed released O- and N-glycans from both forms. L-B-CD34 is relatively minor compared with L-NB-CD34 and represented less than 10% of total tonsillar CD34. MECA-79, a mAb to sulfated core-1 O-glycans, bound exclusively to L-B-CD34 and this form contained all sulfated and fucosylated O-glycans. 6-Sulfo SLex epitopes occur on core-2 and extended core-1 O-glycans with approximately 20% of total L-B-CD34 O-glycans expressing 6-sulfo SLex. N-glycans containing potential 6-sulfo SLex epitopes were also present in L-B-CD34, but their removal did not abolish binding to L-selectin. Thus, a minor glycoform of CD34 carries relatively abundant 6-sulfo SLex epitopes on O-glycans that are important for its recognition by L-selectin.

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
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