scholarly journals P- and E-selectin use common sites for carbohydrate ligand recognition and cell adhesion.

1993 ◽  
Vol 120 (5) ◽  
pp. 1227-1235 ◽  
Author(s):  
D V Erbe ◽  
S R Watson ◽  
L G Presta ◽  
B A Wolitzky ◽  
C Foxall ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Sialic Acid ◽  
Sialyl Lewis X ◽  
Homologous Region ◽  
Carbohydrate Recognition ◽  
Lectin Domain ◽  
Calcium Dependent ◽  
Sialyl Lewis ◽  
Adhesive Interactions ◽  
Carbohydrate Ligand

The selectins are a family of three calcium-dependent lectins that mediate adhesive interactions between leukocytes and the endothelium during normal and abnormal inflammatory episodes. Previous work has implicated the carbohydrate sialyl Lewis(x) (sLe(x); sialic acid alpha 2-3 galactose beta 1-4 [Fucose alpha 1-3] N-acetyl glucosamine) as a component of the ligand recognized by E- and P-selectin. In the case of P-selectin, other components of the cell surface, including 2'6-linked sialic acid and sulfatide (galactose-4-sulfate ceramide), have also been proposed for adhesion mediated by this selectin. We have recently defined a region of the E-selectin lectin domain that appears to be directly involved with carbohydrate recognition and cell adhesion (Erbe, D. V., B. A. Wolitzky, L. G. Presta, C. R. Norton, R. J. Ramos, D. K. Burns, R. M. Rumberger, B. N. N. Rao, C. Foxall, B. K. Brandley, and L. A. Lasky. 1992. J. Cell Biol. 119:215-227). Here we describe a similar analysis of the P-selectin lectin domain which demonstrates that a homologous region of this glycoprotein's lectin motif is involved with carbohydrate recognition and cell binding. In addition, we present evidence that is inconsistent with a biological role for either 2'6-linked sialic acid or sulfatide in P-selectin-mediated adhesion. These results suggest that a common region of the E- and P-selectin lectin domains appears to mediate carbohydrate recognition and cell adhesion.

scholarly journals The three members of the selectin receptor family recognize a common carbohydrate epitope, the sialyl Lewis(x) oligosaccharide

1992 ◽  
Vol 117 (4) ◽  
pp. 895-902 ◽  
Author(s):  
C Foxall ◽  
SR Watson ◽  
D Dowbenko ◽  
C Fennie ◽  
LA Lasky ◽  
...  
Keyword(s):  
Adhesion Molecule ◽  
Leukocyte Adhesion ◽  
Structural Features ◽  
Sialyl Lewis X ◽  
Lewis X ◽  
Leukocyte Adhesion Molecule ◽  
Lectin Domain ◽  
Calcium Dependent ◽  
Carbohydrate Epitope ◽  
Sialyl Lewis

The selectins (lectin-EGF-complement binding-cell adhesion molecules [LEC-CAMs]) are a family of mammalian receptors implicated in the initial interactions between leukocytes and vascular endothelia, leading to lymphocyte homing, platelet binding, and neutrophil extravasation. The three known selectins, L-selectin (leukocyte adhesion molecule-1 [LECAM-1]), E-selectin (endothelial-leukocyte adhesion molecule-1 [ELAM-1]), and P-selectin (GMP-140) share structural features that include a calcium-dependent lectin domain. The sialyl Lewis(x) carbohydrate epitope has been reported as a ligand for both E- and P-selectins. Although L-selectin has been demonstrated to bind to carbohydrates, structural features of potential mammalian carbohydrate ligand(s) have not been well defined. Using an ELISA developed with a sialyl Lewis(x)-containing glycolipid and an E-selectin-IgG chimera, we have demonstrated the direct binding of the L-selectin-IgG chimera to sialyl Lewis(x). This recognition was calcium dependent, and could be blocked by Mel-14 antibody but not by other antibodies. Recognition was confirmed by the ability of cells expressing the native L-selectin to adhere to immobilized sialyl Lewis(x). These data suggest that the sialyl Lewis(x) oligosaccharide may form the basis of a recognition domain common to all three selectins.

Synthetic Studies on Sialoglycoconjugates 85: Synthesis of Sialyl Lewis X Ganglioside Analogs Containing a Variety of Anionic Substituents in Place of Sialic Acid

1996 ◽  
Vol 15 (4) ◽  
pp. 399-418 ◽  
Author(s):  
Masahiro Yoshida ◽  
Yukiko Kawakami ◽  
Hideharu Ishida ◽  
Makoto Kiso ◽  
Akira Hasegawa
Keyword(s):  
Sialic Acid ◽  
Sialyl Lewis X ◽  
Lewis X ◽  
Sialyl Lewis ◽  
Synthetic Studies

In Vitro Selection of the RNA Aptamer against the Sialyl Lewis X and Its Inhibition of the Cell Adhesion

2001 ◽  
Vol 281 (1) ◽  
pp. 237-243 ◽  
Author(s):  
Sunjoo Jeong ◽  
Tae-Yeon Eom ◽  
Se-Jin Kim ◽  
Seong-Wook Lee ◽  
Jaehoon Yu
Keyword(s):  
Cell Adhesion ◽  
In Vitro Selection ◽  
Sialyl Lewis X ◽  
Rna Aptamer ◽  
Lewis X ◽  
Sialyl Lewis ◽  
Selection Of

scholarly journals Sialyl-Lewis x-Independent Infection of Human Myeloid Cells by Anaplasma phagocytophilum Strains HZ and HGE1

2007 ◽  
Vol 75 (12) ◽  
pp. 5720-5725 ◽  
Author(s):  
Madhubanti Sarkar ◽  
Dexter V. Reneer ◽  
Jason A. Carlyon
Keyword(s):  
Sialic Acid ◽  
Anaplasma Phagocytophilum ◽  
Myeloid Cells ◽  
Sialyl Lewis X ◽  
Lewis X ◽  
Bacterial Populations ◽  
Obligate Intracellular ◽  
Granulocytic Anaplasmosis ◽  
Sialyl Lewis ◽  
N Terminus

ABSTRACT Anaplasma phagocytophilum, the causative agent of human granulocytic anaplasmosis, is an obligate intracellular bacterium that infects neutrophils and neutrophil precursors. Bacterial recognition of P-selectin glycoprotein ligand-1 (PSGL-1) and the α2,3-sialylated- and α1,3-fucosylated-moiety sialyl-Lewis x (sLex), which modifies the PSGL-1 N terminus, is important for adhesion to and invasion of myeloid cells. We have previously demonstrated that A. phagocytophilum organisms of the NCH-1 strain that utilize an sLex-modified PSGL-1-independent means of entry can be enriched for by cultivation in undersialylated HL-60 cells that are unable to construct sLex. Because it was unknown whether other A. phagocytophilum isolates share this ability, we extended our studies to the geographically diverse strains HZ and HGE1. HL-60 A2 is a clonal cell line that is defective for sialylation and α1,3-fucosyltransferase. HL-60 A2 cell surfaces, therefore, not only lack sLex but also are virtually devoid of any other sialic acid- and/or α1,3-fucose-modified glycan. By cultivating HZ and HGE1 in HL-60 A2 cells, we enriched for bacterial subpopulations (termed HZA2 and HGE1A2) that bind and/or infect myeloid cells in the absence of sialic acid and α1,3-fucose and in the presence of antibody that blocks the N terminus of PSGL-1. Thus, multiple A. phagocytophilum isolates share the ability to use sLex-modified PSGL-1-dependent and -independent routes of entry into myeloid cells. HZA2 and HGE1A2 represent enriched bacterial populations that will aid dissection of the complexities of the interactions between A. phagocytophilum and host myeloid cells.

scholarly journals Suppression of Sialyl Lewis X Expression and E-selectin-mediated Cell Adhesion in Cultured Human Lymphoid Cells by Transfection of Antisense cDNA of an α1→3 Fucosyltransferase (Fuc-T VII)

1996 ◽  
Vol 271 (49) ◽  
pp. 31556-31561 ◽  
Author(s):  
Nozomu Hiraiwa ◽  
Taeko Dohi ◽  
Naoko Kawakami-Kimura ◽  
Miki Yumen ◽  
Katsuyuki Ohmori ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Lymphoid Cells ◽  
Sialyl Lewis X ◽  
Lewis X ◽  
Sialyl Lewis

Glycan engineering using synthetic ManNAc analogues enhances sialyl-Lewis-X expression and adhesion of leukocytes

2021 ◽  
Author(s):  
Anam Tasneem ◽  
Shubham Parashar ◽  
Tanya Jain ◽  
Simran Aittan ◽  
Jyoti Rautela ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Inflammatory Diseases ◽  
Leukocyte Adhesion ◽  
Fold Increase ◽  
Sialyl Lewis X ◽  
Lewis X ◽  
Sialyl Lewis ◽  
Acute Myeloid Leukemia Cells ◽  
Coated Surfaces ◽  
Cell Cell

Cell surface glycans, depending on their structures and dynamic modifications, act as the first point of contact and regulate cell-cell, cell-matrix, and cell-pathogen interactions. Particularly, the sialyl-Lewis-X (sLeX, CD15s) tetrasaccharide epitope, expressed on both glycoproteins and gangliosides, participates in leukocyte extravasation via interactions with selectins expressed on endothelial cells, lymphocytes, and platelets (CD62-E/L/P). Neutrophils carrying sLeX epitopes are thought to be responsible for chronic inflammatory diseases resulting in plaque formation and atherosclerosis. Intense efforts have been devoted to the development of sLeX mimetics for inhibition of cell adhesion. On the other hand, dysregulated expression of sLeX and poor extravasation are the major underlying causes of leukocyte adhesion deficiency-II (LAD-II) disorders that result in frequent infections and poor immune response. We hypothesized that metabolic processing of peracetyl N-(cycloalkyl)acyl-D-mannosamine derivatives, through the sialic acid pathway, might result in the expression of sialoglycans with altered hydrophobicity which in-turn could modulate their binding to endogenous lectins, including selectins. Herein, we show that treatment of HL-60 (human acute myeloid leukemia) cells with peracetyl N-cyclobutanoyl-D-mannosamine (Ac4ManNCb), at 50 microM for 48 h, resulted in a robust three to four fold increase in the binding of anti-sLeX (CSLEX1) antibody and enhanced cell adhesion to E-selectin coated surfaces; while the corresponding straight-chain analogue, peracetyl N-pentanoyl-D-mannosamine (Ac4ManNPent), and peracetyl N-cyclopropanoyl-D-mannosamine (Ac4ManNCp) both resulted in 2.0-2.5fold increase compared to controls. The ability to enhance sLeX expression using small molecules has the potential to provide novel opportunities to address challenges in the treatment of immune deficiency disorders.

scholarly journals Evaluation of Strategies Aimed at Improving Liver Progenitor Cell Rolling and Subsequent Adhesion to the Endothelium

2020 ◽  
Vol 29 ◽  
pp. 096368972091270
Author(s):  
Pierre Edouard Dollet ◽  
Mei Ju Hsu ◽  
Jérôme Ambroise ◽  
Milena Rozzi ◽  
Joachim Ravau ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Cell Adhesion ◽  
Alternative Methods ◽  
Sialyl Lewis X ◽  
Thermosensitive Polymer ◽  
Lewis X ◽  
Promising Alternative ◽  
Sialyl Lewis ◽  
Selectin Ligand

Adult-derived human liver stem/progenitor cells (ADHLSCs) are a promising alternative to orthotopic liver transplantation in the treatment of inborn errors of metabolism. However, as is the case with many mesenchymal stromal cells, ADHLSCs have shown a low level of engraftment, which could be explained by the fact that they lack expression of selectin ligand and LFA-1 and only slightly express VLA- 4, molecules that have been shown to be involved in cell adhesion to the endothelium. In this paper, we have investigated strategies to increase their rolling and adhesion during the homing process by (1) adding a selectin ligand (Sialyl Lewis X) to their surface using biotinyl- N-hydroxy-succinimide–streptavidin bridges, and (2) protecting the adhesion proteins from trypsinization-induced damage using a thermosensitive polymer for cell culture and a nonenzymatic cell dissociation solution (CDS) for harvest. Despite increasing adhesion of ADHLSCs to E-selectin during an adhesion test in vitro performed under shear stress, the addition of Sialyl Lewis X did not increase adhesion to endothelial cells under the same conditions. Cultivating cells on a thermosensitive polymer and harvesting them with CDS increased their adhesion to endothelial cells under noninflammatory conditions, compared to the use of trypsin. However, we were not able to demonstrate any improvement in cell adhesion to the endothelium following culture on polymer and harvest with CDS, suggesting that alternative methods of improving engraftment still need to be evaluated.

scholarly journals Systematic chemoenzymatic synthesis of O-sulfated sialyl Lewis x antigens

2016 ◽  
Vol 7 (4) ◽  
pp. 2827-2831 ◽  
Author(s):  
Abhishek Santra ◽  
Hai Yu ◽  
Nova Tasnima ◽  
Musleh M. Muthana ◽  
Yanhong Li ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Chemoenzymatic Synthesis ◽  
Sialyl Lewis X ◽  
Lewis X ◽  
Sialyl Lewis

O-Sulfated sialyl Lewisxantigens containing different sialic acid forms were chemoenzymatically synthesized using a bacterial sialyltransferase mutant.

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