Untitled

Abstract

Glycosylated structures on the cell surface have a role in cell adhesion, migration, and proliferation. Repair of the airway epithelium after injury requires each of these processes, but the normal cell surface glycosylation of non-mucin producing airway epithelial cells is unknown. We examined cell surface glycosylation in human airway epithelial cells in tissue sections and in human airway epithelial cell lines in culture. Thirty-eight lectin probes were used to determine specific carbohydrate residues by lectin-histochemistry. Galactose or galactosamine-specific lectins labeled basal epithelial cells, lectins specific for several different carbohydrate structures bound columnar epithelial cells, and fucose-specific lectins labeled all airway epithelial cells. The epithelial cell lines 1HAEo- and 16HBE14o- bound lectins that were specific to basal epithelial cells. Flow cytometry of these cell lines with selected lectins demonstrated that lectin binding was to cell surface carbohydrates, and revealed possible hidden tissue antigens on dispersed cultured cells. We demonstrate specific lectin-binding patterns on the surface of normal human airway epithelial cells. The expression of specific carbohydrate residues may be useful to type epithelial cells and as a tool to examine cell events involved in epithelial repair.

Variation in Carbohydrates between Cancer and Normal Cell Membranes Revealed by Super‐Resolution Fluorescence Imaging

“…Lectin from Phaseolus vulgaris (PHA‐L, from EY laboratories) for oligosaccharide,38, 39 Maackia amurensis lectin (MAL, from Sigma) for sialic acid linked to galactose by an α2‐3 linkage,40, 41 wheat germ agglutinin (WGA, from Sigma) mainly binding to GlcNAc and its β‐(1→4)‐linked oligosaccharides,38, 42 erythrina cristagalli lectin (ECL, from Sigma) for D‐Galβ1‐4GlcNAc (Gal),38 lectin from glycine max (soybean) (SBA) with high affinity for GalNAc,42, 43 lectin from Morniga M (MNA‐M, from EY laboratories) for Man,44 and lectin from Anguilla anguilla (eel) (AAA, from Sigma) for Fuc 38, 45. With finishing the reaction of the lectin solution with Alexa647 (Molecular Probes) at 27 °C for ≈3 h with gentle vortex, the redundant free Alexa647 was removed by using a PD Spin Trap G‐25 filtration column (GE Healthcare).…”

Systemic localization of seven major types of carbohydrates on cell membranes by dSTORM imaging

“…S1, in Supporting Information ). Based on the curves, the labeling concentration of each lectin was determined as ~3 μg/mL of maackia amurensis lectin (MAL) showing high affinity for sialic acid linked to galactose by an α2-3 linkage (Sia) 23 24 , ~9.3 μg/mL of lectin from Phaseolus vulgaris (PHA-L) for oligosaccharide (pentasaccharide sequence Galβ1-4GlcNAcβ1-2(Galβ1-4GlcNAcβ1-6) Manα1-R (the so-called “2,6-branch”)) 25 26 , ~2.88 μg/mL of wheat germ agglutinin (WGA) that mainly interacts with high affinity with N-acetyl-D-glucosamine (GlcNAc) and its β-(1 → 4)-linked oligosaccharides 25 27 , ~12.5 μg/mL of lectin from Anguilla anguilla (eel) (AAA) that is a fucose (Fuc) specific lectin 25 28 , ~7 μg/mL of lectin from Morniga M (MNA-M) whose binding specificities of mannose (Man) 29 , ~3.75 μg/mL of erythrina cristagalli lectin (ECL) for D-Galβ1-4GlcNAc (Gal) 25 , and ~10.5 μg/mL of lectin from glycine max (SBA) possessing high affinity for N-acetylgalactosamine (GalNAc) 27 30 .…”

Development of a highly selective glycomimetic ligand for L-SIGN: a new tool against SARS-CoV-2 and Ebola viruses

“…4 KDapp or IC50 ratio of DC-SIGN over L-SIGN. 5 As measured by ITC (Fig. 3) * KD of the monovalent ligand not determined.…”

“…The diverse CLRs differ in size, oligomerization state and signaling pathways, and will therefore have a different impact on the immune system depending on the panels of glycans they recognize 2,3 . However, not all CLRs are strictly dedicated to immunity and some of them are even expressed in other cell types and tissues such as hepatocytes or endothelial cells from blood capillaries to airway epithelia 4,5 . These lectin receptors, therefore, have other functions such as physiological clearance mechanisms (e.g.…”