Subsets of Epidermal Langerhans Cells as Defined by Lectin Binding Profiles

Abstract

In this study we characterize the cell surface glycoconjugate moieties of strain 2 guinea pig epidermal Langerhans cells (LC) in single cell suspension by using a battery of 17 fluorescent lectins. All LC displayed binding sites for concanavalin A, succinylated concanavalin A, Lens culinaris agglutinin, Pisum sativum agglutinin, wheat germ agglutinin, succinylated wheat germ agglutinin, Griffonia simplicifolia agglutinin I, Ricinus communis agglutinin I, Phaseolus vulgaris E agglutinin, and Phaseolus vulgaris L agglutinin, but failed to bind Sophora japonica agglutinin (SJA), Dolichos biflorus agglutinin (DBA), and Ulex europaeus agglutinin I (UEA I). Neuraminidase pretreatment rendered LC reactive for SJA, but not for DBA and UEA I. The binding profiles of certain lectins point to the existence of LC subpopulations in that Griffonia simplicifolia I-B4 isolectin, peanut agglutinin (PNA), Helix pomatia agglutinin, and soybean agglutinin bound to only 80% (range 70-90%) of Ia-positive epidermal cells; binding sites for these lectins on primarily unreactive Ia-positive cells were unmasked when epidermal cells were treated with neuraminidase prior to lectin labeling. Ultrastructural PNA labeling studies revealed that the vast majority of Birbeck granule-containing LC displayed PNA binding sites, whereas indeterminate cells were consistently PNA-negative. Identification of carbohydrate configurations expressed on LC surfaces by lectin binding may provide a clue for the elucidation of the mechanisms of established LC functions and possibly the discovery of as yet unknown properties of this cell type.

Identification of dendritic antigen-presenting cells in the zebrafish

“…Measurements of these granules through the rodshaped region gave a mean diameter of 37.7 ± 8.59 nm, similar to that of Birbeck granules found in human (45 nm) and murine (43 nm) LCs (23,24). Considering that Birbeck granules are the morphological markers of mammalian LCs, and that these cells also exhibit PNA binding (15,16), we postulate that PNA hi DCs isolated from skin are the LC counterpart in zebrafish, supporting the existence of LCs in teleosts, as previously proposed (10).…”

“…Lectins are sugar-binding proteins that recognize complex carbohydrate structures on the cell surface and have been used extensively to distinguish different leukocyte populations in mice and humans (13). Peanut agglutinin (PNA) is a lectin that binds preferentially to galactosyl (β−1, 3) N-acetylgalactosamine, a carbohydrate structure present on some leukocytes, including DC subsets in humans and LCs in both mouse and guinea pigs (14)(15)(16). For these reasons, we examined PNA binding on zebrafish leukocytes.…”

Role of epidermal Langerhans cells in viral infections

“…Langerhans cells are bone marrow-derived [59], bear class II antigens [92,120], and display the T-6 and the T-200 antigens in man [38,76] whereas in mice they generally express the T L and Ly-5 antigens [68,95]. Several subsets of Langerhans cells have been identified by selective binding to various lectins [101]. Their cytoplasm stains positive with anti-S-100 (a protein found in Schwann cells and melanocytes) [96] and anti-vimentin (a protein found both in endothelial cells and fibroblasts) [32] antisera.…”

Lectin binding in oral mucosa of mammals.

“…PNA and RCA-1 are linked to Dgalactose (Gal) ; DBA and SBA, to N-acetyl-D-galactosamine (Ga1NAC) ; WGA to N-acetyl-D-glucosamine (G1cNAc) and N-acetyl-D-neuraminic acid (NeuNAc) ; UEA-1, to L-fucose (Fuc) (8). It has been pointed out that lectin-conjugates bind to intercellular materials, cells coats, and basement membranes of oral mucosa (3-6) and skin (1,9,15,16,25,26,30). These experiments were conducted to determine if the cell coat or intercellular materials in oral epithelia contain Gal, GaINAc, and G1cNAc residues in the spinous cells and hence determine if they are positive to PAS staining.…”