title: Griffonia simplicifolia lectins bind specifically to endothelial cells and some epithelial cells in mouse tissues.
abstract: The binding of Griffonia simplicifolia agglutinin-I (GSA-I) and the isolectins GSA-I-AB3 and GSA-I-B4, having affinity for some alpha-D-galactosyl and N-acetyl galactosaminyl residues was studied in different mouse tissues. In brain, cardiac muscle and skeletal muscle, the GSA-I-lectin conjugates showed prominent binding only to blood vessel endothelia. Similarly, in the liver and kidney cortex the GSA-I-conjugates selectively reacted with endothelial cells of the sinusoids and with intertubular and glomerular capillaries, respectively. However, a strong reactivity with the GSA-I-conjugates was additionally seen in the acinar cells of the pancreas, in the stratified squamous epithelia of skin and tongue, and in transitional epithelium. SDS-PAGE electrophoresis combined with the lectin-blotting technique indicated that a similar set of glycoproteins are responsible for the GSA-I binding, even in different tissues. Another lectin with specificity for alpha-D-galactose, the Maclura pomifera agglutinin, displayed a distinctly different distribution of binding sites, mainly in the basement membranes, of all mouse tissues studied. The results suggest that some alpha-D-galactosyl residues, recognized by the binding of GSA-I lectins, are preferentially expressed in endothelial cells of mouse tissues, and also provide further evidence that endothelial cells can present a highly specific surface glycosylation pattern.
mesh_terms: D000818:Animals; D004727:Endothelium / Q000276:immunology*; D004848:Epithelium / Q000276:immunology; D006651:Histocytochemistry; D037102:Lectins / Q000378:metabolism*; D051379:Mice; D008815:Mice, Inbred Strains; D037121:Plant Lectins; D011975:Receptors, Mitogen / Q000378:metabolism*; D013045:Species Specificity; D014018:Tissue Distribution
chemical_list: C045475:Griffonia simplicifolia lectins; D037102:Lectins; D037121:Plant Lectins; D011975:Receptors, Mitogen