Identification of UEA I-binding surface glycoproteins of cultured human endothelial cells.
Ulex europaeus agglutinin (UEAI) binds mainly to endothelial cells in human tissues. In cultured human umbilical vein endothelial cells TRITC-UEAI gave an even surface staining but no binding to pericellular material. After permeabilization of the cells UEAI decorated the Golgi apparatus as a juxtanuclear structure. Electrophoresis of Triton X-100 lysates of 35S-methionine labeled cells bound to lectin agarose beads showed that a similar set of polypeptides was recognized by UEA-I and WGA while distinctly different polypeptides were bound to LcA-agarose. Surface labelling revealed major glycoproteins with Mr 220 kD, 160 kD, 140 kD, 120 kD, 80 kD and 50 kD, most of which could be extracted with Triton X-100. However, only the 140 kD gp, 120 kD gp and 80 kD gp showed binding to UEA 140 kD gp, 120 kD gp and 80 kD gp showed binding to UEA I-lectin. The results show that among a distinct set of surface glycoproteins in cultured human endothelial cells only a few have alpha-l-fucosyl moieties capable of binding to UEAI lectin.
D000373:Agglutinins; D001665:Binding Sites; D002478:Cells, Cultured; D004727:Endothelium / Q000378:metabolism*; D005643:Fucose / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D011485:Protein Binding
D000373:Agglutinins; D006023:Glycoproteins; D008565:Membrane Proteins; D005643:Fucose