Open AccessEvidence of Glycosylated Sites on the Endothelin-1 Receptor in Swiss 3T3 Cells
Author(s) -
Pierre Devesly,
Christina Cade,
Mark A. Polokoff,
L Botelho
Publication year - 1991
Publication title -
journal of cardiovascular pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.762
H-Index - 100
eISSN - 1533-4023
pISSN - 0160-2446
DOI - 10.1097/00005344-199100177-00036
Subject(s) - wheat germ agglutinin , soybean agglutinin , concanavalin a , agglutinin , peanut agglutinin , lectin , biology , receptor , biochemistry , microbiology and biotechnology , monosaccharide , in vitro
The effects of incubation of intact cells with six different lectins on the specific binding of [125I]endothelin-1 (ET-1) were determined in Swiss 3T3 fibroblasts. ET-1 binding was unaffected by pretreatment of cells for 1 h at 37 degrees C with concanavalin A, soybean agglutinin, Ulex europaeus agglutinin I, peanut agglutinin, or Galanthus nivalis agglutinin. However, preincubation of cells with 300 micrograms/ml of wheat germ agglutinin resulted in a 70% decrease in specific binding of ET-1 to cell-surface receptors. The inhibitory effects of wheat germ agglutinin were diminished by brief incubation of lectin-treated cells with 100 mM N-acetylglucosamine, a monosaccharide specifically recognized by wheat germ agglutinin. Neither glucose nor mannose had any effect on wheat germ agglutinin-mediated inhibition of the specific binding of ET-1. These results suggest that the ET-1 receptor on 3T3 cells is a glycoprotein that contains one or more N-acetylglucosamine residues at or near the ligand binding site.