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  • Title: Wheat germ agglutinin specifically inhibits formyl peptide-induced polymorphonuclear leukocyte chemotaxis.
    Author: Perez HD, Ong R, Khanna K, Banda D, Goldstein IM.
    Journal: J Immunol; 1982 Dec; 129(6):2718-24. PubMed ID: 6897258.
    Abstract:
    Evidence that surface membrane glycoproteins of polymorphonuclear leukocytes (PMN) are involved in stimulus-response coupling prompted us to examine effects on these cells of various plant lectins. We have found that wheat germ agglutinin (WGA) (1.0 microgram/ml) completely, specifically, and irreversibly inhibits directed migration (chemotaxis) of human PMN toward the synthetic peptide, N-formylmethionyl-leucyl-phenylalanine (FMLP) (0.1 to 100 nM). This effect of WGA was not shared by subagglutinating concentrations of either concanavalin A or Bandeirea simplicifolia lectin. In contrast to its effects on FMLP-induced chemotaxis, WGA did not influence other FMLP-induced PMN responses (i.e., selective discharge of lysosomal enzymes from cytochalasin B-treated cells, generation of superoxide anion radical(s). WGA also did not influence PMN chemotactic responses to either the complement-derived peptide, C5a, or the lipoxygenase product, leukotriene B4. Inhibition of FMLP-induced chemotaxis by WGA was not reversed by washing WGA-treated cells, but was reversed (and prevented) by N-acetyl-D-glucosamine (not by N-acetyl-D-galactosamine or mannosamine). WGA did not affect either orientation or stimulated random motility of PMN, and did not interfere with specific binding to PMN of (3H)-FMLP. A derivative of WGA with 10-fold less agglutinating activity for human erythrocytes was prepared by treating the native lectin with cyanogen bromide and formic acid. The derivative also inhibited FMLP-induced PMN chemotaxis specifically and selectively. These data suggest that WGA specifically inhibits FMLP-induced PMN chemotaxis by attaching to N-acetyl-D-glucosamine residues at a locus on the PMN plasma membrane that is distinct from the binding site of the FMLP receptor.
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