Identification of the major lectin-binding surface proteins of human
neutrophils and alveolar macrophages
NP Christiansen and KM Skubitz
Department of Medicine, University of Minnesota Medical School,
Minneapolis.
Concanavalin A (Con A) and wheat germ agglutinin (WGA) are frequently used
as stimuli of neutrophils and macrophages. While the effects of these
lectins on cell function are presumably mediated by interaction with
cell-surface molecules, the target structures on the cell surface involved
are not well defined. We have used the techniques of lactoperoxidase
catalyzed cell-surface iodination, lectin affinity chromatography,
monoclonal antibody immunoprecipitation, and NaDodSO4- polyacrylamide gel
electrophoresis to study the surface proteins of human neutrophils and
alveolar macrophages that react with six lectins including Con A and WGA.
We found that several major surface-labeled proteins of neutrophils bound
Con A. Four of these proteins were identified by immunoprecipitation as
members of the LFA-1/HMac- 1/gp150,95 adhesion glycoprotein family. Con A
also bound CR1 and a 135- kd surface-labeled protein recognized by CD15
monoclonal antibodies. WGA also bound many of these proteins, but had a
much lower avidity for CR1. All three of the major surface-labeled proteins
of human alveolar macrophages bound to Con A, including the 183-kd mannose
receptor and the 30-kd smoking-associated protein. WGA also bound the
183-kd macrophage protein, but not the 30-kd protein. These results should
aid the understanding of studies using these lectins as stimuli.
Volume 71,
Issue 6,
pp. 1624-1632,
06/01/1988
Copyright © 1988 by The American Society of Hematology
