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Aberrant capping of membrane proteins on neutrophils from patients with
leukocyte adhesion deficiency
AL Kindzelskii, W Xue, RF Todd , LA Boxer and HR Petty
Department of Biological Sciences, Wayne State University, Detroit, MI
48202.
Several functional defects have been found in neutrophils from leukocyte
adhesion deficiency (LAD) patients who fail to express the CD11/CD18
leukoadhesins: Mo1, LFA-1, and p150,95. To better understand the functional
defects of LAD neutrophils, we have performed capping experiments. Purified
normal or LAD neutrophils were labeled with fluorochrome-conjugated
concanavalin A (Con A) or F(ab')2 fragments of antiurokinase-type
plasminogen activator receptor (uPAR), anti-Fc gamma RIII (CD16), anti-Mo5,
and anti-CD14 antibodies. F(ab')2-labeled cells were capped using a
second-step F(ab')2 fragment of an antimurine Fab antiserum. Cells were
capped for 30 minutes at 37 degrees C, then observed by fluorescence
microscopy. LAD neutrophils were found to be deficient in capping, but not
clustering of all of the reagents tested to date. The percent of cells
exhibiting capping of Con A, Fc gamma RIII, urokinase receptor, CD14, and
Mo5 were 52%, 67%, 70%, 25%, and 64% for normal neutrophils but were only
10%, 5%, 2%, 3%, and 1%, respectively, for LAD neutrophils. Capping of this
panel of membrane components in LAD or normal neutrophils was not augmented
by the addition of either 10(-5) mol/L colchicine or 10(-7) mol/L FMLP.
Because capping requires membrane-to-cytosol communication and an intact
microfilament linkage, we suggest that leukoadhesins may play a broad role
in promoting the redistribution of membrane components including
adherence-related receptors such as Fc gamma RIII and the urokinase
receptor.
Volume 83,
Issue 6,
pp. 1650-1655,
03/15/1994
Copyright © 1994 by The American Society of Hematology
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