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Beta 2-integrin and L-selectin are obligatory receptors in neutrophil
aggregation [see comments]
SI Simon, YP Rochon, EB Lynam, CW Smith, DC Anderson and LA Sklar
Department of Pathology, University of New Mexico Cancer Center, School of
Medicine, Albuquerque.
We have recently found that antibodies to L-selectin, the homing receptor
on neutrophils, are as effective as those to beta 2-integrin at blocking
formyl peptide-stimulated aggregation. Therefore, we investigated the
requirements for expression of L-selectin and beta 2- integrin on adjacent
cells during aggregation. Fluorescence flow cytometry allowed
characterization of aggregates on the basis of size and color, as well as
antibody binding to these two adhesive molecules. Formyl peptide-stimulated
aggregate formation was measured for individual populations fluorescently
labeled red (LDS-751) or green (CD44-FITC), and interpopulation red-green
cell conjugates. Blocking either the beta 2-integrin or L-selectin adhesive
epitope with monoclonal antibody on individual cell populations resulted in
an approximately 50% reduction in two-color aggregation as compared with
that in unblocked samples. Shedding the L-selectin on a cell population by
preincubation with complexes of lipopolysaccharide and its plasma membrane
binding protein also decreased aggregation to a control population by
approximately 50%. We examined the aggregation of neutrophils from patients
genetically deficient in beta 2-integrin and clinically leukocyte adhesion
deficient (LAD). LAD adhesion to normal neutrophils was dependent on the
expression of L-selectin on LAD cells and beta 2-integrin on normal cells.
Thus, the minimum requirement for adhesion between two mixed populations of
neutrophils was that one population expressed the beta 2-integrin and the
other expressed the L- selectin adhesive epitope.
Volume 82,
Issue 4,
pp. 1097-1106,
08/15/1993
Copyright © 1993 by The American Society of Hematology
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