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Simultaneous mobilization of Mac-1 (CD11b/CD18) and formyl peptide
chemoattractant receptors in human neutrophils [published erratum appears
in Blood 1993 Mar 15;81(6):1668]
V Graves, T Gabig, L McCarthy, EF Strour, T Leemhuis and D English
Bone Marrow Transplantation Laboratory, Methodist Hospital of Indiana,
Indianapolis 46202.
Mobilization of a distinct subset of specific granules provides a
physiologically important mechanism to recruit Mac-1 (CD11b/CD18) from an
intracellular pool to the external surface of the neutrophil plasma
membrane, where the functionally active heterodimer mediates several
adherence-dependent processes that are crucial for adequate host defense
and cellular inflammatory responses. We observed similar characteristics
for translocation of Mac-1 and neutrophil formyl peptide receptors (FPR)
and hypothesize that the readily accessible pools of both Mac-1 and FPR are
colocalized within this specific granule subset. Plasma membrane levels of
both FPR (assessed with 3H- FMLP) and Mac-1 (assessed by
fluorescence-activated cell sorter analysis of fluorescein isothiocyanate
[FITC]-Mo-1-labeled cells) were markedly downregulated in cells prepared at
low temperature from blood cooled to 4 degrees C immediately after removal
from the circulation. Levels of both FPR and Mac-1 remained low on cells
held at 4 degrees C. Upon warming, spontaneous upregulation of Mac-1 and
FPR occurred with similar kinetics and temperature dependency.
Translocation of both Mac- 1 and FPR was markedly potentiated by exposure
of cells to either fluoride ion (which has been shown by others to
specifically elicit exocytosis of gelatinase-rich and vitamin B-12 binding
protein-poor granules) or granulocyte-macrophage colony-stimulating factor
(GM-CSF), a cytokine that markedly potentiates the neutrophils' host
defense capabilities. Levels of both FPR and Mac-1 on F-- or GM-CSF-treated
neutrophils exceeded those present on cells incubated at 37 degrees C for
extended time intervals, indicating that stimulated translocation may
involve mobilization of an additional granule subset. Scatchard analysis
showed that only low-affinity FPR were translocated during spontaneous and
stimulus-dependent upregulation. To directly compare FPR levels on the
surface of cells displaying varying levels of Mac-1 within a single cell
suspension, cells were labeled with FITC-Mo-1 and sorted into
subpopulations based on fluorescence intensity. After sorting, the
individual populations were held at 4 degrees C to prevent further
spontaneous upregulation, concentrated by centrifugation, and assayed for
FPR levels. Under a variety of conditions, FPR levels correlated with Mac-1
(CD11b) expression on cell populations selected on the basis of CD11b
fluorescence intensity. Analysis of subcellular fractions obtained from
disrupted neutrophils before and after upregulation provided additional
support for the hypothesis that Mac-1 and FPR are colocalized within a
readily accessible subset of neutrophil granules.(ABSTRACT TRUNCATED AT 400
WORDS)
Volume 80,
Issue 3,
pp. 776-787,
08/01/1992
Copyright © 1992 by The American Society of Hematology
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