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Regulation and lectin activity of the human neutrophil peripheral lymph
node homing receptor
MA Jutila, TK Kishimoto and EC Butcher
Department of Pathology, Stanford University, CA.
We characterize the nature and regulation of a human neutrophil cell
surface antigen recognized by monoclonal antibodies (the DREG series)
against a human lymphocyte peripheral lymph node homing receptor. Human
neutrophils express high levels of the DREG antigen, whose expression is
downregulated after treatment with phorbol myristate acetate, or the
chemotactic factors C5a and FMLP. Interestingly, C5a treatment also
downregulated the monocyte DREG antigen, but had no effect on expression of
the lymphocyte molecule. Within 3 minutes after treatment with C5a, greater
than 80% of neutrophil DREG antigen expression is lost, and essentially the
molecule is completely removed from the cell surface by 5 minutes. The
human neutrophil DREG antigen is 10 Kd larger than the lymphocyte molecule.
These features are similar to those of the mouse neutrophil MEL-14 antigen
(murine peripheral lymph node homing receptor). The mannose-6-phosphate
rich phosphomannan (PPME) binds human lymphocytes via the DREG antigen.
PPME also binds neutrophils, but little difference in binding is seen
between unactivated and activated cells. We show that PPME binding to
unactivated neutrophils is mediated primarily by a cation- and DREG
antigen-dependent mechanism, whereas activated neutrophil-PPME binding is
DREG antigen- and cation-independent, and may be due to the translocation
of lysosomal mannose-6-phosphate receptors to the cell surface. The DREG
antibodies offer powerful tools for analyzing the role of homing receptors
in human neutrophil-endothelial cell interactions, and also may prove
valuable in the clinical assessment of neutrophil activation.
Volume 76,
Issue 1,
pp. 178-183,
07/01/1990
Copyright © 1990 by The American Society of Hematology
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