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Blood, 1 March 2002, Vol. 99, No. 5, pp. 1785-1793
PHAGOCYTES
Secretion of heparin-binding protein from human neutrophils is
determined by its localization in azurophilic granules and
secretory vesicles
Hans Tapper,
Anna Karlsson,
Matthias Mörgelin,
Hans Flodgaard, and
Heiko Herwald
From the Department of Cell and Molecular Biology, Lund
University, Sweden; the Department of Medical Microbiology and
Immunology, Göteborg University, Sweden; and Leukotech A/S,
Copenhagen, Denmark.
Human neutrophils have an important role in host defense against
microbial infection. At different stages of an infectious process,
neutrophils progressively up-regulate receptors and release various
effector molecules. These are stored in several distinct types of
granules with varying propensity to be secreted. Heparin-binding protein (HBP), also known as CAP37 or azurocidin, is a multifunctional, inactive serine-protease homologue. The present work shows that HBP is
released from neutrophils on stimulation with secretagogues that do not
trigger the secretion of azurophilic granule content. Therefore, the
subcellular localization of HBP was investigated in more detail.
Immunofluorescence microscopy revealed that HBP was localized close to
the plasma membrane. Further analysis by fractionation of postnuclear
supernatants from cavitated neutrophils showed that HBP is stored in
azurophilic granules and secretory vesicles but that it is also
detected to a minor extent in the plasma membrane. These findings were
confirmed by immunoelectron microscopy showing that HBP colocalized
with marker proteins of azurophilic granules and secretory vesicles.
The presence of HBP in secretory vesicles possibly depends on the stage
of cell differentiation, since the promyelocytic cell line HL-60
contains less HBP than mature neutrophils, stored exclusively in the
less easily mobilized azurophilic granules. Our findings suggest that
HBP can be synthesized or targeted to easily mobilized compartments at
a late stage of neutrophil maturation. The ability of neutrophils to
secrete HBP from secretory vesicles may be important for
proinflammatory functions of this protein, such as the alteration of
vascular permeability.
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