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Human Eosinophils Express, Relative to Other Circulating
Leukocytes, Large Amounts of Secretory 14-kD
Phospholipase A2
M. Blom,
A.T.J. Tool,
P.C. Wever,
G.J. Wolbink,
M.C. Brouwer,
J. Calafat,
A. Egesten,
E.F. Knol,
C.E. Hack,
D. Roos, and
A.J. Verhoeven
From the Central Laboratory of the Netherlands Red Cross Blood
Transfusion Service and Laboratory of Experimental and Clinical
Immunology, Academic Medical Center, University of Amsterdam,
Amsterdam, The Netherlands; the Clinical and Laboratory Immunology
Unit, Department of Internal Medicine, Academic Medical Center,
University of Amsterdam, Amsterdam, The Netherlands; the Netherlands
Cancer Institute, Amsterdam, The Netherlands; and the Division of
Hematology, Department of Medicine, Lund Hospital, Lund, Sweden.
Human eosinophils perform several functions dependent on
phospholipase A2 (PLA2) activity, most notably
the synthesis of platelet-activating factor (PAF) and leukotriene
C4 (LTC4). Several forms of PLA2 have been identified in mammalian cells. In the present study, the
14-kD, secretory form of PLA2 was detected in human
eosinophils by immunocytochemical staining with the specific monoclonal
antibody (MoAb) 4A1. In contrast, preparations of neutrophils,
monocytes, lymphocytes, and basophils did not show detectable staining.
With two MoAbs in a sandwich enzyme-linked immunosorbent assay (ELISA), large amounts of sPLA2 were detected in lysates of
eosinophils, that were 20-fold to 100-fold higher than in the other
circulating leukocytes (ie, neutrophils, basophils, monocytes, and
lymphocytes). In addition, with a commercially available
sPLA2 activity assay kit, we were able to show high
activity of sPLA2 in human eosinophils relative to
neutrophils. Investigations at the ultrastructural level showed that
sPLA2 in eosinophils is mainly located in specific granules. Immunoelectron microscopy also visualized sPLA2
within phagosomes after addition of opsonized particles to the
eosinophils. However, sPLA2 was not detected in the
cell-free supernatants of activated eosinophils, in contrast to
eosinophil-cationic protein (ECP), which colocalizes with
sPLA2 in resting eosinophils. These findings warrant
further studies into the role of sPLA2 in eosinophil function.
Blood, Vol. 91 No. 8 (April 15), 1998:
pp. 3037-3043
© 1998 by The American Society of Hematology.
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