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Ultrastructural localization of lactoferrin and myeloperoxidase in human
neutrophils by immunogold
E Cramer, KB Pryzwansky, JL Villeval, U Testa and J Breton-Gorius
Colloidal gold was used as a marker for immunoelectron microscopy to
localize lactoferrin (LF) and myeloperoxidase (MPO) in human peripheral
blood neutrophils. Cells were reacted with monospecific antibodies against
LF or MPO and then with gold-labeled antiglobulin. MPO cytochemistry was
also associated with immunologic detection of LF. Immunologic labeling of
thin sections after embedding in glycol methacrylate gave good
ultrastructural morphology and specific localization of both proteins. MPO
was detected in the large azurophil granules, whereas LF was consistently
localized in the matrix of another population of morphologically distinct
granules, smaller and more numerous than azurophil granules. When
cytochemical detection of MPO was coupled with immunologic detection of LF,
LF was observed in the population of MPO-negative granules, which were
identified as specific. This was confirmed on cells that were permeabilized
with saponin and stained for LF and MPO before embedding. No other
neutrophil organelles displayed labeling for LF; other blood cells also
were unreactive for LF. In the bone marrow, myeloblast and promyelocyte
granulations were not stained and LF-containing granules appeared at the
myelocyte stage. In conclusion, we confirm previous biochemical and light
microscopic studies by ultrastructural demonstration of LF and MPO in two
categories of granules, the specific and azurophil granules, respectively.
The method described in this article avoids disruption caused by cell
fractionation procedures. In the future, other intragranular proteins can
be localized by a similar approach.
Volume 65,
Issue 2,
pp. 423-432,
02/01/1985
Copyright © 1985 by The American Society of Hematology
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