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Ultrastructural localization of the Charcot-Leyden crystal protein
(lysophospholipase) to a distinct crystalloid-free granule population in
mature human eosinophils
AM Dvorak, L Letourneau, GR Login, PF Weller and SJ Ackerman
Department of Pathology, Beth Israel Hospital, Boston, MA 02215.
The Charcot-Leyden crystal (CLC) protein is a unique constituent of
eosinophils and basophils. This protein forms the hexagonal bipyramidal
crystals observed in tissues at sites of eosinophil accumulations,
possesses lysophospholipase activity (lysolecithin acylhydrolase
E.C.3.1.1.5), and comprises an estimated 7% to 10% of total eosinophil
protein. The ultrastructural localization of CLC protein was studied in
mature peripheral blood eosinophils from normal donors and from patients
with the idiopathic hypereosinophilic syndrome. Subcellular localization
was evaluated by immunoelectron microscopy using eosinophils, both from
buffy coat and purified cell suspensions, that were fixed by a variety of
methods. Immunochemical detection of CLC protein employed rabbit antiserum
to eosinophil CLC protein, affinity chromatography-purified monospecific
IgG antibodies, and postembedding immunogold techniques. Controls for
specificity included (1) omission of the primary antibody to CLC protein
and (2) substitution of primary antibody with a nonimmune preimmunization
serum, a protein A-purified nonimmune IgG, or a protein A-purified
nonreactive IgG prepared from solid-phase CLC protein-Sepharose-absorbed
anti-CLC antiserum. CLC protein was localized to a minor (approximately 5%)
subpopulation of eosinophil granules. These membrane-bound cytoplasmic
granules were large (greater than 0.5 mu), were devoid of crystalloid
inclusions, and were morphologically compatible with persisting eosinophil
primary granules. The crystalloid-containing, large, specific granules did
not stain for CLC protein. Insufficient numbers of small dense granules,
lipid bodies, and vesiculotubular structures were present to adequately
evaluate their potential as additional sites for the subcellular
localization of CLC protein. The cellular specificity of the immunogold
localization of CLC protein in the eosinophil was affirmed by the absence
of staining in neutrophils and lymphocytes present in the same sections.
The ultrastructural immunogold localization of CLC protein
(lysophospholipase) to a large, crystalloid-free granule in mature
circulating eosinophils supports the persistence of a distinct "primary"
granule population that serves as a major intracytoplasmic repository for
this enzyme.
Volume 72,
Issue 1,
pp. 150-158,
07/01/1988
Copyright © 1988 by The American Society of Hematology
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