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RIII (CD16) and Its Mobilization by Chemoattractants in Human Eosinophils1
Section of Pulmonary and Critical Care Medicine, Department of Medicine, and Departments of Pharmacological and Physiological Sciences, Pediatrics, Anesthesia, and Critical Care, and Committees on Clinical Pharmacology and Cell Physiology, Division of Biological Sciences, University of Chicago, Chicago, IL 60637
We characterized the existence, translocation, and reabsorption
during cellular activation of a constitutively expressed intracellular
CD16 in the human eosinophil. By two-color flow cytometry, we showed
that 6.5 ± 0.3% of nonpurified eosinophils expressed surface
CD16. After digestion with phosphotidylinositol-specific phospholipase
C, surface CD16 on both neutrophils and eosinophils decreased
substantially, suggesting that eosinophil CD16 is a
glycosyl-phosphatidylinositol-linked isoform. However, CD16 was
substantially expressed intracellularly in human eosinophils.
Epitope-specific binding to CLB-gran11 mAb from non-NA2/NA2 donors
demonstrated that intracellular eosinophil CD16 also differed from the
transmembrane isoform of CD16 expressed on NK cells or macrophages.
Western blot analysis performed with 3G8 or DJ130c mAb showed a broad
band at 
65 to 80 kDa, which was the same as neutrophil CD16 from the
same NA2/NA2 donors. Upon stimulation by chemoattractants C5a, FMLP, or
platelet-activating-factor, eosinophilic intracellular CD16 was rapidly
translocated to the eosinophil surface, expressed maximally at 30
s, and then gradually disappeared from the cell surface during the next
10 min. Intracellular flow cytometry of stimulated eosinophils and
sandwich ELISA of stimulated eosinophil supernatants demonstrated that
the disappearance was due to its rapid release into medium and
reabsorption by the cells. Our data identify a CD16B that is
consistently expressed intracellularly but only rarely on the surface
of nonactivated human eosinophils. This CD16 is transiently expressed
during stimulation by chemoattractants.
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