Journal of Leukocyte Biology
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Originally published online as doi:10.1189/jlb.0207112 on June 18, 2007

Published online before print June 18, 2007
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(Journal of Leukocyte Biology. 2007;82:551-558.)
© 2007 by Society for Leukocyte Biology

Intracellular pools of Fc{alpha}R (CD89) in human neutrophils are localized in tertiary granules and secretory vesicles, and two Fc{alpha}R isoforms are found in tertiary granules

Na Yin, Min Peng, Yukun Xing and Wei Zhang1

Institute of Basic Medical Sciences Chinese Academy of Medical Sciences, School of Basic Medicine Peking Union Medical College, Beijing, China

1 Correspondence: Department of Immunology, Institute of Basic Medical Sciences, 5 Dong Dan San Tiao, Beijing 100005, China. E-mail: wzhang{at}pumc.edu.cn

The human Fc{alpha}RI (CD89) is expressed on cells of myeloid lineage and plays an important role in host defense. Neutrophils make up the majority of Fc{alpha}RI-positive cells. Previous reports suggested that Fc{alpha}R was stored in neutrophil intracellular pools, and it could be mobilized quickly once neutrophils were activated. However, the subcellular localization of Fc{alpha}R in neutrophils has not been defined yet. In this study, we identified that Fc{alpha}R was stored in secretory vesicles and tertiary granules of neutrophils by flow cytometry analysis, ELISA, confocal microscopy, and Western blotting. The molecular mass of Fc{alpha}R in secretory vesicles was different from that in tertiary granules. Fc{alpha}R stored in tertiary granules had a molecular mass of 50–70 kDa, whereas Fc{alpha}R in secretory vesicles and membranes had a molecular mass of 55–75 kDa. After treatment by peptide-N-glycosidase F, an enzyme that removes N-glycosylation, Fc{alpha}R from secretory vesicles and tertiary granules revealed a core protein of 32 kDa, which was the same as the backbone of full length of Fc{alpha}R. A smaller Fc{alpha}R variant with a core protein of 29–30 kDa was found in tertiary granules but not in secretory vesicles. The nature of the small variant is not clear at present and remains to be investigated further.

Key Words: IgA receptor • PMN • gelatinase • alternative splicing






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