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A more recent version of this article appeared on September 1, 2007

Published online before print June 18, 2007
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© by The Society for Leukocyte Biology
Journal of Leukocyte Biology, doi:10.1189/jlb.0207112

Received for publication February 15, 2007.
Revised May 17, 2007.
Accepted for publication May 20, 2007.

Article

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 Zhang @

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

@ To whom correspondence should be addressed. E-mail: wzhang{at}pumc.edu.cn.


  Abstract

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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Copyright © 2007 by the Society for Leukocyte Biology.