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The Journal of Immunology, 2002, 168: 1252-1258.
Copyright © 2002 by The American Association of Immunologists

Fc{alpha}RI/CD89 Circulates in Human Serum Covalently Linked to IgA in a Polymeric State1

Paul J. M. van der Boog*, Ger van Zandbergen*, Johan W. de Fijter*, Ngaisah Klar-Mohamad*, Anneke van Seggelen*, Per Brandtzaeg{dagger}, Mohamed R. Daha* and Cees van Kooten2,*

* Department of Nephrology, Leiden University Medical Center, Leiden, The Netherlands; and {dagger} Laboratory of Immunohistochemistry and Immunopathology, University of Oslo, Oslo, Norway

The FcR for IgA CD89/Fc{alpha}RI, is a type I receptor glycoprotein, expressed on myeloid cells, with important immune effector functions. In vitro CD89 can be released from CD89-expressing cells upon activation. Little information is available on the existence of this soluble molecule in vivo. Using specific and sensitive ELISA techniques (detection limit 50 pg/ml), we were not able to detect circulating CD89 in human sera. However, using Western blotting, a 30-kDa soluble CD89 molecule was demonstrated in both serum and plasma. Moreover, using a specific semiquantitative dot-blot system, we found CD89 in all human sera tested (mean concentration 1900 ng/ml). Size fractionation of human serum using gel filtration chromatography showed that the CD89 molecule was predominantly present in larger molecular mass fractions. Direct complexes between IgA and CD89 were demonstrated by anti-IgA affinity purification, and when analyzed under nonreducing conditions appeared to be covalently linked. Size fractionation of affinity-purified IgA showed the presence of soluble CD89 only in the high molecular mass fractions of IgA, but not in monomeric IgA. High molecular mass complexes of CD89-IgA could be distinguished from J chain containing dimeric IgA. These data show that CD89 circulates in complex with IgA, and suggest that CD89 might contribute to the formation of polymeric serum IgA.




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