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RI/CD89) Triggers FcR 
-Chain-Dependent Shedding of Soluble CD891
,
*
Department of Nephrology, Leiden University Medical Center, Leiden, The Netherlands; and
Department of Immunology and
Medarex Europe, University Medical Center Utrecht, Utrecht, The Netherlands
CD89/Fc
RI is a 55- to 75-kDa type I receptor glycoprotein,
expressed on myeloid cells, with important immune effector functions.
At present, no information is available on the existence of soluble
forms of this receptor. We developed an ELISA for the detection of
soluble CD89 (sCD89) forms and investigated the regulation of sCD89
production. PMA/ionomycin stimulation of monocytic cell lines (U937,
THP-1, and MM6), but not of neutrophils, resulted in release of sCD89.
Crosslinking of CD89 either via its ligand IgA or with anti-CD89
mAbs similarly resulted in sCD89 release. Using CD89-transfected cells,
we showed ligand-induced shedding to be dependent on coexpression of
the FcR 
-chain subunit. Shedding of sCD89 was dependent on signaling
via the -chain and prevented by addition of inhibitors of protein
kinase C (staurosporine) or protein tyrosine kinases (genistein).
Western blotting revealed sCD89 to have an apparent molecular mass of
30 kDa and to bind IgA in a dose-dependent fashion. In conclusion, the
present data document a ligand-binding soluble form of CD89 that is
released upon activation of CD89-expressing cells. Shedding of CD89 may
play a role in fine-tuning CD89 immune effector
functions.
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