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J Biol Chem, Vol. 274, Issue 11, 7216-7225, March 12, 1999

Alternative Endocytic Pathway for Immunoglobulin A Fc Receptors (CD89) Depends on the Lack of FcRgamma Association and Protects against Degradation of Bound Ligand

Pierre LaunayDagger , Claire Patry§, Agnès LehuenDagger , Benoit PasquierDagger , Ulrich Blank, and Renato C. MonteiroDagger

From Dagger  INSERM, Unité 25, Hôpital Necker, 75743 Paris, § Unité Mixte de Recherche, Institut Curie/CNRS 144, 75005 Paris, and the  Unité d'Immunoallergie, Institut Pasteur, 75015 Paris, France

IgA is the most abundant immunoglobulin in mucosal areas but is only the second most common antibody isotype in serum because it is catabolized faster than IgG. IgA exists in monomeric and polymeric forms that function through receptors expressed on effector cells. Here, we show that IgA Fc receptor(s) (Fcalpha R) are expressed with or without the gamma  chain on monocytes and neutrophils. gamma -less Fcalpha R represent a significant fraction of surface Fcalpha R molecules even on cells overexpressing the gamma  chain. The Fcalpha R-gamma 2 association is up-regulated by phorbol esters and interferon-gamma . To characterize gamma -less Fcalpha R functionally, we generated mast cell transfectants expressing wild-type human Fcalpha R or a receptor with a point mutation (Arg right-arrow Leu at position 209) which was unable to associate with the gamma  chain. Mutant gamma -less Fcalpha R bound monomeric and polymeric human IgA1 or IgA2 but failed to induce exocytosis after receptor clustering. The two types of transfectant showed similar kinetics of Fcalpha R-mediated endocytosis; however, the endocytosis pathways of the two types of receptor differed. Whereas mutant Fcalpha R were localized mainly in early endosomes, those containing Fcalpha R-gamma 2 were found in endo-lysosomal compartments. Mutant gamma -less Fcalpha R recycled the internalized IgA toward the cell surface and protected against IgA degradation. Cells expressing the two forms of Fcalpha R, associated or unassociated with gamma  chains, may thus have differential functions either by degrading IgA antibody complexes or by recycling serum IgA.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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