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J Biol Chem, Vol. 274, Issue 11, 7216-7225, March 12, 1999
From 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) (Fc
Alternative Endocytic Pathway for Immunoglobulin A Fc Receptors
(CD89) Depends on the Lack of FcR
Association and Protects against
Degradation of Bound Ligand
,
,
,
INSERM,
R) are
expressed with or without the
chain on monocytes and neutrophils.
-less Fc
R represent a significant fraction of surface Fc
R
molecules even on cells overexpressing the
chain. The Fc
R-
2
association is up-regulated by phorbol esters and interferon-
. To
characterize
-less Fc
R functionally, we generated mast cell
transfectants expressing wild-type human Fc
R or a receptor with a
point mutation (Arg
Leu at position 209) which was unable to
associate with the
chain. Mutant
-less Fc
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 Fc
R-mediated endocytosis; however, the endocytosis
pathways of the two types of receptor differed. Whereas mutant Fc
R
were localized mainly in early endosomes, those containing Fc
R-
2 were found in endo-lysosomal compartments. Mutant
-less Fc
R recycled the internalized IgA toward the cell surface and protected against IgA degradation. Cells expressing the two forms of Fc
R, associated or unassociated with
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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