Expression and Function of FcγR in Mouse Mast Cells

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Abstract
Activation of mast cells for the release of secretory granule, membrane lipid, and cytokine mediators via FcγR requires cell surface expression of FcγRIII. A soluble factor(s) from fibroblasts up-regulates the surface expression of FcγRIII in interleukin-3-dependent, bone-marrow-derived mast cells, which otherwise degrade FcγRIII intracellularly. Using a receptor-specific rabbit polyclonal antibody made to a peptide from the cytoplasmic domain of FcγRIIIα chain, we show that steady-state levels of FcγRIIIα protein increase in bone-marrow-derived mast cells after coculture with fibroblasts. Thus, the posttranslational stability of this functionally relevant receptor in mast cells is probably regulated by a fibroblast-derived cytokine(s).

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