Interleukin-10 is localized to and released by human lung mast cells.

Abstract

Mast cells control the local inflammation by producing many kinds of cytokines. Interleukin (IL)-10 is one of the important cytokine that upregulate or downregulate inflammation. The aim of this study is to ascertain whether IL-10 is produced from human lung mast cells by cross-linkage of high-affinity Fcepsilon receptors (FcepsilonRI). Mast cells were purified using affinity magnetic selection with mAb YB5.B8 (> 93% pure). Mast cells were precultured with human myeloma IgE (3 microg/mL) for 16 h and then washed, and stimulated with anti-IgE in the presence or absence of recombinant human stem cell factor (rhSCF). We have studied the production of IL-10 by using reverse transcription-PCR, enzyme-linked immunosorbent assay and immunocytochemistry. We found that human lung mast cells were immunocytochemically stained with anti-IL-10 mAb after IgE-dependent stimulation. The activation of mast cells via FcepsilonRI enhanced the intensity of the IL-10 mRNA signal. Anti-IgE (1 microg/mL) induced a median IL-10 release of 301.7 (7.8-1532.4) pg/106 mast cells/24 h. In contrast, mast cells released only a small amount of IL-10 in the absence of anti-IgE. This difference was statistically significant (P = 0.02, n = 11). Our findings indicate that human lung mast cells are capable of producing IL-10 in response to IgE-dependent stimulation.