Functional expression of the high affinity receptor for IgE (FcepsilonRI) in human platelets and its' intracellular expression in human megakaryocytes.

The high affinity IgE receptor (FcepsilonRI) expressed on the cell surface of mast cells and basophils is the key molecule in triggering the IgE-mediated allergic reaction. Recently, it was elucidated that the FcepsilonRI is expressed on a variety of other cells like Langerhans cells, monocytes, and eosinophils, and the functional importance of the FcepsilonRI expression in Langerhans cells was also shown. Some studies suggest that human platelets may play important roles in allergic inflammation through the cell-surface expression of the FcepsilonRII and FcgammaRII. Here, we report that human platelets and megakaryocytes constitutively express the messenger RNA and protein for the FcepsilonRI. Although the FcepsilonRI is expressed on the cell surface of human platelets, it is only detected in the cytoplasm of human megakaryocytes. We also confirmed that human platelets express the genes for the alpha, beta, and gamma chains of the FcepsilonRI without any defined mutations. Furthermore, stimulation of human platelets via the FcepsilonRI induced the release of serotonin and RANTES (Regulated on Activation, Normal T Expressed, and presumably Secreted). Taken together, these results suggest a novel and important role for human platelets in perpetuating allergic inflammation through the expression of and activation via the FcepsilonRI.