Molecular Mechanisms for Regulation of the Human High-Affinity IgE Receptor beta Subunit (FcepsilonRIbeta) Gene Expression

摘要

Background: FcepsilonRI is a key molecule for mast cell activation in allergic reactions, consisting of three subunits, one alpha, one beta, and a homodimer of gamma. There has recently been some focus on the beta-chain as a dualfunctional (positive/negative) signal regulator based on the unique beta-chain ITAM (immunore-ceptor tyrosine-based activation motif), which contains two canonical, and one noncanonical tyrosine residues. Therefore, we considered that elucidation of regulatory mechanisms of the p-chain gene expression would make a meaningful contribution to research on the manipulation of allergic reaction. Genomic DNA fragments of the human FcepsilonRI beta-chain gene were tested for their transcriptional regulatory activities employing a reporter assay with luciferase activity. To identify factors constituting the complex with myeloid zinc finger/four and a half LIM-only protein 3 (MZF-1/FHL3), yeast three-hybrid screening assay was performed. To elucidate that nuclear transcription factor YC (NFYC) and histone deacetylase (HDAC) interact with the beta-chain gene, chromatin immunoprecipitation (ChIP) assay was employed.