Interleukin 39: a new member of interleukin 12 family

Abstract

interleukin (iL)-12 family member is a heterodimer glycoprotein, composed of two covalently linked subunits, α and β chains. The α subunit consists of iL-23p19, iL-27p28, and iL-12p35, and the β subunit includes iL-12p40 and epstein-Barr virus-induced gene (ebi3). iL-39 is a new heterodimeric iL-12 family member composed of iL-23p19 and ebi3 subunits. iL-39 is secreted by lipopolysaccharide-stimulated B cells. other immune cells, such as dendritic cells and macrophages, express iL-39 mRna. in lupus-like mice, gL7+B cells and cD138+plasma cells are highly activated and widely expressed, promoting high expression of iL-39. iL-39 mediates inflammatory responses through binding to a heterodimer of iL-23R/gp130 receptor and activation of signal transducer and activator of transcription (STaT)1/STaT3 signal molecules. The serum levels of iL-39 were significantly increased in patients with acute coronary syndrome compared with patients with normal coronary arteries. This review discusses the biological characteristics, receptor, and signal pathway as well as biological activity of iL-39 and its potential role in inflammation and other diseases.