摘要: Interleukin (IL)-lα and IL-1β are produced by two different genes share 26% amino acid homology. Both forms synthesized as 31 kDa precursor peptides (pro-IL-lα pro-IL-1β), which specifically cleaved to generate 17 proteins for mature IL-lα IL-1β. is primarily macrophages secreted after cleavage of its proform IL-1β-convertase enzyme (ICE, also termed caspase 1). In addition, other enzymes in the absence ICE can process pro-IL-1β [1, 2]. without a hydrophobic leader peptide thus does not follow typical secretion pathway. Recently it has become apparent that be either through exocytosis endoplasmic vesicles or rapidly released microvesicles budding off cell membrane [3, 4]. contrast, expressed intracellular membrane-bound protein human. An important distinction between these molecules biologically inactive, whereas both pro-IL-lα exhibit full receptor binding activity. biologic effects following binding, exerts functions inside cells [5-7].