Thornberry N A, Bull H G, Calaycay J R, Chapman K T, Howard A D, Kostura M J, Miller D K, Molineaux S M, Weidner J R, Aunins J
Department of Biochemistry, Merck Research Laboratories, Rahway, New Jersey 07065.
Nature. 1992 Apr 30;356(6372):768-74. doi: 10.1038/356768a0.
Interleukin-1 beta (IL-1 beta)-converting enzyme cleaves the IL-1 beta precursor to mature IL-1 beta, an important mediator of inflammation. The identification of the enzyme as a unique cysteine protease and the design of potent peptide aldehyde inhibitors are described. Purification and cloning of the complementary DNA indicates that IL-1 beta-converting enzyme is composed of two nonidentical subunits that are derived from a single proenzyme, possibly by autoproteolysis. Selective inhibition of the enzyme in human blood monocytes blocks production of mature IL-1 beta, indicating that it is a potential therapeutic target.
白细胞介素-1β（IL-1β）转换酶将IL-1β前体切割成成熟的IL-1β，后者是炎症的重要介质。本文描述了该酶作为一种独特的半胱氨酸蛋白酶的鉴定以及强效肽醛抑制剂的设计。互补DNA的纯化和克隆表明，IL-1β转换酶由两个不同的亚基组成，这两个亚基可能来自单一的酶原，可能是通过自身蛋白水解作用产生的。在人血单核细胞中对该酶的选择性抑制可阻断成熟IL-1β的产生，表明它是一个潜在的治疗靶点。
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