Cartier Jessy, Marivin Arthur, Berthelet Jean, Dubrez Laurence
Inserm UMR 866, Faculté de Médecine, Université de Bourgogne, 7, Boulevard Jeanne d'Arc, 21079 Dijon Cedex, France.
Med Sci (Paris). 2012 Jan;28(1):69-75. doi: 10.1051/medsci/2012281019. Epub 2012 Jan 27.
The function of IAP has long been limited to an inhibition of apoptosis through their capacity to bind some caspases. Since the expression of these proteins is altered in some tumor samples, IAPs are targets for anticancer therapy and many small molecules have been designed for their capacity to inhibit IAP-caspase interaction. Unexpectedly, these molecules appeared to significantly affect NF-κB activation. In this review, we will discuss the central role of cIAP1, cIAP2 and XIAP in the regulation of NF-κB activating signaling pathways.
长期以来,凋亡抑制蛋白(IAP)的功能一直局限于通过其与某些半胱天冬酶结合的能力来抑制细胞凋亡。由于这些蛋白质的表达在一些肿瘤样本中发生了改变,IAP成为抗癌治疗的靶点,并且已经设计出许多小分子来抑制IAP-半胱天冬酶的相互作用。出乎意料的是,这些分子似乎显著影响核因子κB(NF-κB)的激活。在这篇综述中,我们将讨论细胞IAP1、细胞IAP2和X连锁IAP(XIAP)在调节NF-κB激活信号通路中的核心作用。