Bhattacharya Sujoy, Guo Huazhang, Ray Ramesh M, Johnson Leonard R
Department of Physiology, University of Tennessee Health Science Center, Memphis, TN 38163, USA.
Biochem J. 2007 Oct 15;407(2):243-54. doi: 10.1042/BJ20070293.
Inhibition of ornithine decarboxylase by DFMO (alpha-difluromethylornithine) and subsequent polyamine depletion increases p21Cip1 protein, induces cell cycle arrest and confers resistance to apoptosis on intestinal epithelial cells. However, the mechanism by which polyamines regulate p21Cip1 expression and apoptosis is unknown. On the basis of the involvement of p21Cip1 as an anti-apoptotic protein, we tested the role of p21Cip1 in providing protection from apoptosis. Simultaneously, we investigated the role of E47, a basic helix-loop-helix protein, in the regulation of p21Cip1 gene transcription. Gene-specific siRNA (small interfering RNA) decreased E47 protein levels, increased p21Cip1 promoter activity and protein levels and protected cells from TNFalpha (tumour necrosis factor alpha)-induced apoptosis. Knockdown of p21Cip1 protein by siRNA resulted in cells becoming more susceptible to apoptosis. In contrast, incubation with EGF (epidermal growth factor) stimulated p21Cip1 mRNA and protein levels and rescued cells from apoptosis. During apoptosis, the level of E47 mRNA increased, causing a concomitant decrease in p21Cip1 mRNA and protein levels. Polyamine depletion decreased E47 mRNA levels and cell survival. Caspase 3-mediated cleavage of p130Cas has been implicated in p21Cip1 transcription. The progression of apoptosis led to a caspase 3-dependent cleavage of p130Cas and generated a 31 kDa fragment, which translocated to the nucleus, associated with nuclear E47 and inhibited p21Cip1 transcription. Polyamine depletion inhibited all these effects. Transient expression of the 31 kDa fragment prevented the expression of p21Cip1 protein and increased apoptosis. These results implicate p21Cip1 as an anti-apoptotic protein and suggest a role for polyamines in the regulation of p21Cip1 via the transcription repressor E47. Caspase-mediated cleavage of p130Cas generates a 31 kDa fragment, inhibits p21Cip1 transcription and acts as an amplifier of apoptotic signalling.
DFMO(α-二氟甲基鸟氨酸)对鸟氨酸脱羧酶的抑制作用以及随后的多胺耗竭会增加p21Cip1蛋白水平,诱导细胞周期停滞,并赋予肠上皮细胞抗凋亡能力。然而,多胺调节p21Cip1表达和凋亡的机制尚不清楚。基于p21Cip1作为一种抗凋亡蛋白的作用,我们测试了p21Cip1在提供抗凋亡保护中的作用。同时,我们研究了一种碱性螺旋-环-螺旋蛋白E47在p21Cip1基因转录调控中的作用。基因特异性小干扰RNA(siRNA)降低了E47蛋白水平,增加了p21Cip1启动子活性和蛋白水平,并保护细胞免受肿瘤坏死因子α(TNFα)诱导的凋亡。用siRNA敲低p21Cip1蛋白会使细胞对凋亡更敏感。相反,用表皮生长因子(EGF)孵育会刺激p21Cip1 mRNA和蛋白水平,并使细胞免于凋亡。在凋亡过程中,E47 mRNA水平升高,导致p21Cip1 mRNA和蛋白水平随之降低。多胺耗竭降低了E47 mRNA水平和细胞存活率。半胱天冬酶3介导的p130Cas裂解与p21Cip1转录有关。凋亡进程导致p130Cas发生半胱天冬酶3依赖性裂解,并产生一个31 kDa的片段,该片段易位至细胞核,与核内E47结合并抑制p21Cip1转录。多胺耗竭抑制了所有这些效应。31 kDa片段的瞬时表达阻止了p21Cip1蛋白的表达并增加了凋亡。这些结果表明p21Cip1是一种抗凋亡蛋白,并提示多胺通过转录抑制因子E47在p21Cip1的调控中发挥作用。半胱天冬酶介导的p130Cas裂解产生一个31 kDa的片段,抑制p21Cip1转录并作为凋亡信号的放大器。