Department of Clinical Sciences, Tufts Cummings School of Veterinary Medicine, Grafton, Massachusetts 01536, USA.
Am J Physiol Gastrointest Liver Physiol. 2011 Aug;301(2):G385-400. doi: 10.1152/ajpgi.00430.2010. Epub 2011 May 5.
Cholestatic liver disorders are accompanied by the hepatic accumulation of cytotoxic bile acids that induce cell death. Increases in cAMP protect hepatocytes from bile acid-induced apoptosis by a cAMP-guanine exchange factor (cAMP-GEF)/phosphoinositide-3-kinase (PI3K)/Akt pathway. The aim of these studies was to identify the downstream substrate in this pathway and to determine at what level in the apoptotic cascade cytoprotection occurs. Since inhibitory phosphorylation of glycogen synthase kinase-3 (GSK) occurs downstream of PI3K/Akt and this phosphorylation has been implicated in cell survival, we conducted studies to determine whether GSK was downstream in cAMP-GEF/PI3K/Akt-mediated cytoprotection. Our results show that treatment of hepatocytes with the cAMP-GEF-specific analog, 4-(4-chlorophenylthio)-2'-O-methyladenosine-3',5'-cAMP, results in PI3K-dependent phosphorylation of GSK. Direct chemical inhibition of GSK in rat hepatocytes or human HUH7-NTCP cells with several structurally and functionally distinct inhibitors including bromoindirubin-3'-oxime (BIO), maleimides (SB216763, SB415286), thiadiazolidine derivatives, and LiCl attenuates apoptosis induced by glycochenodeoxycholate (GCDC). In addition, genetic silencing of the GSK β isoform with small interfering RNA attenuates GCDC apoptosis in HUH7-NTCP cells. Adenoviral inhibition of the Rap1 blocks both cAMP-GEF-mediated cytoprotection against GCDC-induced apoptosis and Akt/GSK3β phosphorylation. GCDC-induced phosphorylation of the proapoptotic kinase, c-Jun NH(2)-terminal kinase (JNK) is inhibited by GSK inhibition or cAMP-GEF activation. GCDC-induced apoptosis is accompanied by phosphorylation of the endoplasmic reticulum stress markers pIEF2α and IRE-1, and pretreatment with the cAMP-GEF analog or GSK inhibitors prevents this phosphorylation. Collectively, our results support the presence of a cAMP/cAMP-GEF/Rap1/PI3K/Akt/GSKβ survival pathway in hepatocytes that inhibits bile acid-induced JNK phosphorylation.
胆汁淤积性肝病伴随着细胞毒性胆汁酸在肝脏中的积累,从而诱导细胞死亡。cAMP 的增加通过 cAMP-鸟嘌呤交换因子 (cAMP-GEF)/磷酸肌醇-3-激酶 (PI3K)/Akt 途径保护肝细胞免受胆汁酸诱导的细胞凋亡。这些研究的目的是确定该途径中的下游底物,并确定细胞保护作用发生在凋亡级联的哪个水平。由于糖原合酶激酶-3 (GSK) 的抑制性磷酸化发生在 PI3K/Akt 的下游,并且这种磷酸化与细胞存活有关,因此我们进行了研究以确定 GSK 是否是 cAMP-GEF/PI3K/Akt 介导的细胞保护作用的下游。我们的结果表明,用 cAMP-GEF 特异性类似物 4-(4-氯苯基硫代)-2'-O-甲基腺苷-3',5'-cAMP 处理肝细胞会导致 PI3K 依赖性 GSK 磷酸化。用几种结构和功能不同的抑制剂(包括溴代靛红-3'-肟(BIO)、马来酰亚胺(SB216763、SB415286)、噻二唑烷衍生物和 LiCl)直接化学抑制大鼠肝细胞或人 HUH7-NTCP 细胞中的 GSK,可减轻甘氨胆酸 (GCDC) 诱导的细胞凋亡。此外,用小干扰 RNA 对 GSK β 同工型进行基因沉默可减弱 HUH7-NTCP 细胞中 GCDC 诱导的细胞凋亡。腺病毒抑制 Rap1 可阻断 cAMP-GEF 介导的对 GCDC 诱导的细胞凋亡的保护作用和 Akt/GSK3β 磷酸化。GSK 抑制或 cAMP-GEF 激活可抑制 GCDC 诱导的促凋亡激酶 c-Jun NH(2)-末端激酶 (JNK) 的磷酸化。GCDC 诱导的细胞凋亡伴随着内质网应激标志物 pIEF2α 和 IRE-1 的磷酸化,而用 cAMP-GEF 类似物或 GSK 抑制剂预处理可防止这种磷酸化。总的来说,我们的结果支持肝细胞中存在 cAMP/cAMP-GEF/Rap1/PI3K/Akt/GSKβ 存活途径,该途径可抑制胆汁酸诱导的 JNK 磷酸化。