Division of Nephrology, Guangdong Provincial People's Hospital, Guangdong Academy of Medical Sciences, Guangzhou, Guangdong, China.
Department of Nephrology, Sun Yat-sen Memorial Hospital, Sun Yat-sen University, Guangzhou, Guangdong, China.
Cell Death Dis. 2021 Jun 8;12(6):593. doi: 10.1038/s41419-021-03865-8.
Autophagy is an important renal-protective mechanism in septic acute kidney injury (AKI). Receptor interacting protein kinase 3 (RIP3) has been implicated in the renal tubular injury and renal dysfunction during septic AKI. Here we investigated the role and mechanism of RIP3 on autophagy in septic AKI. We showed an activation of RIP3, accompanied by an accumulation of the autophagosome marker LC3II and the autophagic substrate p62, in the kidneys of lipopolysaccharide (LPS)-induced septic AKI mice and LPS-treated cultured renal proximal tubular epithelial cells (PTECs). The lysosome inhibitor did not further increase the levels of LCII or p62 in LPS-treated PTECs. Moreover, inhibition of RIP3 attenuated the aberrant accumulation of LC3II and p62 under LPS treatment in vivo and in vitro. By utilizing mCherry-GFP-LC3 autophagy reporter mice in vivo and PTECs overexpression mRFP-GFP-LC3 in vitro, we observed that inhibition of RIP3 restored the formation of autolysosomes and eliminated the accumulated autophagosomes under LPS treatment. These results indicated that RIP3 impaired autophagic degradation, contributing to the accumulation of autophagosomes. Mechanistically, the nuclear translocation of transcription factor EB (TFEB), a master regulator of the lysosome and autophagy pathway, was inhibited in LPS-induced mice and LPS-treated PTECs. Inhibition of RIP3 restored the nuclear translocation of TFEB in vivo and in vitro. Co-immunoprecipitation further showed an interaction of RIP3 and TFEB in LPS-treated PTECs. Also, the expression of LAMP1 and cathepsin B, two potential target genes of TFEB involved in lysosome function, were decreased under LPS treatment in vivo and in vitro, and this decrease was rescued by inhibiting RIP3. Finally, overexpression of TFEB restored the autophagic degradation in LPS-treated PTECs. Together, the present study has identified a pivotal role of RIP3 in suppressing autophagic degradation through impeding the TFEB-lysosome pathway in septic AKI, providing potential therapeutic targets for the prevention and treatment of septic AKI.
自噬是脓毒症急性肾损伤(AKI)的重要肾保护机制。受体相互作用蛋白激酶 3(RIP3)已被牵涉到脓毒症 AKI 期间的肾小管损伤和肾功能障碍中。在这里,我们研究了 RIP3 在脓毒症 AKI 中的自噬作用及其机制。我们发现,在脂多糖(LPS)诱导的脓毒症 AKI 小鼠和 LPS 处理的肾小管上皮细胞(PTEC)中,RIP3 被激活,同时自噬体标志物 LC3II 和自噬底物 p62 积累。溶酶体抑制剂在 LPS 处理的 PTEC 中并未进一步增加 LCII 或 p62 的水平。此外,在体内和体外,抑制 RIP3 可减弱 LPS 处理下 LC3II 和 p62 的异常积累。通过利用体内 mCherry-GFP-LC3 自噬报告小鼠和体外过表达 mRFP-GFP-LC3 的 PTEC,我们观察到抑制 RIP3 可恢复自噬溶酶体的形成并消除 LPS 处理下积累的自噬体。这些结果表明,RIP3 损害了自噬降解,导致自噬体的积累。从机制上讲,转录因子 EB(TFEB)的核易位被抑制,TFEB 是溶酶体和自噬途径的主要调节因子,在 LPS 诱导的小鼠和 LPS 处理的 PTEC 中。在体内和体外,抑制 RIP3 可恢复 TFEB 的核易位。免疫共沉淀进一步表明,在 LPS 处理的 PTEC 中,RIP3 和 TFEB 相互作用。此外,LAMP1 和组织蛋白酶 B 的表达(两个涉及溶酶体功能的 TFEB 的潜在靶基因)在体内和体外 LPS 处理时均降低,抑制 RIP3 可挽救这种降低。最后,TFEB 的过表达可恢复 LPS 处理的 PTEC 中的自噬降解。总之,本研究确定了 RIP3 通过抑制脓毒症 AKI 中的 TFEB-溶酶体途径来抑制自噬降解的关键作用,为脓毒症 AKI 的预防和治疗提供了潜在的治疗靶点。