Joshi Suresh G, Francis Charles W, Silverman David J, Sahni Sanjeev K
Hematology-Oncology Unit, Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642, USA.
Infect Immun. 2003 Jul;71(7):4127-36. doi: 10.1128/IAI.71.7.4127-4136.2003.
Apoptotic host cell death is a critical determinant in the progression of microbial infections and outcome of resultant diseases. The potentially fatal human infection caused by Rickettsia rickettsii, the etiologic agent of Rocky Mountain spotted fever, involves the vascular endothelium of various organ systems of the host. Earlier studies have shown that survival of endothelial cells (EC) during this infection depends on their ability to activate the transcription factor nuclear factor kappa B (NF-kappa B). Here, we investigated the involvement of caspase cascades and associated signaling pathways in regulation of host cell apoptosis by NF-kappa B. Infection of cultured human EC with R. rickettsii with simultaneous inhibition of NF-kappa B induced the activation of apical caspases 8 and 9 and also the executioner enzyme, caspase 3, whereas infection alone had no significant effect. Inhibition of either caspase-8 or caspase-9 with specific cell-permeating peptide inhibitors caused a significant decline in the extent of apoptosis, confirming their importance. The peak caspase-3 activity occurred at 12 h postinfection and led to cleavage of poly(ADP-ribose) polymerase, followed by DNA fragmentation and apoptosis. However, the activities of caspases 6 and 7, other important downstream executioners, remained unchanged. Caspase-9 activation was mediated through the mitochondrial pathway of apoptosis, as evidenced by loss of transmembrane potential and cytoplasmic release of cytochrome c. These findings suggest that activation of NF-kappa B is required for maintenance of mitochondrial integrity of host cells and protection against infection-induced apoptotic death by preventing activation of caspase-9- and caspase-8-mediated pathways. Targeted inhibition of NF-kappa B may therefore be exploited to enhance the clearance of infections with R. rickettsii and other intracellular pathogens with similar survival strategies.
凋亡性宿主细胞死亡是微生物感染进展及由此引发疾病结局的关键决定因素。由落基山斑疹热的病原体立氏立克次体引起的潜在致命性人类感染涉及宿主多个器官系统的血管内皮。早期研究表明,在此感染过程中内皮细胞(EC)的存活取决于其激活转录因子核因子κB(NF-κB)的能力。在此,我们研究了半胱天冬酶级联反应及相关信号通路在NF-κB调控宿主细胞凋亡中的作用。用立氏立克次体感染培养的人内皮细胞并同时抑制NF-κB,可诱导顶端半胱天冬酶8和9以及执行酶半胱天冬酶3的激活,而单独感染则无显著影响。用特异性细胞穿透肽抑制剂抑制半胱天冬酶-8或半胱天冬酶-9可使凋亡程度显著下降,证实了它们的重要性。半胱天冬酶-3活性在感染后12小时达到峰值,导致聚(ADP-核糖)聚合酶裂解,随后出现DNA片段化和凋亡。然而,其他重要的下游执行者半胱天冬酶6和7的活性保持不变。半胱天冬酶-9的激活是通过凋亡的线粒体途径介导的,这可通过跨膜电位的丧失和细胞色素c的胞质释放得到证明。这些发现表明,激活NF-κB对于维持宿主细胞的线粒体完整性以及通过防止半胱天冬酶-9和半胱天冬酶-8介导的途径激活来保护细胞免受感染诱导的凋亡死亡是必需的。因此,靶向抑制NF-κB可能被用于增强对立氏立克次体及其他具有类似生存策略的细胞内病原体感染的清除。