Abstract

Complete prevention of the killing of L929 fibroblasts by tumor necrosis factor alpha (TNF) in the presence of 0.5 microg/ml actinomycin D (ActD) was obtained with cyclosporin A (CyA), an inhibitor of the mitochondrial permeability transition (MPT), and aristolochic acid (ArA), a phospholipase A2 inhibitor. Peripheral benzodiazepine receptor (PBzR) agonists (PK11195, FGIN 1-27, or chlorodiazepam), agents known to potentiate induction of the MPT, potentiated the cytotoxicity of TNF in the absence of ActD, an effect prevented by CyA plus ArA. The MPT was demonstrated independently of its effect on viability as the CyA-sensitive loss of rhodamine 123 fluorescence from cells preloaded with the dye. Treatment with TNF and ActD resulted in the loss of 80% of rhodamine fluorescence within 6 h, a time prior to any loss of viability. CyA plus ArA completely prevented this effect of TNF. Potentiation of the cytotoxicity of TNF by PBzR agonists was associated with induction of the MPT, as assessed by the loss of rhodamine fluorescence. CyA plus ArA completely prevented the loss of rhodamine 123. Ceramide replaced TNF in killing L929 fibroblasts, an effect also prevented by CyA plus ArA. Ceramide in the presence of ActD resulted in the loss of rhodamine fluorescence, an effect that was again prevented by CyA plus ArA. In addition, CyA plus ArA prevented the ability of PBzR agonists to potentiate the cytotoxicity of ceramide. In the presence of each PBzR agonist, ceramide caused the loss of rhodamine fluorescence, an effect completely prevented by CyA plus ArA. D609, an inhibitor of phosphatidylcholine-specific phospholipase C, completely prevented the killing by TNF, but not by ceramide, in the presence of ActD. D609 prevented induction of the MPT occurring with TNF, but not with ceramide. Inhibitors of endocytosis, as well as lysosomotropic amines, prevented the cytotoxicity of TNF, but not that of ceramide. It is concluded that the MPT is causally linked to the genesis of irreversible cell injury with TNF. In the face of an inhibition of protein synthesis, the MPT occurs as a consequence of the formation of ceramide.

Highlights

  • ¶ To whom correspondence should be addressed: Rm. 251, Jefferson Alumni Hall, Dept. of Pathology, Thomas Jefferson University, Philadelphia, PA 19107

  • We have utilized the L929 line of mouse fibroblasts to document that the mitochondrial permeability transition (MPT) is an essential event in the pathogenesis of the lethal cell injury induced by Tumor necrosis factor ␣ (TNF)

  • Cycloheximide (1 ␮M) sensitized L929 fibroblasts to the cytotoxicity of TNF

Read more

Summary

Introduction

¶ To whom correspondence should be addressed: Rm. 251, Jefferson Alumni Hall, Dept. of Pathology, Thomas Jefferson University, Philadelphia, PA 19107. TNF kills cancer cells in intact animals and a variety of cell lines in vitro. Attributed to both apoptosis and necrosis, the biochemical basis of the cytotoxic action of TNF is still largely unknown. The L929 line of mouse fibroblasts has been widely used to explore the mechanism of the cytotoxicity of TNF In these cells, the signaling pathways initiated by TNF lead to a death that is better characterized as necrosis rather than apoptosis [3, 4]. We have utilized the L929 line of mouse fibroblasts to document that the MPT is an essential event in the pathogenesis of the lethal cell injury induced by TNF. We provide an account that ceramide is an important

Methods
Results
Conclusion
Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.