In human endothelial cells rapamycin causes mTORC2 inhibition and impairs cell viability and function

Cardiovasc Res. 2008 Jun 1;78(3):563-71. doi: 10.1093/cvr/cvn024. Epub 2008 Feb 4.

Abstract

Aim: Drug-eluting stents are widely used to prevent restenosis but are associated with late endothelial damage. To understand the basis for this effect, we have studied the consequences of a prolonged incubation with rapamycin on the viability and functions of endothelial cells.

Methods and results: Human umbilical vein or aorta endothelial cells were exposed to rapamycin in the absence or in the presence of tumour necrosis factor alpha (TNFalpha). After a 24 h-incubation, rapamycin (100 nM) caused a significant cell loss associated with the increase of both apoptosis and necrosis, as quantified by propidium iodide staining, caspase 3 activity, and lactate dehydrogenase release. Rapamycin also impaired cell mobility, as assessed by a wound test, and promoted the formation of actin stress fibres, as determined with confocal microscopy. Moreover, the inhibitor prolonged TNFalpha-dependent E-selectin induction, inhibited endothelial nitric oxide synthase expression at both mRNA (quantitative real-time polymerase chain reaction) and protein level (enzyme-linked immunosorbent assay and western blot), and lowered bioactive nitric oxide output (RFL-6 reporter cell assay). Under the conditions adopted, rapamycin inhibited both mammalian target-of-rapamycin complexes (mTORC1 and mTORC2), as indicated by the reduced amount of raptor and rictor bound to mTOR in immunoprecipitates and by the marked hypophosphorylation of protein S6 kinase I (p70S6K) and Akt, determined by western blotting. The selective inhibition of mTORC1 by AICAR did not affect endothelial viability.

Conclusion: A prolonged treatment with rapamycin impairs endothelial function and hinders cell viability. Endothelial damage seems dependent on mTORC2 inhibition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Apoptosis / drug effects
  • Blotting, Western
  • Cardiovascular Agents / toxicity*
  • Carrier Proteins / metabolism
  • Caspase 3 / metabolism
  • Cell Movement / drug effects
  • Cell Survival / drug effects
  • Dose-Response Relationship, Drug
  • E-Selectin / metabolism
  • Endothelial Cells / drug effects*
  • Endothelial Cells / enzymology
  • Endothelial Cells / metabolism
  • Endothelial Cells / pathology
  • Enzyme-Linked Immunosorbent Assay
  • Humans
  • Immunoprecipitation
  • L-Lactate Dehydrogenase / metabolism
  • Mechanistic Target of Rapamycin Complex 1
  • Microscopy, Confocal
  • Multiprotein Complexes
  • Necrosis
  • Nitric Oxide / metabolism
  • Nitric Oxide Synthase Type III / metabolism
  • Polymerase Chain Reaction
  • Protein Kinases / metabolism*
  • Proteins / metabolism
  • Rapamycin-Insensitive Companion of mTOR Protein
  • Regulatory-Associated Protein of mTOR
  • Ribosomal Protein S6 Kinases, 70-kDa / metabolism
  • Sirolimus / toxicity*
  • Stress Fibers / drug effects
  • Stress Fibers / metabolism
  • TOR Serine-Threonine Kinases
  • Tacrolimus / pharmacology
  • Theophylline / analogs & derivatives
  • Time Factors
  • Transcription Factors / antagonists & inhibitors
  • Tumor Necrosis Factor-alpha / metabolism
  • Up-Regulation

Substances

  • Adaptor Proteins, Signal Transducing
  • Cardiovascular Agents
  • Carrier Proteins
  • E-Selectin
  • Multiprotein Complexes
  • Proteins
  • RICTOR protein, human
  • RPTOR protein, human
  • Rapamycin-Insensitive Companion of mTOR Protein
  • Regulatory-Associated Protein of mTOR
  • Transcription Factors
  • Tumor Necrosis Factor-alpha
  • Nitric Oxide
  • Theophylline
  • L-Lactate Dehydrogenase
  • NOS3 protein, human
  • Nitric Oxide Synthase Type III
  • Protein Kinases
  • MTOR protein, human
  • Mechanistic Target of Rapamycin Complex 1
  • Ribosomal Protein S6 Kinases, 70-kDa
  • TOR Serine-Threonine Kinases
  • CASP3 protein, human
  • Caspase 3
  • Sirolimus
  • Tacrolimus
  • bamifylline