Inhibitor of apoptosis proteins as novel targets in inflammatory processes

Arterioscler Thromb Vasc Biol. 2011 Oct;31(10):2240-50. doi: 10.1161/ATVBAHA.111.234294. Epub 2011 Aug 4.

Abstract

Objective: Inhibitor of apoptosis proteins (IAPs), such as X-linked or cellular IAP 1/2 (XIAP, cIAP1/2), are important regulators of apoptosis. IAP antagonists are currently under clinical investigation as anticancer agents. Interestingly, IAPs participate in the inflammation-associated TNF receptor signaling complex and regulate NFκB signaling. This raises the question about the role of IAPs in inflammation. Here, we investigated the anti-inflammatory potential of IAP inhibitors and the role of IAPs in inflammatory processes of endothelial cells.

Methods and results: In mice, the small molecule IAP antagonist A-4.10099.1 (ABT) suppressed antigen-induced arthritis, leukocyte infiltration in concanavalin A-evoked liver injury, and leukocyte transmigration in the TNFα-activated cremaster muscle. In vitro, we observed an attenuation of leukocyte-endothelial cell interaction by downregulation of the intercellular adhesion molecule-1. ABT did not impair NFκB signaling but decreased the TNFα-induced activation of the TGF-β-activated kinase 1, p38, and c-Jun N-terminal kinase. These effects are based on the proteasomal degradation of cIAP1/2 accompanied by an altered ratio of the levels of membrane-localized TNF receptor-associated factors 2 and 5.

Conclusions: Our results reveal IAP antagonism as a profound anti-inflammatory principle in vivo and highlight IAPs as important regulators of inflammatory processes in endothelial cells.

MeSH terms

  • Animals
  • Anti-Inflammatory Agents / pharmacology*
  • Apoptosis / drug effects
  • Arthritis, Experimental / immunology
  • Arthritis, Experimental / metabolism
  • Arthritis, Experimental / prevention & control*
  • Baculoviral IAP Repeat-Containing 3 Protein
  • Caspases / metabolism
  • Cell Adhesion / drug effects
  • Chemical and Drug Induced Liver Injury / immunology
  • Chemical and Drug Induced Liver Injury / metabolism
  • Chemical and Drug Induced Liver Injury / prevention & control*
  • Concanavalin A
  • Disease Models, Animal
  • Dose-Response Relationship, Drug
  • Endothelial Cells / drug effects*
  • Endothelial Cells / immunology
  • Endothelial Cells / metabolism
  • Enzyme Activation
  • HeLa Cells
  • Humans
  • Inhibitor of Apoptosis Proteins / antagonists & inhibitors*
  • Inhibitor of Apoptosis Proteins / genetics
  • Inhibitor of Apoptosis Proteins / metabolism
  • Intercellular Adhesion Molecule-1 / metabolism
  • JNK Mitogen-Activated Protein Kinases / metabolism
  • Leukocytes / drug effects
  • Leukocytes / immunology
  • Leukocytes / metabolism
  • MAP Kinase Kinase Kinases / metabolism
  • Male
  • Mice
  • Mice, Inbred C57BL
  • NF-kappa B / metabolism
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Processing, Post-Translational
  • RNA Interference
  • Serum Albumin, Bovine
  • TNF Receptor-Associated Factor 2 / metabolism
  • TNF Receptor-Associated Factor 5 / metabolism
  • Time Factors
  • Transendothelial and Transepithelial Migration / drug effects
  • Transfection
  • Tumor Necrosis Factor-alpha / metabolism
  • Ubiquitin-Protein Ligases
  • Ubiquitination
  • p38 Mitogen-Activated Protein Kinases / metabolism

Substances

  • Anti-Inflammatory Agents
  • Inhibitor of Apoptosis Proteins
  • NF-kappa B
  • TNF Receptor-Associated Factor 2
  • TNF Receptor-Associated Factor 5
  • Tumor Necrosis Factor-alpha
  • methylated bovine serum albumin
  • Concanavalin A
  • Intercellular Adhesion Molecule-1
  • Serum Albumin, Bovine
  • BIRC2 protein, human
  • BIRC3 protein, human
  • Baculoviral IAP Repeat-Containing 3 Protein
  • Ubiquitin-Protein Ligases
  • JNK Mitogen-Activated Protein Kinases
  • p38 Mitogen-Activated Protein Kinases
  • MAP Kinase Kinase Kinases
  • MAP kinase kinase kinase 7
  • Caspases
  • Proteasome Endopeptidase Complex