Programmed Cell Death in the Left and Right Ventricle of the Late Phase of Post-Infarction Heart Failure

Int J Mol Sci. 2020 Oct 21;21(20):7782. doi: 10.3390/ijms21207782.

Abstract

While necroptosis has been shown to contribute to the pathogenesis of post-infarction heart failure (HF), the role of autophagy remains unclear. Likewise, linkage between these two cell death modalities has not been sufficiently investigated. HF was induced by 60-min left coronary occlusion in adult Wistar rats and heart function was assessed 6 weeks later followed by immunoblotting analysis of necroptotic and autophagic proteins in both the left (LV) and right ventricle (RV). HF had no effect on RIP1 and RIP3 expression. PhosphoSer229-RIP3, acting as a pro-necroptotic signal, was increased in LV while deceased in RV of failing hearts. Total MLKL was elevated in RV only. Decrease in pSer555-ULK1, increase in pSer473-Akt and no significant elevation in beclin-1 and LC3-II/I ratio indicated rather a lowered rate of autophagy in LV. No beclin-1 upregulation and decreased LC3 processing also suggested the inhibition of both autophagosome formation and maturation in RV of failing hearts. In contrast, p89 PARP1 fragment, a marker of executed apoptosis, was increased in RV only. This is the first study showing a different signaling in ventricles of the late phase of post-infarction HF, highlighting necroptosis itself rather than its linkage with autophagy in LV, and apoptosis in RV.

Keywords: autophagy; cell death; heart failure; necroptosis.

MeSH terms

  • Animals
  • Apoptosis* / physiology
  • Autophagy / physiology
  • Heart Failure / etiology
  • Heart Failure / metabolism
  • Heart Failure / pathology*
  • Heart Ventricles / pathology
  • Male
  • Myocardial Infarction / complications
  • Myocardial Infarction / pathology*
  • Necroptosis / physiology
  • Organ Size
  • Protein Serine-Threonine Kinases / metabolism
  • Rats, Sprague-Dawley
  • Rats, Wistar
  • Receptor-Interacting Protein Serine-Threonine Kinases / metabolism
  • Signal Transduction

Substances

  • Protein Serine-Threonine Kinases
  • RIPK1 protein, rat
  • Receptor-Interacting Protein Serine-Threonine Kinases
  • Ripk3 protein, rat