Deletion of Ripk3 Prevents Motor Neuron Death In Vitro but not In Vivo

eNeuro. 2019 Feb 19;6(1):ENEURO.0308-18.2018. doi: 10.1523/ENEURO.0308-18.2018. eCollection 2019 Jan-Feb.

Abstract

Increasing evidence suggests that necroptosis, a form of programmed cell death (PCD), contributes to neurodegeneration in several disorders, including ALS. Supporting this view, investigations in both in vitro and in vivo models of ALS have implicated key molecular determinants of necroptosis in the death of spinal motor neurons (MNs). Consistent with a pathogenic role of necroptosis in ALS, we showed increased mRNA levels for the three main necroptosis effectors Ripk1, Ripk3, and Mlkl in the spinal cord of mutant superoxide dismutase-1 (SOD1G93A) transgenic mice (Tg), an established model of ALS. In addition, protein levels of receptor-interacting protein kinase 1 (RIPK1; but not of RIPK3, MLKL or activated MLKL) were elevated in spinal cord extracts from these Tg SOD1G93A mice. In postmortem motor cortex samples from sporadic and familial ALS patients, no change in protein levels of RIPK1 were detected. Silencing of Ripk3 in cultured MNs protected them from toxicity associated with SOD1G93A astrocytes. However, constitutive deletion of Ripk3 in Tg SOD1G93A mice failed to provide behavioral or neuropathological improvement, demonstrating no similar benefit of Ripk3 silencing in vivo. Lastly, we detected no genotype-specific myelin decompaction, proposed to be a proxy of necroptosis in ALS, in either Tg SOD1G93A or Optineurin knock-out mice, another ALS mouse model. These findings argue against a role for RIPK3 in Tg SOD1G93A-induced neurodegeneration and call for further preclinical investigations to determine if necroptosis plays a critical role in the pathogenesis of ALS.

Keywords: ALS; Ripk3; mice; motor neuron; necroptosis; neurodegeneration.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adult
  • Aged
  • Aged, 80 and over
  • Amyotrophic Lateral Sclerosis / metabolism
  • Animals
  • Astrocytes / metabolism
  • Astrocytes / pathology
  • Cell Cycle Proteins
  • Cell Death / physiology*
  • Cell Line
  • Coculture Techniques
  • Eye Proteins / genetics
  • Eye Proteins / metabolism
  • Female
  • Humans
  • Male
  • Membrane Transport Proteins
  • Mice, Inbred C57BL
  • Mice, Transgenic
  • Middle Aged
  • Motor Cortex / metabolism
  • Motor Cortex / pathology
  • Motor Neurons / metabolism*
  • Motor Neurons / pathology
  • Primary Cell Culture
  • Protein Kinases / metabolism
  • Receptor-Interacting Protein Serine-Threonine Kinases / deficiency*
  • Receptor-Interacting Protein Serine-Threonine Kinases / genetics
  • Receptor-Interacting Protein Serine-Threonine Kinases / metabolism
  • Spinal Cord / metabolism
  • Spinal Cord / pathology
  • Superoxide Dismutase-1 / genetics
  • Superoxide Dismutase-1 / metabolism

Substances

  • Cell Cycle Proteins
  • Eye Proteins
  • Membrane Transport Proteins
  • Optn protein, mouse
  • SOD1 protein, human
  • Superoxide Dismutase-1
  • MLKL protein, mouse
  • Protein Kinases
  • Receptor-Interacting Protein Serine-Threonine Kinases
  • Ripk3 protein, mouse