Nuclear lamina defects cause ATM-dependent NF-κB activation and link accelerated aging to a systemic inflammatory response

Genes Dev. 2012 Oct 15;26(20):2311-24. doi: 10.1101/gad.197954.112. Epub 2012 Sep 26.

Abstract

Alterations in the architecture and dynamics of the nuclear lamina have a causal role in normal and accelerated aging through both cell-autonomous and systemic mechanisms. However, the precise nature of the molecular cues involved in this process remains incompletely defined. Here we report that the accumulation of prelamin A isoforms at the nuclear lamina triggers an ATM- and NEMO-dependent signaling pathway that leads to NF-κB activation and secretion of high levels of proinflammatory cytokines in two different mouse models of accelerated aging (Zmpste24(-/-) and Lmna(G609G/G609G) mice). Causal involvement of NF-κB in accelerated aging was demonstrated by the fact that both genetic and pharmacological inhibition of NF-κB signaling prevents age-associated features in these animal models, significantly extending their longevity. Our findings provide in vivo proof of principle for the feasibility of pharmacological modulation of the NF-κB pathway to slow down the progression of physiological and pathological aging.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aging / immunology
  • Aging / pathology
  • Aging / physiology*
  • Animals
  • Anti-Inflammatory Agents, Non-Steroidal / pharmacology
  • Ataxia Telangiectasia Mutated Proteins
  • Cell Cycle Proteins / metabolism*
  • Cell Line
  • Cells, Cultured
  • Cellular Senescence
  • DNA-Binding Proteins / metabolism*
  • Humans
  • Inflammation / enzymology
  • Inflammation / physiopathology
  • Intracellular Signaling Peptides and Proteins / metabolism
  • Lamin Type A
  • Longevity / drug effects
  • Longevity / genetics
  • Membrane Proteins / deficiency
  • Membrane Proteins / genetics
  • Metalloendopeptidases / deficiency
  • Metalloendopeptidases / genetics
  • Mice
  • NF-kappa B / genetics
  • NF-kappa B / metabolism*
  • Nuclear Lamina / enzymology
  • Nuclear Lamina / genetics*
  • Nuclear Lamina / metabolism*
  • Nuclear Proteins / metabolism
  • Protein Precursors / metabolism
  • Protein Serine-Threonine Kinases / metabolism*
  • Signal Transduction
  • Sodium Salicylate / pharmacology
  • Transcription Factor RelA / genetics
  • Transcription Factor RelA / metabolism
  • Transcriptional Activation / drug effects
  • Tumor Suppressor Proteins / metabolism*

Substances

  • Anti-Inflammatory Agents, Non-Steroidal
  • Cell Cycle Proteins
  • DNA-Binding Proteins
  • Intracellular Signaling Peptides and Proteins
  • Lamin Type A
  • Membrane Proteins
  • NEMO protein, mouse
  • NF-kappa B
  • Nuclear Proteins
  • Protein Precursors
  • Transcription Factor RelA
  • Tumor Suppressor Proteins
  • prelamin A
  • ATM protein, human
  • Ataxia Telangiectasia Mutated Proteins
  • Atm protein, mouse
  • Protein Serine-Threonine Kinases
  • Metalloendopeptidases
  • Zmpste24 protein, mouse
  • Sodium Salicylate