Atypical pathways of NF-kappaB activation and aging

Exp Gerontol. 2009 Apr;44(4):250-5. doi: 10.1016/j.exger.2008.12.005. Epub 2009 Jan 12.

Abstract

The eukaryotic transcription factor Nuclear Factor-kappaB (NF-kappaB) is a master regulator for inflammatory responses, mediating cellular defense against infectious agents and environmental and cellular stress. However, recent evidence-based studies have demonstrated that constitutive activation of NF-kappaB is a ubiquitous phenomenon among various cell types in the aging phenotype, contributing deleterious effects that oppose the acutely beneficial effects of NF-kappaB seen in the inflammatory response. Expression of NF-kappaB with age is consistent with elevated levels of inflammatory markers and a pro-inflammatory phenotype, manifested in many age-associated diseases. While inducible activating mechanisms for NF-kappaB in the innate immune response are well characterized, constitutive activation in aging cells warrants further investigation of mechanisms collectively called atypical pathways. In this review, we provide a comprehensive examination of such NF-kappaB activating mechanisms, including mitochondrial dysfunction, endoplasmic stress response, organelle cross-talk, secondary messengers and DNA damage. Investigation of mechanisms of NF-kappaB in aging as an important marker of cellular stress provides guidance for the development of a systems view of cellular aging.

Publication types

  • Review

MeSH terms

  • Aging / genetics*
  • Aging / physiology
  • Calcium Channels / genetics
  • Calcium Channels / physiology
  • DNA Damage / genetics
  • Gene Expression Regulation / genetics*
  • Humans
  • Inflammation / genetics*
  • Inflammation / physiopathology
  • Membrane Proteins / genetics
  • Mitochondrial Proteins / genetics
  • NF-kappa B / genetics*
  • NF-kappa B / physiology
  • Oxidative Stress / genetics
  • Signal Transduction / genetics*

Substances

  • Calcium Channels
  • Membrane Proteins
  • Mitochondrial Proteins
  • NF-kappa B
  • ROMO1 protein, human