Changes in jun N-terminal kinase activation by stress during aging of cultured normal human fibroblasts

Mol Carcinog. 1996 Sep;17(1):8-12. doi: 10.1002/(SICI)1098-2744(199609)17:1<8::AID-MC2>3.0.CO;2-F.

Abstract

The molecular changes associated with the aging process include the reduced activity of transcription factors (such as AP-1) and an impaired response to stress, which has been well documented in the case of the heat-shock (HS) response. Using human diploid fibroblasts of early and late passages as an in vitro model for aging, we elucidated changes in the activation of jun N-terminal kinases (JNKs), which play an important role in the mammalian stress response. We found that early-passage cells exhibited a greater degree of JNK activation in response to HS and ultraviolet (UV) C light treatments than did late-passage cells. Decreased JNK activation was dependent on the number of passages but was not affected by varying doses of UV irradiation. Analysis of protein kinase A, mitogen-activated protein kinase, and src-related tyrosine kinases revealed no decreased activities in aged cells, indicating a selective rather than generalized decrease in kinase activities during aging. A further understanding of this impaired activation of JNK may provide insights into the mechanisms of stress response and cellular aging.

MeSH terms

  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
  • Cellular Senescence*
  • Enzyme Activation
  • Fibroblasts / enzymology
  • Heat-Shock Response / genetics*
  • Humans
  • JNK Mitogen-Activated Protein Kinases
  • Mitogen-Activated Protein Kinases*
  • Stress, Physiological / enzymology
  • Stress, Physiological / genetics*
  • Ultraviolet Rays

Substances

  • Calcium-Calmodulin-Dependent Protein Kinases
  • JNK Mitogen-Activated Protein Kinases
  • Mitogen-Activated Protein Kinases