Autophagy: The missing link between non-enzymatically glycated proteins inducing apoptosis and premature senescence of endothelial cells?

Autophagy. 2008 May;4(4):521-3. doi: 10.4161/auto.5904. Epub 2008 Mar 13.

Abstract

In a series of studies into the fate of endothelial cells exposed to non-enzymatically glycated collagen I, a model of cytotoxic molecules relevant to diabetic vasculopathy, we demonstrate that cells either undergo apoptosis or become prematurely senescent despite relatively spared telomeres and telomerase activity. Our most recent work shows that long-lived advanced glycation end product (AGE)-modified proteins induce (1) lysosomal permeabilization leading to the inefficiency of autophagy due to the reduced digestion (early) and non-fusion (later) of lysosomes with phagosomes--a frustrated autophagy; and (2) accumulation of lipid mediators, such as ceramide and sphingosine-1-phosphate, known to be involved in autophagic cell death. Under the experimental conditions described here, the seesaw relations between premature senescence and apoptosis are integrated by autophagy, which plays a novel function of a cellular switch between states of premature senescence and apoptosis.

MeSH terms

  • Apoptosis / physiology*
  • Autophagy / physiology*
  • Biomarkers / metabolism
  • Cell Line
  • Cellular Senescence*
  • Endothelial Cells / physiology*
  • Glycation End Products, Advanced / metabolism
  • Glycosylation
  • Humans
  • Lysosomes / metabolism
  • Membrane Lipids / metabolism

Substances

  • Biomarkers
  • Glycation End Products, Advanced
  • Membrane Lipids