Nrf2 activity is lost in the spinal cord and its astrocytes of aged mice

In Vitro Cell Dev Biol Anim. 2009 Jul-Aug;45(7):388-97. doi: 10.1007/s11626-009-9194-5. Epub 2009 May 19.

Abstract

We report herein a study of aging using in vitro and in vivo models. Glial fibrillary acidic protein and ferritin expression levels increased, and the levels of glutamate transporter 1 and transferrin receptor 1 decreased in aging mouse spinal cord and its astrocytes. Mitochondrial transmembrane potential in astrocytes decreased after 60 d of culture. Given the relationship between aging and loss of antioxidant tolerance capacity, we examined the expression of heme oxygenase 1 (HO1) and NAD(P)H/quinone oxidoreductase 1 (NQO1) in the old mouse astrocytes and spinal cord. Indeed, both antioxidant enzymes decreased there. Total nuclear factor E2-related factor 2, which governs basal and inducible expression of HO1 and NQO1, decreased significantly. Significantly, epigallocatechin gallate restored the Nrf2 activity.

MeSH terms

  • Aging / metabolism*
  • Animals
  • Astrocytes / metabolism*
  • Catechin / analogs & derivatives
  • Catechin / pharmacology
  • Cells, Cultured
  • Excitatory Amino Acid Transporter 2 / metabolism
  • Ferritins / metabolism
  • Glial Fibrillary Acidic Protein / metabolism
  • Heme Oxygenase-1 / metabolism
  • Membrane Potential, Mitochondrial
  • Mice
  • Models, Animal
  • NAD(P)H Dehydrogenase (Quinone)
  • NADPH Dehydrogenase / metabolism
  • NF-E2-Related Factor 2 / metabolism*
  • Neuroprotective Agents / pharmacology
  • Receptors, Transferrin / metabolism
  • Spinal Cord / cytology
  • Spinal Cord / metabolism*
  • Time Factors

Substances

  • Excitatory Amino Acid Transporter 2
  • Glial Fibrillary Acidic Protein
  • NF-E2-Related Factor 2
  • Neuroprotective Agents
  • Nfe2l2 protein, mouse
  • Receptors, Transferrin
  • Tfrc protein, mouse
  • Catechin
  • Ferritins
  • epigallocatechin gallate
  • Heme Oxygenase-1
  • NAD(P)H Dehydrogenase (Quinone)
  • Nqo1 protein, mouse
  • NADPH Dehydrogenase