Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin

These results suggest that, together with glutathione peroxidase and catalase, Prx enzymes likely play an important role in eliminating peroxides generated during metabolism as well as during stimulation of cell surface receptors

Ho Zoon Chae; Hyung Jung Kim; Sang Won Kang; Sue Goo Rhee

2002

Scholarcy highlights

  • A peroxidase from yeast that reduces H2O2 with the use of electrons provided by thioredoxin together with homologs from a wide variety of species constitute the peroxiredoxin family of proteins
  • Twelve mammalian Prx members have been previously identified in association with various cellular functions apparently unrelated to peroxidase activity
  • Immunoblot analysis of various rat tissues and cultured cells indicated that most cell types contain the three Prx isoforms, the sum of which amounts to ∼1–10 μg per milligram of soluble protein
  • Prx I and II are cytosolic proteins, whereas Prx III is localized in mitochondria
  • These results suggest that, together with glutathione peroxidase and catalase, Prx enzymes likely play an important role in eliminating peroxides generated during metabolism as well as during stimulation of cell surface receptors

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