Cyclophilin A Binds to Peroxiredoxins and Activates Its Peroxidase Activity

Using matrixassisted laser desorption/ionization time-of-flight mass spectrometry and MS-Fit, we identified the 20-kDa Prx VI-binding protein as a cyclophilin A

Sang Pil Lee; Young Sun Hwang; Yong Jun Kim; Ki-Sun Kwon; Hyung Jung Kim; Kanghwa Kim; Ho Zoon Chae

2002

Scholarcy highlights

  • Peroxiredoxin1 is a member of a growing family of thiol peroxidases that reduce peroxides to corresponding alcohols using reactive cysteine residue(s) in its active center
  • The Glutathione peroxidase activity of Prx VI has been confirmed, peroxidase activity of Prx VI in the presence of GSH was generally much lower than that with dithiothreitol, while the glutamine synthetase protection activity of Prx VI in the presence of DTT was comparable with selenium-GPx as well as other Prx members
  • To identify the possible electron donor or the protein functionally linked to Prx VI, we performed a Prx VI protein overlay assay with fractionated rat lung crude extracts
  • To confirm whether the human CyP-A itself has the capacity to reduce Prx, we investigated the hCyPA-dependent reduction of an intermolecular disulfide bond of Prx II by using non-reducing SDS-PAGE analysis
  • Using the Prx VI overlay assay, we have identified cyclophilin A as a Prx VI-binding protein and its activation of Prx VI antioxidant activity
  • Samples containing 200 ng of Prx II were analyzed on a 12% SDS-PAGE gel without 2-mercaptoethanol, and the separated Prx II protein bands were visualized by Western immunostaining with Prx II-specific antiserum
  • Protection activity of Prx II or Prx III and the reduction of Prx II, clearly demonstrate the cyclosphorin A independence of cyclophilin A binding and activation of Prx isotypes

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