Redox regulation of cyclophilin A by glutathionylation

Pietro Ghezzi, Simona Casagrande, Tania Massignan, Manuela Basso, Emanuele Bellacchio, Luca Mollica, Emiliano Biasini, Rossella Tonelli, Ivano Eberini, Elisabetta Gianazza, Wei Wei Dai, Maddalena Fratelli, Mario Salmona, Barbara Sherry, Valentina Bonetto

Research output: Contribution to journalArticlepeer-review


Using redox proteomics techniques to characterize the thiol status of proteins in human T lymphocytes, we identified cyclophilin A (CypA) as a specifically oxidized protein early after mitogen activation. CypA is an abundantly expressed cytosolic protein, target of the immunosuppressive drug cydosporin A (CsA), for which a variety of functions has been described. In this study, we could identify CypA as a protein undergoing glutathionylation in vivo. Using MALDI-MS we identified Cys52 and Cys62 as targets of glutathionylation in T lymphocytes, and, using bioinformatic tools, we defined the reasons for the susceptibility of these residues to the modification. In addition, we found by circular dichroism spectroscopy that glutathionylation has an important impact on the secondary structure of CypA. Finally, we suggest that glutathionylation of CypA may have biological implications and that CypA may play a key role in redox regulation of immunity.

Original languageEnglish
Pages (from-to)817-825
Number of pages9
Issue number3
Publication statusPublished - Feb 2006


  • Cyclophilin A
  • Glutathionylation
  • T lymphocytes

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


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