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 journalArticle

33 Citations (Scopus)

Abstract

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
JournalProteomics
Volume6
Issue number3
DOIs
Publication statusPublished - Feb 2006

Fingerprint

Cyclophilin A
Oxidation-Reduction
T-cells
Proteins
Circular dichroism spectroscopy
T-Lymphocytes
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Bioinformatics
Immunosuppressive Agents
Circular Dichroism
Computational Biology
Mitogens
Sulfhydryl Compounds
Proteomics
Immunity
Spectrum Analysis
Chemical activation
Pharmaceutical Preparations

Keywords

  • Cyclophilin A
  • Glutathionylation
  • T lymphocytes

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Ghezzi, P., Casagrande, S., Massignan, T., Basso, M., Bellacchio, E., Mollica, L., ... Bonetto, V. (2006). Redox regulation of cyclophilin A by glutathionylation. Proteomics, 6(3), 817-825. https://doi.org/10.1002/pmic.200500177

Redox regulation of cyclophilin A by glutathionylation. / Ghezzi, Pietro; Casagrande, Simona; Massignan, Tania; Basso, Manuela; Bellacchio, Emanuele; Mollica, Luca; Biasini, Emiliano; Tonelli, Rossella; Eberini, Ivano; Gianazza, Elisabetta; Dai, Wei Wei; Fratelli, Maddalena; Salmona, Mario; Sherry, Barbara; Bonetto, Valentina.

In: Proteomics, Vol. 6, No. 3, 02.2006, p. 817-825.

Research output: Contribution to journalArticle

Ghezzi, P, Casagrande, S, Massignan, T, Basso, M, Bellacchio, E, Mollica, L, Biasini, E, Tonelli, R, Eberini, I, Gianazza, E, Dai, WW, Fratelli, M, Salmona, M, Sherry, B & Bonetto, V 2006, 'Redox regulation of cyclophilin A by glutathionylation', Proteomics, vol. 6, no. 3, pp. 817-825. https://doi.org/10.1002/pmic.200500177
Ghezzi P, Casagrande S, Massignan T, Basso M, Bellacchio E, Mollica L et al. Redox regulation of cyclophilin A by glutathionylation. Proteomics. 2006 Feb;6(3):817-825. https://doi.org/10.1002/pmic.200500177
Ghezzi, Pietro ; Casagrande, Simona ; Massignan, Tania ; Basso, Manuela ; Bellacchio, Emanuele ; Mollica, Luca ; Biasini, Emiliano ; Tonelli, Rossella ; Eberini, Ivano ; Gianazza, Elisabetta ; Dai, Wei Wei ; Fratelli, Maddalena ; Salmona, Mario ; Sherry, Barbara ; Bonetto, Valentina. / Redox regulation of cyclophilin A by glutathionylation. In: Proteomics. 2006 ; Vol. 6, No. 3. pp. 817-825.
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