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 language | English |
|---|---|
| Pages (from-to) | 817-825 |
| Number of pages | 9 |
| Journal | Proteomics |
| Volume | 6 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Feb 2006 |
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Keywords
- Cyclophilin A
- Glutathionylation
- T lymphocytes
ASJC Scopus subject areas
- Molecular Biology
- Genetics
Cite this
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 journal › Article
}
TY - JOUR
T1 - Redox regulation of cyclophilin A by glutathionylation
AU - Ghezzi, Pietro
AU - Casagrande, Simona
AU - Massignan, Tania
AU - Basso, Manuela
AU - Bellacchio, Emanuele
AU - Mollica, Luca
AU - Biasini, Emiliano
AU - Tonelli, Rossella
AU - Eberini, Ivano
AU - Gianazza, Elisabetta
AU - Dai, Wei Wei
AU - Fratelli, Maddalena
AU - Salmona, Mario
AU - Sherry, Barbara
AU - Bonetto, Valentina
PY - 2006/2
Y1 - 2006/2
N2 - 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.
AB - 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.
KW - Cyclophilin A
KW - Glutathionylation
KW - T lymphocytes
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UR - http://www.scopus.com/inward/citedby.url?scp=32944477519&partnerID=8YFLogxK
U2 - 10.1002/pmic.200500177
DO - 10.1002/pmic.200500177
M3 - Article
C2 - 16372262
AN - SCOPUS:32944477519
VL - 6
SP - 817
EP - 825
JO - Proteomics
JF - Proteomics
SN - 1615-9853
IS - 3
ER -