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Cyclophilin‐A is a zinc‐dependent DNA binding protein in macrophages
Author(s) -
Krummrei Ulrike,
Bang Renate,
Schmidtchen Robert,
Brune Kay,
Bang Holger
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00815-q
Subject(s) - cyclophilin a , cyclophilin , zinc , chemistry , dna , microbiology and biotechnology , biochemistry , biology , gene , organic chemistry
The association of cyclosporin A (CsA) immunosuppression with inhibition of transcription factor‐dependent lymphokine gene activation formed the basis of our decision to investigate nuclear‐associated Cyp isoforms. Immunofluorescence microscopy of mouse macrophages cell line with a monoclonal antibody mAb7F1 raised against CypA shows a co‐localisation of CypA in the nucleus and in the cytosol. Nuclear CypA binds to DNA in a zinc ion‐dependent manner, in contrast to recombinant CypB. Peptidyl‐prolyl cisltrans isomerase (PPIase) activity of nuclear CypA is inhibited by zinc ions. The zinc inhibited CypA does not bind cyclosporin A (CsA). We suggest that nuclear Cyp in complex with zinc ions recognizes DNA sequences and is involved in transcription modulating processes.