Cyclophilin‐A is a zinc‐dependent DNA binding protein in macrophages

FEBS Letters

Bang, Renate¹  Brune, Kay¹  Krummrei, Ulrike¹  Bang, Holger¹  Schmidtchen, Robert¹ 

[1] Institute of Experimental and Clinical Pharmacology and Toxicology, University of Erlangen-Nürnberg, Universitätsstr 22, 91054 Erlangen, Germany

关键词: PPIase;    Peptidyl-prolyl-cis/trans-isomerase;    Cyclophilin;    CsA;    Zinc binding;    DNA binding;    Macrophage;    Cyp;    cyclophilin;    CsA;    cyclosporin A;    HPLC;    high performance liquid chromatography;    Ig;    immunglobulin;    mAb(s);    monoclonal antibody(-ies);    PBS;    phosphate-buffered saline;    PPIase;    peptidylprolyl cis/trans-isomerase;    SDS-PAGE;    sodium dodecylsulfate polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(95)00815-Q

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown