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nature portfolio permissions reprints dohme research laboratories privacy policy immunology research peptidyl-prolyl cis–trans isomerases advertising subscribe nature social media nature 337 nature 338 nature 341 nature peptidyl-prolyl isomerase activity9 slyd samuel pazickyanna-leoni peptidyl-prolyl isomerase activity cyclosporin a-binding protein personal data data protection springerlink instant access permissions molecular life sciences cell-activation genes privacy cytokine signaling activity cytokine secretion assay cytosolic binding protein explore content subscription content fk-506 binding protein european economic area earliest responses inhibited inter-leu kins 2 institutional subscriptions read shirley lin & nolan accepting optional cookies journals search log issue learn newly discovered immunosuppressant manage preferences genome-wide characterization article siekierka distinct cytosolic proteins5 content article purchase salt upregulated cyclophilin journal publish molecular mechanisms article cite lymphocyte activation

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         headline:A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
         description:CYCLOSPORIN A and the newly discovered immunosuppressant, FK-506, are potent inhibitors of T cell activation1. In addition to their clinical importance in the prevention of allograft rejection, cyclosporin A and FK-506 represent important reagents for the study of the molecular mechanisms of lymphocyte activation. Cyclosporin A, a cyclic undecapeptide and FK-506, a macrolide, although chemically distinct, inhibit similar lymphocyte activation responses1, 2. The earliest responses inhibited in the T cell seem to be the expression of early phase T cell-activation genes for inter-leu kins 2, 3 and 4, granulocyte-macrophage colony stimulating factor and gamma interferon2–4. Although FK-506 and cyclosporin A seem to inhibit similar signal transduction processes, they do so by interacting with distinct cytosolic proteins5, 6. We report here the purification to homogeneity of a specific FK-506 binding protein that is distinct from the cyclosporin A-binding protein, cyclophilin7, 8. In addition, we show that this FK-506 binding protein, like cyclophilin, has peptidyl-prolyl isomerase activity9, 10.
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      headline:A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
      description:CYCLOSPORIN A and the newly discovered immunosuppressant, FK-506, are potent inhibitors of T cell activation1. In addition to their clinical importance in the prevention of allograft rejection, cyclosporin A and FK-506 represent important reagents for the study of the molecular mechanisms of lymphocyte activation. Cyclosporin A, a cyclic undecapeptide and FK-506, a macrolide, although chemically distinct, inhibit similar lymphocyte activation responses1, 2. The earliest responses inhibited in the T cell seem to be the expression of early phase T cell-activation genes for inter-leu kins 2, 3 and 4, granulocyte-macrophage colony stimulating factor and gamma interferon2–4. Although FK-506 and cyclosporin A seem to inhibit similar signal transduction processes, they do so by interacting with distinct cytosolic proteins5, 6. We report here the purification to homogeneity of a specific FK-506 binding protein that is distinct from the cyclosporin A-binding protein, cyclophilin7, 8. In addition, we show that this FK-506 binding protein, like cyclophilin, has peptidyl-prolyl isomerase activity9, 10.
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