Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins (original) (raw)
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- Published: 02 February 1989
Nature volume 337, pages 476–478 (1989)Cite this article
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Abstract
The enzyme peptidyl-prolyl cis-trans isomerase (PPIase) was recently discovered in mammalian tissues and purified from porcine kidney1. It catalyses the slow cis-trans isomerization of proline peptide (Xaa-Pro) bonds in oligopeptides and accelerates slow, rate-limiting steps in the folding of several proteins2-5. Here, we report the N-terminal sequence of PPIase together with further chemical and enzymatic properties. The results indicate that this enzyme is probably identical to cyclophilin, a recently discovered mammalian protein which binds tightly to cyclosporin A (CsA). Cyclophilin is thought to be linked to the immunosuppressive action of CsA6-11. The first 38 amino-acid residues of porcine PPIase and of bovine cyclophilin are identical and the two proteins both have a relative molecular mass of about 17,000 (ref. 7). The catalysis of prolyl isomerization in oligopeptides and of protein folding by PPIase are strongly inhibited in the presence of low levels of CsA. The activities of both PPIase and cyclophilin depend on a single sulphydryl group. At present it is unknown whether the inhibition of prolyl isomerase activity is related with the immunosuppressive action of CsA.
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Authors and Affiliations
- WB Biochemie, Sektion Biowissenschaften, Martin-Luther-Universität Halle, Domplatz 1, DDR-4020, Halle, GDR
Gunter Fischer - Max-Planck-Institut für Molekulare Genetik, Ihnestrasse 63-73, D-1000, Berlin, 33, FRG
Brigitte Wittmann-Liebold - Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, D-8400, Regensburg, FRG
Kurt Lang, Thomas Kiefhaber & Franz X. Schmid
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- Gunter Fischer
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Fischer, G., Wittmann-Liebold, B., Lang, K. et al. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins.Nature 337, 476–478 (1989). https://doi.org/10.1038/337476a0
- Received: 30 September 1988
- Accepted: 05 December 1988
- Issue Date: 02 February 1989
- DOI: https://doi.org/10.1038/337476a0