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Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins

Title data

Fischer, Gunter ; Wittmann-Liebold, Brigitte ; Lang, Kurt ; Kiefhaber, Thomas ; Schmid, Franz X.:
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins.
In: Nature. Vol. 337 (2 February 1989) Issue 6206 . - pp. 476-478.
ISSN 1476-4687
DOI: https://doi.org/10.1038/337476a0

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Abstract in another language

The enzyme peptidyl-prolyl cis-trans isomerase (PPIase) was recently discovered in mammalian tissues and purified from porcine kidney. 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 proteins. 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 CsA. 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.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 2666859
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professorship Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 30 Apr 2015 13:21
Last Modified: 30 Apr 2015 13:21
URI: https://eref.uni-bayreuth.de/id/eprint/11237