Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin

Peptidyl-prolyl cis-trans isomerase (PPIase) catalyses the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and has been shown to accelerate the refolding of several proteins in vitro. Its activity has been detected in yeast, insects and Escherichia coli as well as in mammals...

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Bibliographic Details
Published in:Nature (London) 1989-02, Vol.337 (6206), p.473-475
Main Authors: Takahashi, Nobuhiro, Hayano, Toshiya, Suzuki, Masanori
Format: Article
Language:English
Subjects:
Amino Acid Isomerases - antagonists & inhibitors
Amino Acid Isomerases - metabolism
Amino Acid Sequence
Animals
Carrier Proteins - metabolism
Cattle
cyclosporin A-binding protein
Cyclosporins - metabolism
Cyclosporins - pharmacology
E coli
Electrophoresis, Polyacrylamide Gel
Genetics
Humans
kidney
Kidney - enzymology
Lymphocyte Activation
Medical research
Molecular Sequence Data
Molecular Weight
Peptidylprolyl Isomerase
pigs
Protein synthesis
Proteins
Rats
Sequence Homology, Nucleic Acid
Swine
T-Lymphocytes - immunology
Yeasts
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Summary:Peptidyl-prolyl cis-trans isomerase (PPIase) catalyses the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and has been shown to accelerate the refolding of several proteins in vitro. Its activity has been detected in yeast, insects and Escherichia coli as well as in mammals, and it is though to be essential for protein folding during protein synthesis in the cell. We purified PPIase from pig kidney and found that its amino-acid sequence is identical to that reported for bovine cyclophilin, a protein known to bind the immunosuppressive drug, cyclosporin A (ref. 5). To investigate the functional relationship between PPIase and cyclophilin we examined the effect of cyclosporin A on PPIase activity and found that it was inhibitory. Thus we propose that the peptidyl-prolyl cis-trans isomerizing activity of PPIase may be involved in events, such as those occurring early in T-cell activation, that are suppressed by cyclosporin A.
ISSN:0028-0836
1476-4687
DOI:10.1038/337473a0