PT  - JOURNAL ARTICLE
AU  - JIAN CHEN
AU  - ROBERT LIEFKE
AU  - LIXIN JIANG
AU  - JIAHUI WANG
AU  - CHAOQUN HUANG
AU  - ZHAOHUA GONG
AU  - CORDELIA SCHIENE-FISCHER
AU  - LONG YU
TI  - Biochemical Features of Recombinant Human Cyclophilin J
DP  - 2016 Mar 01
TA  - Anticancer Research
PG  - 1175--1180
VI  - 36
IP  - 3
4099  - http://ar.iiarjournals.org/content/36/3/1175.short
4100  - http://ar.iiarjournals.org/content/36/3/1175.full
SO  - Anticancer Res2016 Mar 01; 36
AB  - Aim: To characterize the biochemical features of the newest member of cyclophilin family of peptidyl-prolyl cis/trans-isomerases (PPIases), cyclophilin J (CYPJ). Materials and Methods: PPIase assays were performed on purified hCYPJ and its mutated variants. The substrate specificity, half-maximal inhibitory concentration (IC50) of cyclosporin A (CsA) inhibition and circular dichroism (CD) spectrum of CYPJ were measured. Mercury pathway profiling luciferase assays were also performed. Results: The catalytic number/Michaelis constant (kcat/KM) value of CYPJ was 9.5×104 s−1M−1. CYPJ additionally catalyzed norleucine-proline, isoleucine-proline and glutamine-proline peptides compared to CYPA and Escherichia coli PPIases. CYPJ was inhibited by CsA in a dose-dependent manner with IC50 of 12.1±0.9 μM. The CD spectrum of CYPJ was similar to CYPA. CYPJ significantly up-regulated the transcription of E-box, E2F, retinoblastoma (Rb), p53, activator protein 1 (AP1), NF-κB and phospho-cAMP response element (CRE) cis-response element in 293T cells. Conclusion: CYPJ structurally resembles CYPA. It is sensitive to inhibition by CsA and plays a role in regulating cell growth, proliferation, and apoptosis.