| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1 Department of Biological Science and Biotechnology, Tsinghua University, Beijing 100084, P.R. China
2 Protein Science Laboratory of the Ministry of Education, School of Life Science and Engineering, Tsinghua University, Beijing 100084, P.R. China
Reprint requests to: Hai-Meng Zhou, Department of Biological Science and Biotechnology, Tsinghua University, Beijing 100084, P.R. China; e-mail: zhm-dbs{at}mail.tsinghua.edu.cn; fax: 8610-62772245.
Porcine kidney 18 kD peptidyl-prolyl cis-trans isomerase (PPIase) belongs to the cyclophilin family that is inhibited by the immunosuppressive drug cyclosporin A. The chaperone activity of PPIase was studied using inactive, active, and alkylated PPIase during rabbit muscle creatine kinase (CK) refolding. The results showed that low concentration inactive or active PPIase was able to improve the refolding yields, while high concentration PPIase decreased the CK reactivation yields. Aggregation was inhibited by inactive or active PPIase, and completely suppressed at 32 or 80 times the CK concentration (2.7 µM). However, alkylated PPIase was not able to prevent CK aggregation. In addition, the ability of inactive PPIase to affect CK reactivation and prevent CK aggregation was weaker than that of active PPIase. These results indicate that PPIase interacted with the early folding intermediates of CK, thus preventing their aggregation in a concentration-dependent manner. PPIase exhibited chaperone-like activity during CK refolding. The results also suggest that the isomerase activity of PPIase was independent of the chaperone activity, and that the proper molar ratio was important for the chaperone activity of PPIase. The cysteine residues of PPIase may be a peptide binding site, and may be an essential group for the chaperone function.
Keywords: Peptidyl-prolyl cis-trans isomerase; creatine kinase; refolding; chaperone-like
Abbreviations: CK, creatine kinase • CsA, cyclosporin A • CyP, cyclophilin • GdmCl, guanidine HCl • PPIase, peptidyl-prolyl cis-trans isomerase • SEC, size-exclusion chromatography
CiteULike 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  S. Li, J.-H. Bai, Y.-D. Park, and H.-M. Zhou Capture of monomeric refolding intermediate of human muscle creatine kinase Protein Sci., January 1, 2006; 15(1): 171 - 181. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T.-J. Zhao, W.-B. Ou, Q. Xie, Y. Liu, Y.-B. Yan, and H.-M. Zhou Catalysis of Creatine Kinase Refolding by Protein Disulfide Isomerase Involves Disulfide Cross-link and Dimer to Tetramer Switch J. Biol. Chem., April 8, 2005; 280(14): 13470 - 13476. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 F.-G. Meng, Y.-K. Hong, H.-W. He, A. E. Lyubarev, B. I. Kurganov, Y.-B. Yan, and H.-M. Zhou Osmophobic Effect of Glycerol on Irreversible Thermal Denaturation of Rabbit Creatine Kinase Biophys. J., October 1, 2004; 87(4): 2247 - 2254. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Schubert and S. Grimm Cyclophilin D, a Component of the Permeability Transition-Pore, Is an Apoptosis Repressor Cancer Res., January 1, 2004; 64(1): 85 - 93. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Chakraborty, I. Das, R. Datta, B. Sen, D. Bhattacharyya, C. Mandal, and A. K. Datta A Single-domain Cyclophilin from Leishmania donovani Reactivates Soluble Aggregates of Adenosine Kinase by Isomerase-independent Chaperone Function J. Biol. Chem., November 27, 2002; 277(49): 47451 - 47460. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
