Cyclophilin A Binds to Peroxiredoxins and Activates Its Peroxidase Activity
作者： Sang Pil Lee , Young Sun Hwang , Yong Jun Kim , Ki-Sun Kwon , Hyung Jung Kim
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摘要: Six distinct peroxiredoxin (Prx) proteins (Prx I-VI) from genes have been identified in mammalian tissues. Prxs are members of a group peroxidases that conserved reactive cysteine residue(s) the active site(s). An immediate physiological electron donor for peroxidase catalysis five Prx I-V) has as thioredoxin (Trx), but VI (1-Cys Prx) is still unclear. To identify an and binding protein VI, we performed overlay assay. A 20-kDa was by assay with flow-through fractions High-Q column rat lung crude extracts. Using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF) MS-Fit, VI-binding cyclophilin (CyP-A). The recombinant human CyP-A (hCyP-A) to confirmed using hCyP-A Western immunoblot analysis hCyP-A-specific antibodies. enhanced antioxidant activity well other known isotypes. supported II both against thiol (dithiothreitol)-containing metal-catalyzed oxidation (MCO) systems ascorbate-containing MCO systems. reduced without help any reductant, reduction cyclosporin A-independent. These results strongly suggest not only binds also supports its donor. In addition, Cys(115) Cys(161) were found be involved activation Prx.
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