Proteomic analyses reveal that ginsenoside Rg3() partially reverses cellular senescence in human dermal fibroblasts by inducing peroxiredoxin.

BACKGROUND

The cellular senescence of primary cultured cells is an irreversible process characterized by growth arrest. Restoration of senescence by ginsenosides has not been explored so far. Rg3() treatment markedly decreased senescence-associated β-galactosidase activity and intracellular reactive oxygen species levels in senescent human dermal fibroblasts (HDFs). However, the underlying mechanism of this effect of Rg3() on the senescent HDFs remains unknown.

METHODS

We performed a label-free quantitative proteomics to identify the altered proteins in Rg3()-treated senescent HDFs. Upregulated proteins induced by Rg3() were validated by real-time polymerase chain reaction and immunoblot analyses.

RESULTS

Finally, 157 human proteins were identified, and variable peroxiredoxin (PRDX) isotypes were highly implicated by network analyses. Among them, the mitochondrial PRDX3 was transcriptionally and translationally increased in response to Rg3() treatment in senescent HDFs in a time-dependent manner.

CONCLUSION

Our proteomic approach provides insights into the partial reversing effect of Rg3 on senescent HDFs through induction of antioxidant enzymes, particularly PRDX3.