Oligonol-induced degradation of perilipin 1 is regulated through lysosomal degradation machinery.

The results obtained from our previous study showed that the addition of a lychee fruit-derived low molecular form of polyphenol, Oligonol, provoked higher levels of lipolytic activity via the degradation of perilipin 1 in primary rat adipocytes. In the current study, we investigated the possible mechanisms by which Oligonol could promote the degradation of perilipin 1 protein. The addition of Oligonol caused the degradation of GFP-tagged perilipin 1 in a time-dependent manner. Meanwhile, the co-addition of Oligonol and NH4CI, a lysosome inhibitor, failed to promote the degradation of perilipin 1, while the co-addition of Oligonol and MG132, a proteasome inhibitor, induced a reduction in the levels of perilipin 1. These results suggest that the Oligonol-induced degradation of perilipin 1 is regulated via a lysosome-dependent mechanism.