The results of our study demonstrated that

The results of our study demonstrated that HSL activation by kinsenoside-mediated PKA activation was coordinated with perilipin phosphorylation and facilitated efficient lipolysis, resulting in increased glycerol release and decreased lipid accumulation. The localization and interplay of perilipin and HSL in lipolysis remain unclear; the literature presents contradictory results on this topic. Studies have reported that phosphorylated perilipin dissociates from LDs before HSL catalyzes hydrolysis. However, other research groups comparing these perilipin and HSL interactions to those in isoproterenol stimulation in young and old mice have stated that perilipin\'s dissociation from and HSL\'s binding to the surface of LDs are not necessarily sequential events. Such groups have observed that lipid hydrolysis requires only HSL to dock on the surface of LDs, independent of perilipin subcellular localization. Additionally, studies have proposed that perilipin may serve as a docking protein for the function of HSL (Egan et al., 1992), although other studies have shown that no such protein–protein interaction occurs in a Co-IP and yeast two-hybrid system (Clifford et al., 2000, Shen et al., 1999). Furthermore, one study showed that norepinephrine induced lipolysis in rat fat wnt inhibitor and that this induction of lipolysis was dependent on the localization of pHSL to the LD surface and independent of the level and activity of pHSL-Ser660/563 (Morimoto et al., 2001). Hence, the mechanism underlying the interplay of HSL and perilipin in TG hydrolysis requires further verification. To the best of our knowledge, this study was the first to demonstrate in vitro and in vivo that the lipolytic effect of kinsenoside results from coordination between PKA and AMPK pathways. We validated the lipolytic effect of kinsenoside in vivo and the effect of PKA activation on the modulating AMPK function for FA hydrolysis through HSL and perilipin activation.
Conclusion This study indicated that in addition to activating AMPK, kinsenoside activated HSL and perilipin through a PKA-dependent mechanism to facilitate lipolysis and to reduce fat accumulation both in vitro and in vivo. Thus, kinsenoside could be a promising adjuvant for the prophylaxis of obesity-associated complications.
Introduction Throughout evolution, animals have developed such that excess fats and sugars not immediately required for energy are stored. This biological function, invaluable for survival during times of scarce food and famine, has become less practical in the developed world, where sustenance abounds. The excess triglyceride storage resulting from the modern influx of nutrient-rich foods has become the foundation for metabolic diseases such as obesity. A better understanding of the mechanisms by which fat storage is regulated may prove to be medically indispensable for such diseases. In mammals, triglycerides are stored within structures known as lipid droplets [1]; however, much is still unknown about how lipid droplet formation and morphology is regulated. In an attempt to identify genes involved in this process, genome-wide RNAi screens have been performed in Drosophila cell culture since lipid droplet structure is well conserved from flies to humans [2], [3]. These screens identified several classes of genes that when knocked down generated visible and quantifiable lipid droplet morphology phenotypes. One subset of these genes included various components of the spliceosome.