| First Author | Ding Y | Year | 2020 |
| Journal | Biochem Biophys Res Commun | Volume | 521 |
| Issue | 3 | Pages | 786-790 |
| PubMed ID | 31706571 | Mgi Jnum | J:291762 |
| Mgi Id | MGI:6445427 | Doi | 10.1016/j.bbrc.2019.10.192 |
| Citation | Ding Y, et al. (2020) Sulfhydration of perilipin 1 is involved in the inhibitory effects of cystathionine gamma lyase/hydrogen sulfide on adipocyte lipolysis. Biochem Biophys Res Commun 521(3):786-790 |
| abstractText | Hydrogen sulfide (H2S) is a novel adipokine mediating glucose uptake, lipid storage and mobilization, thus contributing to the genesis of obesity and associated diseases. Our previous work demonstrated that H2S inhibited isoproterenol-stimulated lipolysis by reducing the phosphorylation of perilipin 1 (plin-1), a lipid-droplet protein blocking lipase access. How H2S modulates plin-1 phosphorylation is still unclear. Our present study found that an H2S donor slightly increased adipose tissue weight and reduced lipolysis in mice; by contrast, deleting the key H2S generation enzyme cystathionine gamma lyase (CSE) in adipocytes lowered adipose accumulation and enhanced lipolysis. Intriguingly, an H2S donor induced sulfhydration of plin-1 but not hormone-sensitive lipase, and CSE deletion abolished the post-translational modification of plin-1. During isoproterenol-stimulated lipolysis, plin-1 sulfhydration was associated with reduced phosphorylation, and removing sulfhydration by dithiothreitol recovered the phosphorylation. Finally, plin-1 knockout abolished the effect of H2S on lipolysis, which indicates that plin-1 sulfhydration is a major direct target of H2S in lipolysis. We have identified a new post-translation modification, sulfhydration (direct action by H2S) of plin-1, causing reduced phosphorylation then decreased lipolysis. This finding also highlights a novel molecular regulatory mechanism of lipolysis. |
