| First Author | Tang N | Year | 2020 |
| Journal | Biochem Biophys Res Commun | Volume | 526 |
| Issue | 1 | Pages | 1-7 |
| PubMed ID | 32192773 | Mgi Jnum | J:292012 |
| Mgi Id | MGI:6447406 | Doi | 10.1016/j.bbrc.2020.03.002 |
| Citation | Tang N, et al. (2020) PP2Acalpha inhibits PFKFB2-induced glycolysis to promote termination of liver regeneration. Biochem Biophys Res Commun 526(1):1-7 |
| abstractText | The mechanisms underlying the initiation and proliferation of liver regeneration (LR) has been extensively studied using the partial hepatectomy (PHx) model, while little is known about the termination of LR. PP2Acalpha (protein phosphatase 2 A catalytic subunit alpha isoform) is the catalytic subunit of protein phosphatase 2 A (PP2A), accounting for most of intracellular serine/threonine phosphatase activity. We have previously observed that termination of LR delayed in PP2Acalpha liver-specific knockout (LKO) mice after PHx. In our study, we used phospho explorer antibody array analysis to screen the potential phosphorylation targets of PP2Acalpha, and PP2Acalpha had a great influence on the hepatic phosphoproteomic signaling in the termination of LR after PHx. We then tested the phosphorylation changes and metabolic function of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-2 (PFKFB2), an isoform of the key glycolytic enzyme PFKFB, which was significantly regulated by PP2Acalpha knockout. PP2Acalpha knockout enhanced glycolysis in vivo and in vitro, while adenoviral-mediated RNAi of PFKFB2 reversed the extension of postoperative liver regeneration in KO mice along with the downregulation of glycolysis. Therefore, we demonstrated that PP2Acalpha liver-specific knockout regulated the hepatocytes glycolysis via activating PFKFB2, thus enhancing liver regeneration during the termination stage. |
