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https://hdl.handle.net/10316/109269
Title: | Dichloroacetate, the Pyruvate Dehydrogenase Complex and the Modulation of mESC Pluripotency | Authors: | Rodrigues, Ana Sofia Correia, Marcelo Gomes, Andreia Pereira, Sandro L. Perestrelo, Tânia Sousa, Maria Inês Ramalho-Santos, João |
Issue Date: | 2015 | Publisher: | Public Library of Science | Project: | The authors thank Fundação para a Ciência e a Tecnologia (FCT) Portugal for grant support (PTDC/EBB-EBI/ 120634/2010 and PDTC/ QUI-BIQ/120652/2010 co-funded by Compete/ FEDER/National Funds; and scholarships attributed to ASR (SFRH/BD/33463/2008); to MC (SFRH/BD/ 51681/2011), to TP (SFRH/BD/51684/2011), AG (SFRH/BD/51968/2012) and SLP (SFRH/BPD/98995/ 2013) and also to QREN (Centro-01-0762-FEDER- 00204). Center for Neuroscience and Cell Biology (CNC) funding is also supported by FCT (PEst-C/ SAU/LA0001/2011) | Serial title, monograph or event: | PLoS ONE | Volume: | 10 | Issue: | 7 | Abstract: | The pyruvate dehydrogenase (PDH) complex is localized in the mitochondrial matrix catalyzing the irreversible decarboxylation of pyruvate to acetyl-CoA and NADH. For proper complex regulation the E1-α subunit functions as an on/off switch regulated by phosphorylation/dephosphorylation. In different cell types one of the four-pyruvate dehydrogenase kinase isoforms (PDHK1-4) can phosphorylate this subunit leading to PDH inactivation. Our previous results with human Embryonic Stem Cells (hESC), suggested that PDHK could be a key regulator in the metabolic profile of pluripotent cells, as it is upregulated in pluripotent stem cells. Therefore, we wondered if metabolic modulation, via inexpensive pharmacological inhibition of PDHK, could impact metabolism and pluripotency. | URI: | https://hdl.handle.net/10316/109269 | ISSN: | 1932-6203 | DOI: | 10.1371/journal.pone.0131663 | Rights: | openAccess |
Appears in Collections: | I&D CNC - Artigos em Revistas Internacionais IIIUC - Artigos em Revistas Internacionais FCTUC Ciências da Vida - Artigos em Revistas Internacionais |
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