Alternative splicing of UCP1 by non-cell-autonomous action of PEMT

dc.contributor.author	Johnson, Jordan M.
dc.contributor.author	Verkerke, Anthony R.P.
dc.contributor.author	Maschek, J. Alan
dc.contributor.author	Ferrara, Patrick J.
dc.contributor.author	Lin, Chien-Te
dc.contributor.author	Kew, Kimberly A.
dc.contributor.author	Neufer, P. Darrell
dc.contributor.author	Lodhi, Irfan J.
dc.contributor.author	Cox, James E.
dc.contributor.author	Funai, Katsuhiko
dc.date.accessioned	2020-04-21T18:44:09Z
dc.date.available	2020-04-21T18:44:09Z
dc.date.issued	2019-11-08
dc.description.abstract	Phosphatidylethanolamine methyltransferase (PEMT) generates phosphatidylcholine (PC), the most abundant phospholipid in the mitochondria and an important acyl chain donor for cardiolipin (CL) biosynthesis. Mice lacking PEMT (PEMTKO) are cold-intolerant when fed a high-fat diet (HFD) due to unclear mechanisms. The purpose of this study was to determine whether PEMT-derived phospholipids are important for the function of uncoupling protein 1 (UCP1) and thus for maintenance of core temperature.	en_US
dc.identifier.doi	10.1016/j.molmet.2019.10.007
dc.identifier.uri	http://hdl.handle.net/10342/8309
dc.title	Alternative splicing of UCP1 by non-cell-autonomous action of PEMT	en_US
dc.type	Article	en_US
ecu.journal.name	Alternative splicing of UCP1 by non-cell-autonomous action of PEMT	en_US
ecu.journal.pages	55-66	en_US
ecu.journal.volume	31	en_US

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