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

ECU Author/Contributor (non-ECU co-authors, if there are any, appear on document)
Jordan M.,Verkerke,Anthony R.P.,Maschek,J. Alan,Ferrara,P Johnson (Creator)
Institution
East Carolina University (ECU )
Web Site: http://www.ecu.edu/lib/

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.

Additional Information

Publication
Other
Language: English
Date: 2019

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TitleLocation & LinkType of Relationship
Alternative splicing of UCP1 by non-cell-autonomous action of PEMThttp://hdl.handle.net/10342/8309The described resource references, cites, or otherwise points to the related resource.