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
Title | Location & Link | Type of Relationship |
Alternative splicing of UCP1 by non-cell-autonomous action of PEMT | http://hdl.handle.net/10342/8309 | The described resource references, cites, or otherwise points to the related resource. |