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003 OCoLC;

005 20160329120808.0;

006 m o d ;

007 cr unu||||||||;

008 160129s2015 ncua obm 000 0 eng d;

035 a| (Sirsi) o936213515;

035 a| (OCoLC)936213515;

049 a| EREE;

090 a| QP751;

100 1 a| Ferrara, Patrick Joseph,e| author.?| UNAUTHORIZED;

245 10 a| Deletion of LPCAT3 promotes enhanced insulin signaling in skeletal muscle /c| Patrick Joseph Ferrara.;

264 1 a| [Greenville, N.C.] :b| [East Carolina University],c| 2015.;

300 a| 65 pages :b| illustrations;

336 a| textb| txt2| rdacontent;

337 a| computerb| c2| rdamedia;

338 a| online resourceb| cr2| rdacarrier;

347 a| text fileb| PDFc| 6.32 MB2| rda;

538 a| System requirements: Adobe Reader.;

538 a| Mode of access: World Wide Web.;

502 b| M.S.c| East Carolina Universityd| 2015.;

500 a| Presented to the faculty of the Department of Kinesiology.;

500 a| Advisor: Katsuhiko Funai.;

500 a| Title from PDF t.p. (viewed March 7, 2016).;

504 a| Includes bibliographical references.;

520 3 a| Aberrant lipid metabolism has been linked to skeletal muscle insulin resistance. The exact identity of the lipid species that promote skeletal muscle insulin resistance among the human population remains unclear. In this study we utilized primary muscle cells isolated from lean-insulin sensitive (LN) or obese insulin-resistant (OB) individuals to characterize differences in the muscle lipidome free of contaminating cell types. OB muscles contained lower levels of various species of lysophospholipids (lyso-PLs) compared to LN, a finding that has never been previously described. RNAseq experiments in the same set of samples identified three genes involved in lyso-PL metabolism (PPAP2A, LPIN3, and LPCAT3) to have greater expression in OB vs. LN. Strikingly, lentivirus-mediated deletion of LPCAT3 in C2C12 myotubes resulted in increased insulin signaling (phosphorylation of IR, Akt, AS160) in the absence of, and at various concentrations of insulin. LPCAT3 deletion had no effect on cell morphology, myotube differentiation, fiber type, or abundance of enzymes of the electron transport chain. Future studies should focus on the cellular mechanisms by which LPCAT3 affects IR phosphorylation.;

650 0 a| Lipidsx| Metabolism.=| ^A5881;

650 0 a| Insulin resistance.=| ^A251831;

653 a| Insulin signaling;

653 a| Phospholipid;

653 a| Lysophospholipid;

653 a| Skeletal Muscle;

700 1 a| Funai, Katsuhiko,e| degree supervisor.?| UNAUTHORIZED;

710 2 a| East Carolina University.b| Department of Kinesiology.?| UNAUTHORIZED;

856 40 z| Access via ScholarShipu| http://hdl.handle.net/10342/5136;

949 a| Click on web addressw| ASISh| JOYNER101;

949 a| Click on web addressw| ASISh| HSL111;

949 o| wjh;

994 a| C0b| ERE;

596 a| 1 4;

998 a| 4356323;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 4356323-1001l| JNETm| JOYNERr| Ys| Yt| JNE3ETDu| 1/29/2016x| ETDz| JERESOURCE;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 4356323-2001l| HSLELECm| HSLr| Ys| Yt| HEETDu| 1/29/2016x| ETDz| HERESOURCE;

Deletion of LPCAT3 promotes enhanced insulin signaling in skeletal muscle / Patrick Joseph Ferrara.

Author/creator	Ferrara, Patrick Joseph author.
Other author	Funai, Katsuhiko, degree supervisor.
Other author	East Carolina University. Department of Kinesiology.
Format	Theses and dissertations
Publication	[Greenville, N.C.] : [East Carolina University], 2015.
Description	65 pages : illustrations
Supplemental Content	Access via ScholarShip
Subjects	Lipids--Metabolism. Insulin resistance.

Summary	Aberrant lipid metabolism has been linked to skeletal muscle insulin resistance. The exact identity of the lipid species that promote skeletal muscle insulin resistance among the human population remains unclear. In this study we utilized primary muscle cells isolated from lean-insulin sensitive (LN) or obese insulin-resistant (OB) individuals to characterize differences in the muscle lipidome free of contaminating cell types. OB muscles contained lower levels of various species of lysophospholipids (lyso-PLs) compared to LN, a finding that has never been previously described. RNAseq experiments in the same set of samples identified three genes involved in lyso-PL metabolism (PPAP2A, LPIN3, and LPCAT3) to have greater expression in OB vs. LN. Strikingly, lentivirus-mediated deletion of LPCAT3 in C2C12 myotubes resulted in increased insulin signaling (phosphorylation of IR, Akt, AS160) in the absence of, and at various concentrations of insulin. LPCAT3 deletion had no effect on cell morphology, myotube differentiation, fiber type, or abundance of enzymes of the electron transport chain. Future studies should focus on the cellular mechanisms by which LPCAT3 affects IR phosphorylation.
General note	Presented to the faculty of the Department of Kinesiology.
General note	Advisor: Katsuhiko Funai.
General note	Title from PDF t.p. (viewed March 7, 2016).
Dissertation note	M.S. East Carolina University 2015.
Bibliography note	Includes bibliographical references.
Technical details	System requirements: Adobe Reader.
Technical details	Mode of access: World Wide Web.

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Deletion of LPCAT3 promotes enhanced insulin signaling in skeletal muscle / Patrick Joseph Ferrara.

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