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003 OCoLC;

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006 m o d ;

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008 160829s2016 ncua obm 000 0 eng d;

035 a| (Sirsi) o957491634;

035 a| (OCoLC)957491634;

049 a| EREE;

090 a| QP321;

100 1 a| Turner, Kristen D.,e| author.=| ^A1308210;

245 10 a| Effects of high-insulin exposure on mitochondrial content in skeletal muscle myotubes from lean & severely obese individuals :b| a time course analysis /c| by Kristen D. Turner.;

264 1 a| [Greenville, N.C.] :b| [East Carolina University],c| 2016.;

300 a| 74 pages :b| illustrations;

336 a| textb| txt2| rdacontent;

337 a| computerb| c2| rdamedia;

338 a| online resourceb| cr2| rdacarrier;

347 a| text fileb| PDFc| 2.47 MB2| rda;

538 a| System requirements: Adobe Reader.;

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

502 b| M.S.c| East Carolina Universityd| 2016.;

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

500 a| Advisor: Joseph A. Houmard.;

500 a| Title from PDF t.p. (viewed September 27, 2016).;

520 3 a| Skeletal muscle is the site at which highly regulated energetic processes take place as a means of maintaining both tissue-specific and whole-body metabolism. With the development of severe obesity (BMI [greater-than] or equal to 40 kg/m2), skeletal muscle often loses its ability to properly respond to insulin, which aside from regulating glucose, has also been suggested to regulate factors specific to mitochondrial biogenesis. In this study, we classified human skeletal muscle cells (HSkMCs) derived from lean and severely obese individuals. We found them to be strikingly similar with respect to their proliferation and differentiation behavior. Also, to test the hypothesis that insulin would increase proteins associated with mitochondrial biogenesis, mature myotubes were treated with 100nM insulin at time points ranging from 1-24 hours. To validate our model, we incorporated a number of methodologies, including measures of AKT phosphorylation, which we found to be 51% lower in the obese group at the first hour (p = 0.05). However, 100nM insulin produced no changes in protein content of PGC-1[alpha], nor OXPHOS proteins, Complex V or Complex III. This high-insulin treatment did result in increases in Complex IV at 3 hours (p = 0.02), as well as the slow isoform of MYHC (at multiple time points) in both groups. We also observed trends for decreases in intracellular ATP at 24 hours of high-insulin treatment in both lean and severely obese groups. Collectively, these data demonstrate that insulin produces no consistent increases in mitochondrial biogenesis as defined by PGC-1[alpha] and OXPHOS proteins in myotubes from lean and severely obese individuals. We further conclude that the responses to sustained, high-insulin exposure in these groups are alike as it relates to increases in protein synthesis (i.e., MYHC (slow)) at the rather costly expense of ATP.;

504 a| Includes bibliographical references.;

650 0 a| Muscle cells.=| ^A314031;

650 0 a| Insulin.=| ^A3807;

650 0 a| Mitochondriax| Formation.=| ^A1317930;

650 0 a| Satellite cells.=| ^A492646;

650 0 a| Proteinsx| Synthesis.=| ^A204728;

650 0 a| Obesity.=| ^A409;

653 a| human;

653 a| skeletal muscle;

653 a| cell culture;

653 a| severe obesity;

653 a| PGC-1a;

653 a| AKT;

653 a| myosin heavy chain;

653 a| ATP;

653 a| glucose;

653 a| lactate;

700 1 a| Houmard, Joseph A.,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/10342/5918;

949 o| wjh;

994 a| C0b| ERE;

596 a| 1 4;

998 a| 4511357;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 4511357-1001l| JNETm| JOYNERr| Ys| Yt| JNE3ETDu| 8/29/2016x| ETDz| JERESOURCE;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 4511357-2001l| HSLELECm| HSLr| Ys| Yt| HEETDu| 8/29/2016x| ETDz| HERESOURCE;

Effects of high-insulin exposure on mitochondrial content in skeletal muscle myotubes from lean & severely obese individuals : a time course analysis / by Kristen D. Turner.

Author/creator	Turner, Kristen D. author.
Other author	Houmard, Joseph A., degree supervisor.
Other author	East Carolina University. Department of Kinesiology.
Format	Theses and dissertations
Publication	[Greenville, N.C.] : [East Carolina University], 2016.
Description	74 pages : illustrations
Supplemental Content	Access via ScholarShip
Subjects	Muscle cells. Insulin. Mitochondria--Formation. Satellite cells. Proteins--Synthesis. Obesity.

Summary	Skeletal muscle is the site at which highly regulated energetic processes take place as a means of maintaining both tissue-specific and whole-body metabolism. With the development of severe obesity (BMI [greater-than] or equal to 40 kg/m2), skeletal muscle often loses its ability to properly respond to insulin, which aside from regulating glucose, has also been suggested to regulate factors specific to mitochondrial biogenesis. In this study, we classified human skeletal muscle cells (HSkMCs) derived from lean and severely obese individuals. We found them to be strikingly similar with respect to their proliferation and differentiation behavior. Also, to test the hypothesis that insulin would increase proteins associated with mitochondrial biogenesis, mature myotubes were treated with 100nM insulin at time points ranging from 1-24 hours. To validate our model, we incorporated a number of methodologies, including measures of AKT phosphorylation, which we found to be 51% lower in the obese group at the first hour (p = 0.05). However, 100nM insulin produced no changes in protein content of PGC-1[alpha], nor OXPHOS proteins, Complex V or Complex III. This high-insulin treatment did result in increases in Complex IV at 3 hours (p = 0.02), as well as the slow isoform of MYHC (at multiple time points) in both groups. We also observed trends for decreases in intracellular ATP at 24 hours of high-insulin treatment in both lean and severely obese groups. Collectively, these data demonstrate that insulin produces no consistent increases in mitochondrial biogenesis as defined by PGC-1[alpha] and OXPHOS proteins in myotubes from lean and severely obese individuals. We further conclude that the responses to sustained, high-insulin exposure in these groups are alike as it relates to increases in protein synthesis (i.e., MYHC (slow)) at the rather costly expense of ATP.
General note	Presented to the faculty of the Department of Kinesiology
General note	Advisor: Joseph A. Houmard.
General note	Title from PDF t.p. (viewed September 27, 2016).
Dissertation note	M.S. East Carolina University 2016.
Bibliography note	Includes bibliographical references.
Technical details	System requirements: Adobe Reader.
Technical details	Mode of access: World Wide Web.

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Effects of high-insulin exposure on mitochondrial content in skeletal muscle myotubes from lean & severely obese individuals : a time course analysis / by Kristen D. Turner.

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