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035 a| (OCoLC)747860666;

040 a| EREc| EREd| EREd| UtOrBLW;

049 a| EREE;

090 a| QP552.M85;

100 1 a| Choplin, Eric Seneca.?| UNAUTHORIZED;

245 10 a| Cleaved caspase-3 response to acute resistance exercise in young and old men and women :b| relationship to muscle glycogen content and 5'-AMP-activated protein kinase (AMPK) activity /c| by Eric Seneca Choplin.;

260 a| [Greenville, N.C.] :b| East Carolina University,c| 2011.;

300 a| 94 pages :b| illustrations (some color), digital, PDF file;

336 a| text2| rdacontent;

337 a| computer2| rdamedia;

338 a| online resource2| rdacarrier;

538 a| System requirements: Adobe Reader.;

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

502 b| M.S.c| East Carolina Universityd| 2011.;

500 a| Presented to the faculty of the Department of Exercise and Sport Science.;

500 a| Advisor: Scott Gordon.;

500 a| Title from PDF t.p. (viewed Sept. 20, 2011).;

520 3 a| In addition to suppressing protein synthesis and activating protein degradation in skeletal muscle and other cell types, 5'-AMP-activated protein kinase (AMPK) is known to stimulate nuclear apoptosis in non-muscle cells through cleaved (activated) caspase-3, one of the final steps in the apoptosis cascade. Although it is unknown whether AMPK stimulates caspase-3 cleavage or nuclear apoptosis in skeletal muscle cells in vivo, AMPK activity and nuclear apoptosis are elevated at rest in aged rat skeletal muscle. AMPK phosphorylation and activity are also higher in old vs. young rats and humans in response to overload or resistance exercise. Furthermore, older individuals display lower muscle glycogen content, a condition known to accentuate AMPK activity at rest and during aerobic exercise. We hypothesized that skeletal muscle cleaved caspase-3 content would be higher after acute resistance exercise in older versus younger individuals. Seven young (21.7 + 2.1 yrs) and 11 old (67.0 + 8.6 yrs) subjects performed an acute bout of leg extension resistance exercise. Muscle biopsies were obtained pre-exercise (PRE), immediately post-exercise (0P), 1-hour post-exercise (1P), and 2-hours post-exercise (2P). Glycogen content was measured in muscle samples, as were the phosphorylations (via western blot) of AMPK and acetyl-CoA carboxylase (ACC; a marker of AMPK activity). Procaspase-3 and cleaved (activated) caspase-3 contents were also assessed via western blot. AMPK phosphorylation was significantly (p < 0.05) increased in old, but not young, subjects immediately post-exercise. In both age groups, AMPK activity (assessed by ACC phosphorylation) was elevated vs. PRE at the 0P and 1P time points, and cleaved caspase-3 content was elevated vs. PRE at the 0P, 1P, and 2P time points. However, there was no effect of exercise on procaspase-3 content in either age group, and no differences between age groups in AMPK activity, procaspase-3 content, or cleaved caspase-3 content at any time point. There were significant, or close to significant, relationships between glycogen content and AMPK activity at time points PRE, 0P, and 1P regardless of age. However, no significant correlations between AMPK activity and cleaved caspase-3 content were observed at any time point. In summary, these data indicate that cleaved caspase-3 (e.g., caspase-3 activity) increases in response to acute resistance exercise in both young and old subjects. However, exercise-induced AMPK activation may not be the mechanism by which this occurs.;

504 a| Includes bibliographical references.;

650 0 a| Muscle proteins.=| ^A3712;

650 0 a| Protein kinases.=| ^A396687;

650 0 a| Glycogen.=| ^A231914;

650 0 a| Apoptosis.=| ^A294849;

650 0 a| Musclesx| Aging.=| ^A1002;

653 a| Physiology;

700 1 a| Gordon, Scott Edward.?| UNAUTHORIZED;

710 2 a| East Carolina University.b| Department of Exercise and Sport Science.?| UNAUTHORIZED;

856 40 z| Access via ScholarShipu| http://hdl.handle.net/10342/3652;

949 o| jgml;

994 a| C0b| ERE;

596 a| 1 4;

998 a| 2533124;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 2533124-1001l| JNETm| JOYNERr| Ys| Yt| JNE3ETDu| 8/26/2011x| ETDz| JERESOURCE;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 2533124-2001l| HSLELECm| HSLr| Ys| Yt| HEETDu| 8/26/2011x| ETDz| HERESOURCE;

Cleaved caspase-3 response to acute resistance exercise in young and old men and women : relationship to muscle glycogen content and 5'-AMP-activated protein kinase (AMPK) activity / by Eric Seneca Choplin.

Author/creator	Choplin, Eric Seneca
Other author	Gordon, Scott Edward.
Other author	East Carolina University. Department of Exercise and Sport Science.
Format	Theses and dissertations
Publication Info	[Greenville, N.C.] : East Carolina University, 2011.
Description	94 pages : illustrations (some color), digital, PDF file
Supplemental Content	Access via ScholarShip
Subjects	Muscle proteins. Protein kinases. Glycogen. Apoptosis. Muscles--Aging.

Summary	In addition to suppressing protein synthesis and activating protein degradation in skeletal muscle and other cell types, 5'-AMP-activated protein kinase (AMPK) is known to stimulate nuclear apoptosis in non-muscle cells through cleaved (activated) caspase-3, one of the final steps in the apoptosis cascade. Although it is unknown whether AMPK stimulates caspase-3 cleavage or nuclear apoptosis in skeletal muscle cells in vivo, AMPK activity and nuclear apoptosis are elevated at rest in aged rat skeletal muscle. AMPK phosphorylation and activity are also higher in old vs. young rats and humans in response to overload or resistance exercise. Furthermore, older individuals display lower muscle glycogen content, a condition known to accentuate AMPK activity at rest and during aerobic exercise. We hypothesized that skeletal muscle cleaved caspase-3 content would be higher after acute resistance exercise in older versus younger individuals. Seven young (21.7 + 2.1 yrs) and 11 old (67.0 + 8.6 yrs) subjects performed an acute bout of leg extension resistance exercise. Muscle biopsies were obtained pre-exercise (PRE), immediately post-exercise (0P), 1-hour post-exercise (1P), and 2-hours post-exercise (2P). Glycogen content was measured in muscle samples, as were the phosphorylations (via western blot) of AMPK and acetyl-CoA carboxylase (ACC; a marker of AMPK activity). Procaspase-3 and cleaved (activated) caspase-3 contents were also assessed via western blot. AMPK phosphorylation was significantly (p < 0.05) increased in old, but not young, subjects immediately post-exercise. In both age groups, AMPK activity (assessed by ACC phosphorylation) was elevated vs. PRE at the 0P and 1P time points, and cleaved caspase-3 content was elevated vs. PRE at the 0P, 1P, and 2P time points. However, there was no effect of exercise on procaspase-3 content in either age group, and no differences between age groups in AMPK activity, procaspase-3 content, or cleaved caspase-3 content at any time point. There were significant, or close to significant, relationships between glycogen content and AMPK activity at time points PRE, 0P, and 1P regardless of age. However, no significant correlations between AMPK activity and cleaved caspase-3 content were observed at any time point. In summary, these data indicate that cleaved caspase-3 (e.g., caspase-3 activity) increases in response to acute resistance exercise in both young and old subjects. However, exercise-induced AMPK activation may not be the mechanism by which this occurs.
General note	Presented to the faculty of the Department of Exercise and Sport Science.
General note	Advisor: Scott Gordon.
General note	Title from PDF t.p. (viewed Sept. 20, 2011).
Dissertation note	M.S. East Carolina University 2011.
Bibliography note	Includes bibliographical references.
Technical details	System requirements: Adobe Reader.
Technical details	Mode of access: World Wide Web.

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Cleaved caspase-3 response to acute resistance exercise in young and old men and women : relationship to muscle glycogen content and 5'-AMP-activated protein kinase (AMPK) activity / by Eric Seneca Choplin.

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