Access to abstract permanently restricted to Ball State community only / Access to thesis permanently restricted to Ball State community only / School of Physical Education, Sport, and Exercise Science

There is no abstract available for this thesis. / School of Physical Education

Blainville (1835) wrote the first description of a sand lizard and named it Callisaurus draconoides. Since his time various authors have published articles concerning sand lizards. Girard (1851) described Holbrookia maculata, Trochel (1852) described Cophosaurus texanus, and that same year Baird and Girard synonymized Cophosaurus with Holbrookia providing the name Holbrookia texana, which has stood for over 100 years. Subsequently, Baird (1858) described Uma notata.

The primary focus of this study was to determine basal levels of myogenic (MRF4, myogenin, MyoD), proteolytic (FOXO3A, atrogin-1, MuRF-1), myostatin, and mitochondrial (PGC-1α & Tfam) mRNA in elderly women before and after aerobic training. This approach was taken to gain insight into the molecular adaptations associated with our observed increases in whole muscle cross sectional area (CSA) (11%, p<0.05), knee extensor muscle function (25%, p<0.05) and aerobic capacity (30%, p<0.05) with training. Nine elderly women (71±2y) underwent muscle biopsies obtained from the vastus lateralis before and after 12-weeks of aerobic training on a cycle ergometer. Post training biopsy samples were acquired 48 hours after the last exercise session. Aerobic training reduced (p < 0.05) resting levels of MRF4 by 25% while myogenin showed a trend to decrease (p = 0.09) after training. FOXO3A expression was 27% lower (p < 0.05) while atrogin-1 and MuRF-1 were unaltered after training. Additionally, myostatin gene expression was decreased (p < 0.05) by 57% after training. Lastly, aerobic training did not alter PGC-1α or Tfam mRNA. These findings suggest that aerobic training alters basal transcript levels of growth related genes in skeletal muscle of older women. Further, the reductions in FOXO3A and myostatin indicate the aerobic training induced muscle hypertrophy in older women may be due to alterations in proteolytic machinery. / School of Physical Education, Sport, and Exercise Science

Access to abstract permanently restricted to Ball State community only / Access to thesis permanently restricted to Ball State community only / School of Physical Education, Sport, and Exercise Science

Exercise induces morphological and metabolic adaptations that are highly specific to the mode of exercise training. These specific phenotypical changes are due to an equally specific molecular response that may depend on the activation and coordination intramuscular signaling pathways. Just as metabolic and morphological changes are influenced by the mode of exercise training, the signaling pathways that mediate exercise adaptation may also be directly related to the training status of skeletal muscle. For example, pre-conditioned skeletal muscle may exhibit a specific intracellular signaling response to an acute bout of exercise that is dependent on past training history. Both Akt (protein kinase B) and extra-cellular signal-related kinase (ERK 1 /2) have been shown to be phosphorylated in response to an acute bout of resistance exercise in human skeletal muscle and have been suggested to mediate the adaptive response to exercise. The purpose of this investigation was to examine the response of Akt and ERKI/2 to an acute bout of resistance exercise in three groups with distinctly different exercise training backgrounds. Twenty one subjects performed 3 sets of 10 repetitions of knee extension exercise at 70% 1-RM. The subjects consisted of a resistance-trained group (RE) (n=7), endurance trained group (END) (n=7) and a sedentary group (SED) (n=7). Muscle biopsies were taken from the vastus lateralis muscle before, immediately after, and 10 min post-exercise and were analyzed for phosphorylation of Akt and ERK1/2. ERK1/2 phosphorylation increased 47%, and 54% from pre-exercise to immediately post-exercise in the SED and RE groups respectively (p < 0.05). ERK1/2 phosphorylation increased 95%, 196%, and 47% from pre-exercise to 10 min post-exercise in the SED, RE, and END groups, respectively. (p < 0.05). The magnitude of ERK1/2 phosphorylation 10 min post-exercise was different between each group and may be linked to the group's training status. (p < 0.05) Akt phosphorylation decreased 42% and 37% from pre-exercise to immediately post-exercise in the SED and END group, respectively (p < 0.05). There was a 40 % increase in Akt phosphorylation from immediate post-exercise to 10 min post-exercise in the END group. In conclusion, training status appears to influence the magnitude and time course of activation of both Akt and ERK1/2 in response to an acute bout of resistance exercise. The immediate response of both ERK1/2 and Akt may play a key role in the adaptive response of skeletal muscle ultimately resulting in metabolic and morphological changes that are dependent on the past training history of the individual. / School of Physical Education, Sport, and Exercise Science

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Little is known about protein profiles in slow-twitch (MHC I) and fast-twitch (MHC IIa and MHC IIx) human skeletal muscle fibers. Therefore we developed a method of assessing fiber type specific protein content across the continuum of human skeletal muscle fiber types. The method presented here combines the advantages of SDS-PAGE for fiber typing with the common Western Blot (WB) technique. Individual vastus lateralis muscle fibers (n = 264) were isolated and clipped into two portions, one for fiber-typing and one for protein identification. Following fiber type determination, WB destined fiber segments were combined into fiber type specific pools (20 fibers/pool) and assessed for GAPDH, actin, Citrate Synthase, and total p38 content. GAPDH expression was 69%, 92%, 159%, and 200% more abundant in MHC I/IIa, MHC IIa, MHC IIa/IIx, and MHC IIx pools when compared to MHC I, respectively. Inversely, Citrate synthase content was 526%, 497%, 316%, and 47% more abundant in MHC I, MHC I/IIa, MHC IIa, and MHC IIa/IIx when compared to MHC IIx, respectively. Similar to GAPDH, total p38 expression was 67% greater in MHC IIa versus MHC I fibers. These data establish a novel application of WB combined with SDS-PAGE for fiber type specific protein analysis in human skeletal muscle. These initial results show content of particular proteins exist in a hierarchal fashion throughout the continuum of human skeletal muscle fiber types. Application of these methods will enhance our understanding of skeletal muscle health profiles among physically active and clinically based populations. / Access to thesis permanently restricted to Ball State community only / School of Physical Education, Sport, and Exercise Science

Access to abstract permanently restricted to Ball State community only. / Access to dissertation permanently restricted to Ball State community only. / School of Physical Education, Sport, and Exercise Science

Cyclooxygenase (COX) is the enzyme that catalyzes the rate-limiting step in prostaglandin (PG) synthesis. In skeletal muscle, PGF2a, has been shown to regulate protein synthesis, and ibuprofen and acetaminophen have been shown to block the normal increase in PGF2a and muscle protein synthesis following resistance exercise in humans. The purpose of this investigation was to determine the expression of the COX-1 (COX-1 variants: COX-1 v1, -1v2, -1 b,, -1 b2, and -1b3) and COX-2 isoforms following resistance exercise to help elucidate the isoform or variant through which PGF2a, ibuprofen, and acetaminophen regulate muscle protein synthesis. Human skeletal muscle biopsy samples were taken from 16 individuals (8M, 8F) before, 4 h, and 24 h following a single bout of resistance exercise and analyzed using real-time RT-PCR. COX-Iv1 and COX-1v2 were the most abundant COX mRNA before exercise and remained unchanged (P>0.05) following exercise (i.e., constitutively expressed). Relatively few individuals expressed the intron 1-retaining COX-1 b variants (COX-1 b,, - 1b2, and -1 b3) at any time point, and when expressed these variants were in very low abundance. COX-2 was not expressed in any subject before exercise, but increased significantly (P<0.05) at 4 and 24 h following exercise. These results suggest that the intron 1-retaining COX-1 b,, -1 b2, and -lb3 variants are likely not the COX through which PGF2a is produced to stimulate skeletal muscle protein synthesis. PGF2a, stimulation, as well as ibuprofen and acetaminophen inhibition of skeletal muscle protein synthesis likely work through COX-2, or one of the constitutively expressed COX-1 variants (COX-lv1 or -1v2). / School of Physical Education, Sport, and Exercise Science