Health, Exercise, and Sports Sciences ETDs

Publication Date



Proteins play a critical role in nearly every biological activity. In consequence, organismal health and homeostasis often hinges on the ability of intracellular regulatory systems to sustain the quality and function of these diverse, structurally complex macromolecules. Correct protein function depends on correct form, and during periods of destabilizing cellular stress, protein quality is managed in part by the heat shock response, which acts to support, isolate, and reform new or damaged proteins, and in part by the autophagic recycling of abnormal proteins, cytotoxic protein aggregates, and terminally damaged organelles. We conducted a pooled analysis of available research in humans and rodents regarding heat shock and autophagic activity through the unique proteostatic challenges presented by acute exercise and the post-exercise progression from catabolism to anabolism. This analysis reinforces a model of regulatory coordination between these protein management pathways, offering interspecies support for an Hsp70-moderated transition away from the presiding catabolic influence of autophagy in the immediate post-exercise window, toward an anabolic phase of restoration and remodeling. This relationship has been demonstrated with direct human cellular research, and may help shed light on the molecular underpinning of epidemiological associations between health and physical activity. Differential responses were also observed in these two primary proteostatic systems according to exercise intensity and tissue of origin, which may have important implications for research design, and perhaps eventually for exercise prescription.


Autophagy, Heat Shock Response, Exercise, Hsp70, LC3, Humans, Animals

Document Type




Degree Name

Physical Education

Level of Degree


Department Name

Health, Exercise, and Sports Sciences

First Committee Member (Chair)

Myers, Orrin B.

Second Committee Member


Third Committee Member