Aging, physical inactivity, and obesity are all strongly associated with the onset of insulin resistance (IR). IR marks an early defect in the regulation of blood glucose resulting in type 2 diabetes. Very little is known about the cellular mechanisms regulating insulin sensitivity in skeletal muscle; however, IR is strongly regulated by the activation of a stress molecule known as c-jun N terminal kinase (JNK). We have shown that JNK is highly activated in the skeletal muscle of elderly rodents and rodents fed a high fat diet. Our data implicate increased activation of JNK as a primary factor in causing IR. One of the body’s major defense mechanisms against stress is the induction of heat shock protein 70 (Hsp70). Interestingly, the resting expression of Hsp70 and its production in response to cellular stress is severely attenuated in models of aging and IR. To elucidate the role of Hsp70 in IR, we inhibited the expression of Hsp70, which resulted in reduce glucose uptake by the skeletal muscle. Our pilot data demonstrates that stimulating Hsp70 production in IR skeletal muscle can directly inhibit the activation of JNK. Hsp70 mediated inhibition of JNK significantly improved skeletal muscle insulin sensitivity. Lastly, our data has been the first to show that Hsp70 induction in human skeletal muscle is possible using a simple passive heating therapy. These findings suggest that Hsp70 may serve as a novel, easily implemented, therapeutic countermeasure to IR and thus may play a role in the prevention of diabetes.