To investigate whether heat stress attenuates skeletal muscle atrophy of the extensor digitorum longus (EDL) muscle in streptozotocin-induced diabetic rats, 12-week-old male Wistar rats were randomly assigned to four groups (n = 6 per group): control (Con), heat stress (HS), diabetes mellitus (DM), and diabetes mellitus/heat stress (DM + HS). Diabetes was induced by intraperitoneal injection of streptozotocin (50 mg/kg). Heat stress was induced in the HS and DM + HS groups by immersion of the lower half of the body in hot water at 42 °C for 30 min; it was initiated 7 days after injection of streptozotocin, and was performed once a day, five times a week for 3 weeks. The muscle fiber cross-sectional area of EDL muscles from diabetic and non-diabetic rats was determined; heat stress protein (HSP) 72 and HSP25 expression levels were also analyzed by western blotting. Diabetes-induced muscle fiber atrophy was attenuated upon heat stress treatment in diabetic rats. HSP72 and HSP25 expression was upregulated in the DM + HS group compared with the DM group. Our findings suggest that heat stress attenuates atrophy of the EDL muscle by upregulating HSP72 and HSP25 expression.Keywords: extensor digitorum longus muscle, heat stress, HSP72, HSP25, skeletal muscle atrophy, streptozotocin-induced diabetes Diabetes mellitus (DM) induces skeletal muscle atrophy (7, 19) and decreases muscle strength (7, 9). Consequently, patients with diabetes have a higher risk of falls because of reduced muscle strength (8, 16) and DM-induced-muscle atrophy. Where DM induces skeletal muscle atrophy, fast-twitch fibers are prone to greater atrophy than are slow-twitch fibers (1). Fast-twitch fibers are responsible for high force/power/speed production and maintaining physical balance during postural perturbation. Hence, atrophy of fast-twitch muscle increases the risk of falling in DM patients. Therefore, an efficient strategy is required to attenuate muscle atrophy in order to reduce the risk of falls in DM patients. Heat shock proteins (HSPs) have a protective effect on muscle atrophy. Senf et al. reported that HSP70 overexpression prevented rat soleus muscle fiber atrophy induced by hind limb immobilization (18). Furthermore, overexpression of HSP27 also prevented muscle fiber atrophy of the soleus muscle induced by disuse in rats (5). HSPs are expressed in response to several types of stress such as heat (14, 15) and exercise (12). Exercise increased HSP72 expression (2) and attenuated skeletal muscle fiber atrophy (3) in streptozotocin