Capsaicin partially mimics heat in mouse fibroblast cells in vitro.

Capsaicin activates transient receptor potential vanilloid 1 (TRPV1), a cation channel in the transient receptor potential family, resulting in the transient entry of Ca2+ and Mg2+ and a warm sensation. However, the effects of capsaicin on cells have not fully elucidated in fibroblasts. In this study, we investigated whether capsaicin could induce signal transduction in mouse fibroblast cells and compared the effect with that of heat-induced signal transduction. The activation of the mitogen-activated protein kinases (MAPKs) ERK and p38 MAPK, expression levels of heat shock protein 70 (HSP70) and HSP90, actin assembly, and cell proliferation were analyzed in NIH3T3 mouse fibroblast cells. A 15-min stimulation with capsaicin (∼100 μM) phosphorylated ERK and p38 MAPK and induced actin assembly. A 2-day stimulation with capsaicin increased the level of HSP70, but not HSP90, and the 2-day stimulation with capsaicin (∼100 μM) did not affect cell proliferation. A 15-min exposure to moderate heat (39.5 °C) phosphorylated both ERK and p38 MAPK and induced actin assembly to similar degrees as stimulation with capsaicin. A 2-day exposure to moderate heat increased the levels of both HSP70 and HSP90 and prevented cell proliferation. However, the 2-day stimulation with capsaicin (100 μM) failed to prevent heat shock-induced cell death. Thus, our results suggest that the effects of capsaicin on fibroblast cells partially differ from those of heat. Notably, the 2-day stimulation with capsaicin was not sufficient to develop heat tolerance in fibroblast cells.