Stress Proteins in the Cellular Response to Ultraviolet Radiation

Virtually all cells-from prokaryotes to highly differentiated mammalian tissues-respond to a sudden increase in temperature with increased production of a limited set of proteins, called heat shock proteins or stress proteins (hsp). Other stress factors such as alcohol, heavy metals, oxidants and agents leading to protein denaturation are equally able to induce a similar response. Induction of hsp is followed by a transient state of increased resistance to further stress. Many hsp function as "molecular chaperones" by binding to partially folded or misfolded proteins thus preventing their irreversible denaturation during stress exposure. The high evolutionary conservation of this reaction suggests its importance for the survival of cells and tissues under hostile environment conditions. Ultraviolet radiation (UV) exerts many potentially harmful effects on prokaryotic and eukaryotic cells and hsp may help the cell to cope with UV-induced damage. This review will focus on the role of hsp in the cellular response of mammalian skin to UV. Hsp have been detected in resting as well as stress exposed epidermal and dermal cells and experimental evidence points to the fact that these proteins mediate protection from UV induced cell death in vitro and in vivo. Experimental studies further indicate that UV itself might be able to induce the expression of specific hsp. Thus, hsp might provide an adaptive cellular response to increasing exposure to UV. Furthermore, UV-activation of hsp synthesis may provide a valuable model for investigation of the transcription regulation of UV-induced gene expression.