Stress goes Far East: meeting report of the Sixth International Workshop on the Molecular Biology of Stress Responses

Abstract

The heat shock response was discovered in 1962 by mistake. F. Ritossa was studying the puffing pattern of Drosophila larvae when he discovered a new pattern 1 day (Ritossa 1962, 1996). It turned out that one of his colleagues had raised the temperature of the incubator from 25°C to 32°C leading to the new puffing pattern—and the heat shock response was born. Twelve years later, A. Tissieres studied the heat shock response at the level of proteins using a method of separating radioactively labeled proteins by the newly developed method of polyacrylamide gel electrophoresis. By comparing the protein pattern of different larval tissues grown either at 25°C or heat-shocked to 32°C, Tissieres detected several proteins present at 32°C but absent or nearly absent at 25°C. He coined the term heat shock proteins (Hsps; Larminat et al. 1992). At the end of the 1970s, the heat shock response was discovered in Escherichia coli (Neidhardt and VanBogelen 1981; Yamamori and Yura 1982), and we know now that it occurs in all organisms, from bacteria to man (Shamovsky and Nudler 2008). We also know that the heat shock response is genetically regulated. Important heat shock proteins are molecular chaperones (Saibil 2008) and adenosine triphosphate (ATP)-dependent proteases (Baker and Sauer 2006). But molecular chaperones also play an important role in causing diseases in humans, animals, and plants (Calderwood 2007). Recent books deal with their role in cancer (Calderwood et al. 2007), in inflammation and immunity (Asea and De Maio 2007), and in neurodegenerative diseases (Asea and Brown 2008).