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(T/EH049) HSP90 as a marker for potentially endocrine disrupting processes in crustacea? Preuß, Thomas1, Schill, Ralph1, Woitschella, Astrid1, Nagel, Roland2, Triebskorn, Rita 1,3, Köhler, Heinz-R.1, 1 2 3 ABSTRACT- The 90 kDa stress protein HSP90 belongs to the heat shock protein family. HSP90 is phylogenetically highly conserved. In contrast to other heat shock proteins, HSP90 has some chaperone-like activity for particular molecules involved in signal transduction, such as steroid receptors and various kinases. Since endocrine disruptors in most cases attack steroid receptors, like the estrogen or progesterone receptor and, on the other hand, HSP90 modulates the signal transduction by these proteins, HSP90 might be a useful tool to detect endocrine disrupting effects in a varity of species, including invertebrates, like the freshwater crustacean Gammarus fossarum (Amphipoda). Since HSP90 has several functions, even under non-stress conditions, it is present in the cells in high concentration. Therefore, a suggestive conclusion on the disruption of HSP90-receptor interactions can only be made after separating free from steroid receptor - bound HSP90. By using Native PAGE followed by Western blotting it is possible to separate the complexed from the free HSP90. Asuming that the interaction of a potential endocrine disruptor with the steroid receptor will increasingly release HSP90 from its complex, an oberseved shift in intensity from the protein bands for complexed towards free HSP90 (in comparison to controls) can be used as a marker response for the presence and action of potentially endocrine disrupting chemicals. This study is part of the XEHOGAMM projekt (funded by the Umweltbundesamt, FKZ 29965221/05) which will be presented by Jungmann et al. as poster presentation. Key words: HSP90, endocrine disruption, Native PAGE, Western Blot |
