We have shown that Akt and IKK α Adrenergic Receptors expression and nuclear translocation of NF jB is reduced by 17 DMAG at concentrations that induce cell death does not know. In order to confirm to that these effects were induced by the inhibition of HSP90, we tested several markers of HSP90 inhibition. If HSP90 is not bound to a protein of the customer, binds to HSF1 HSP90 and other chaperone proteins Co. When a protein binds to HSP90 or HSP90 client is blocked, activated HSF1 and chaperone co released from the complex. Activated HSF1 translocation into the nucleus where it react the transcription of heat shock proteins with heat shock protein 70th Erh Hen of HSP70 and translocation of HSF1 h Are frequently used as indicators for the inhibition of HSP90. There is some discrepancy in the literature on the effects of Hsp90 inhibitors on the tats Chlichen expression of HSP90 itself. A report by Clark et al. Al showed a reduced expression of HSP90 inhibition by GA following. Reports of Al Madrigal and Matute. and Ghoshal et al. did not show change of HSP90 expression after inhibition of 17 DMAG. In our studies, we have not Ver Changes in the expression of HSP90 with 17 DMAG independent Ngig observed by cell activation with LPS / IFN-c. This leads us to the conclusion that 17 DMAG does not affect all levels of HSP90 protein. However, we observed an increase of the nucleon Ren translocation of HSF1, which we interpret as an indication of HSP90 inhibition. It was also an increase of HSP70 in response to treatment with 17 DMAG. We interpreted the Erh Increase the expression of HSP70 as a marker of HSP90 inhibition. Taken together, these two markers of HSP90 inhibition, that the anti-inflammatory mechanism of action, a 17-DMAG is based on macrophages in part through inhibition of HSP90. HSP70 is often negatively associated with suppression of apoptosis and the support of pro-inflammatory signaling proteins.
In contrast to this idea was also demonstrated that HSP70 and other HSPs are active by cancer cells and / or passively secreted from necrotic cells as a means of indicating stress and destruction Tion of tissue lost in innate and adaptive immune system. That this signal is an immune HSP70 positive or negative effects of the inflammation is still not completely Ndig determined. It may be that some of the anti-inflammatory effect is the inhibition of HSP90 by erh Hte suppressed expression of HSP70. Has, however, extracellular Ren HSP70 with anti-inflammatory in atherosclerosis, such as the activation of Toll-like receptor 4 on CD4 brought together CD25 Regulatory T cells is believed that the suppressive activity of t hen in atherosclerosis to increased. Although we did not want to show directly that HSP70 inhibited 5 alpha dht IKK activity t in our studies, others have shown that HSP70 has a negative feedback effect jB on the activity t of NF-signaling, perhaps by inhibiting IKK activity. In addition, it has been shown that HSP70 tumor necrosis factor receptor-associated factor 6 to delete. Taken together, these studies suggest increased Hte HSP70 may have an anti-inflammatory and warrants further investigation. Our investigation of the downstream effectors of inflammation, including normal IL-6, TNF and NO. NO production induced by immune stimulation. Recently it was shown that HSP70 may function as an inhibitor of iNOS to k. HSP90 was also.
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