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Heat shock protein (Hsp70) is an important stress response protein in cells. Since Hsp70 is localized in both cytosol and nucleus in retinal pigment epithelial (RPE) cells, it may play an important role in protecting cells from the damaging effects of stress. The synthesis of Hsp70 is known to be regulated at the level of transcription in various tissues. However, the post-transcriptional regulation of Hsp70 has not been well characterized in any cells. To elucidate the molecular mechanism underlying the synthesis of Hsp70 in RPE cells, the regulation of the synthesis of Hsp70 in RPE cells was investigated. The synthesis of Hsp70 was determined in ARPE-19 cells and bovine RPE cells exposed to heat shock and an inhibitor of the translation initiation factor eIF4A. Transcription of Hsp70 mRNA was not
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