PMID: 9551250Apr 29, 1998Paper

17 beta-estradiol-induced increases in glucose-regulated protein 78kD and 94kD protect human breast cancer T47-D cells from thermal injury

The Chinese Journal of Physiology
J G KiangG C Tsokos

Abstract

Heat shock alters the susceptibility of tumor cells to chemotherapeutic agents. We conducted experiments to study the regulation of expression of heat shock proteins (HSP) in 17 beta-estradiol-treated T47-D cells, a human breast cancer cell line. Cells exposed to 17 beta-estradiol for 24-48 h displayed increased expression of glucose regulated protein 78kD (GRP-78) and 94kD (GRP-94), as shown by [35S]methionine incorporation and Western blotting experiments. The increase was time (5 h to 48 h)-dependent at 1 nM and 1 microM 17 beta-estradiol. Cells overexpressing GRP-78 and -94 after treatment with 17 beta-estradiol displayed resistance against heat shock (47 degrees C for 50 min)-induced death. Removal of external Ca2+ or treatment of cells with BAPTA (a Ca2+ chelator) did not alter the synthesis of GRP-78 and -94, suggesting that the 17 beta-estradiol effect on the synthesis of GRP-78 and -94 is Ca(2+)-independent. In addition, exposure of cells to 17 beta-estradiol up to 100 microM did not increase [Ca2+]i, which further supports the view that the estrogen-induced GRPs are not regulated by [Ca2+]i. Treatment with H89 (a protein kinase A inhibitor, 1 microM, 30 min) or GF-109203X (a protein kinase C inhibitor, 1 microM, 30 mi...Continue Reading

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