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Prostate. 2000 Sep 15;45(1):58-65.

Heat-shock proteins inhibit induction of prostate cancer cell apoptosis.

Author information

1
Department of Surgery, Mater Misericordiae Hospital, Conway Institute of Biomedicine and Biomolecular Research, University College Dublin, Ireland.

Abstract

BACKGROUND:

Resistance to apoptosis remains a significant problem in the treatment of prostate cancer. Heat-shock proteins (HSP) have been correlated with tumor progression. The role of HSP in prostate cancer resistance to apoptosis is unknown.

METHODS:

PC-3 and LNCaP prostate cancer cells were heat-shocked and then treated with or without diethyl-maleate, etoposide, cycloheximide, or 3 Gray irradiation. Percent apoptosis was assessed by propidium iodide DNA incorporation. Protein was also extracted for analysis by SDS-PAGE Western blotting.

RESULTS:

Western blotting confirmed an increase in HSP 27 and 72. These cells were resistant to both chemical- and radiation-induced apoptosis. Cycloheximide and specific oligonucleotides to HSP 72 blocked the increased expression of HSP 72 and the resistance to apoptosis. Mcl-1, Bcl-2, Bcl-X(L), and glutathione-S-transferase (GST) expression were increased in a time-dependent manner after heat shock.

CONCLUSIONS:

This study demonstrates that HSP expression, specifically HSP 72, inhibits apoptosis in prostate tumor cell lines, which may be mediated by the production of survival factors.

PMID:
10960843
[Indexed for MEDLINE]

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