Change in the localization of heat shock protein 27 (HSP 27) in BG-1 human ovarian cancer cells following treatment by the ether lipid ET-18-OCH3

We have demonstrated a higher nuclear protein content in the hypodiploid fraction of BG-1 human ovarian cancer cells following treatment with one of the ether lipids, ET-18-OCH3. In this study, we have attempted to identify the overexpressed nuclear protein induced in those dying or dead cells in th...

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Bibliographic Details
Published inAnticancer research Vol. 19; no. 1A; p. 181
Main Authors Fujiwara, K, Shirafuji, H, Fushitani, K, Fujimoto, K, Kohno, I, Modest, E J
Format Journal Article
LanguageEnglish
Published Greece 01.01.1999
Subjects
Adenocarcinoma - metabolism
Amino Acid Sequence
Cell Nucleus - metabolism
Female
Flow Cytometry
Fluorescent Antibody Technique
Heat-Shock Proteins - analysis
Heat-Shock Proteins - metabolism
Humans
Molecular Sequence Data
Nuclear Proteins - analysis
Ovarian Neoplasms - metabolism
Phosphatidylcholines - pharmacology
Phospholipid Ethers
Signal Transduction
Tumor Cells, Cultured
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Summary:We have demonstrated a higher nuclear protein content in the hypodiploid fraction of BG-1 human ovarian cancer cells following treatment with one of the ether lipids, ET-18-OCH3. In this study, we have attempted to identify the overexpressed nuclear protein induced in those dying or dead cells in the hypodiploid fraction and its localization before and after ET-18-OCH3 treatment. The pattern of nuclear proteins was analyzed by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) before and after ET-18-OCH3 treatment. The partial amino acid sequence of the most dominantly and consistently up-regulated protein spot after ET-18-OCH3 treatment was determined and it was found to be heat shock protein 27 (HSP27). Immunofluorescence staining disclosed that HSP27 localizes in the cytoplasm of the BG-1 cells before ET-18-OCH3 treatment. Condensation of HSP27 around the nuclei was observed following treatment by ET-18-OCH3. Ultimately, the nuclei of the cells in the hypodiploid fraction were stained by immunofluorescent HSP27. These results indicate that change of the localization of HSP27 may play an important role as a component of the signal transduction pathways affected by ether lipids.
ISSN:0250-7005