Document Detail

Overexpression of human 27 kDa heat shock protein in laryngeal cancer cells confers chemoresistance associated with cell growth delay.
MedLine Citation:
PMID:  16906418     Owner:  NLM     Status:  MEDLINE    
PURPOSE: Among the family of heat shock proteins (HSPs), HSP70 and HSP27 have been implicated in tumorigenesis and chemoresistance, probably via the prevention of apoptosis. HSP27 levels are frequently increased in large populations of tumors of the head and neck, but the mechanism of its chemoresistance is not yet fully understood. In the present study, the role of HSP27 in the resistance to cytotoxic stress was studied in Hep-2 human laryngeal cancer cells. METHOD: We established a Hep-2 cell line overexpressing HSP27 and examined whether the expression of HSP27 provides resistance to heat shock and several cytotoxic agents using a MTT colorimetic assay. Cell cycle progression was assessed by flow cytometry and fluorescence staining was performed for F-actin filaments. RESULTS: HSP27 overexpression induced cellular resistance to heat shock at 45 degrees C for 1 h as well as against several cytotoxic agents, including cisplatin, staurosporin and H(2)O(2). However, no difference in sensitivity to irradiation or serum starvation was found. Moreover, HSP27 overexpressing Hep-2 cells showed a delayed cell growth, compared to control cells. To determine if the decreased cell proliferation in HSP27 overexpressing cells contributed to chemoresistance, control Hep-2 cells were synchronized at the late G1 phase by treatment with mimosine. The synchronized Hep-2 cells were resistant to cisplatin and H(2)O(2), but not to irradiation or serum starvation, correlating the protection effect shown in HSP27 overexpressing cells. These results suggest that the overexpression of HSP27 in Hep-2 cells confers chemoresistance which is associated with the delay in cell growth. We also propose that the stabilization of F-actin observed in Hep-2/hsp27 cells is partly related to the delay in cell cycle progression, by showing that the induction of actin polymerization in Hep-2/neo cells results in the retardation of cell growth as well as a cytoprotective effect as observed in Hep-2/hsp27.
Jung-Hee Lee; Dongil Sun; Kwang-Jae Cho; Min-Sik Kim; Myung-Hwa Hong; In-Kyung Kim; Jae-Seon Lee; Jeong-Hwa Lee
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-08-12
Journal Detail:
Title:  Journal of cancer research and clinical oncology     Volume:  133     ISSN:  0171-5216     ISO Abbreviation:  J. Cancer Res. Clin. Oncol.     Publication Date:  2007 Jan 
Date Detail:
Created Date:  2006-11-23     Completed Date:  2007-10-19     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  7902060     Medline TA:  J Cancer Res Clin Oncol     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  37-46     Citation Subset:  IM    
Department of Biochemistry, College of Medicine, The Catholic University of Korea, Seoul, 137-701, South Korea.
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MeSH Terms
Antineoplastic Agents / pharmacology*
Blotting, Northern
Blotting, Western
Cell Line, Tumor
Cell Proliferation
Drug Resistance, Neoplasm*
Gene Expression Regulation, Neoplastic
HSP27 Heat-Shock Proteins
Heat-Shock Proteins / metabolism*
Hela Cells
Laryngeal Neoplasms / drug therapy*,  metabolism*
Neoplasm Proteins / metabolism*
Reg. No./Substance:
0/Antineoplastic Agents; 0/HSP27 Heat-Shock Proteins; 0/HSPB1 protein, human; 0/Heat-Shock Proteins; 0/Neoplasm Proteins

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