Document Detail

Expression and distribution of HSP27 in response to G418 in different human breast cancer cell lines.
MedLine Citation:
PMID:  16733662     Owner:  NLM     Status:  MEDLINE    
Heat shock proteins (HSPs) play an important role in folding, intracellular localization and degradation of cellular proteins. However, the cellular role of HSP27 is not completely understood. The conflicting results have been reported regarding stress-induced nuclear translocation of HSP27. In this study, human breast cancer cells transiently and stably expressing HSP27-EGFP chimera were utilized to observe the intracellular localization of HSP27. The data show that the transient and stable expression of HSP27-EGFP displayed distinguishingly cellular localization. The nuclear translocalization of HSP27-EGFP was correlated with the presence of G418. Experiments carried out with different human breast cancer cell lines revealed clearly different distribution patterns of endogenous HSP27. The subcellular distribution of endogenous HSP27 appeared diffuse throughout the cytoplasm in MDA435 cells. In MCF-7 and SKBR3 cells, the accumulation of the protein was distinctly seen along the cell membrane and around nucleus. Moreover, the nuclear translocation of endogenous HSP27 was stimulated by G418 only in MDA435 cells, but not in MCF-7 and SKBR3 cells. Overexpression of HSP27 has been associated with resistance to cisplatin and doxorubicin. The correlation of the expression pattern of HSP27 with the drug resistance may need to be investigated. Further studies on the intracellular function of HSP27 may take into account its interaction proteins in the cells. It may provide useful information for the identification of sensitivity of carcinoma cells to the chemotherapeutic drugs and development of more specific agents to circumvent HSP27.
Lu Qian; Zhiyi Zhang; Ming Shi; Ming Yu; Meiru Hu; Qing Xia; Beifen Shen; Ning Guo
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-05-30
Journal Detail:
Title:  Histochemistry and cell biology     Volume:  126     ISSN:  0948-6143     ISO Abbreviation:  Histochem. Cell Biol.     Publication Date:  2006 Nov 
Date Detail:
Created Date:  2007-01-11     Completed Date:  2007-04-25     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  9506663     Medline TA:  Histochem Cell Biol     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  593-601     Citation Subset:  IM    
Department of Cellular Immunology, Institute of Basic Medical Sciences, Taiping Road 27, Beijing 100850, People's Republic of China.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Blotting, Western
Breast Neoplasms / metabolism*
Cell Line, Tumor
Cell Nucleus / metabolism
Gentamicins / pharmacology*
Green Fluorescent Proteins / genetics
HSP27 Heat-Shock Proteins
Heat-Shock Proteins / biosynthesis*
Neoplasm Proteins / biosynthesis*
Protein Transport
Reg. No./Substance:
0/Gentamicins; 0/HSP27 Heat-Shock Proteins; 0/HSPB1 protein, human; 0/Heat-Shock Proteins; 0/Neoplasm Proteins; 0/enhanced green fluorescent protein; 147336-22-9/Green Fluorescent Proteins; 49863-47-0/antibiotic G 418

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Change of procalcitonin predicts clinical outcome of febrile episodes in patients with hematological...
Next Document:  Distribution of E-cadherin and beta-catenin in relation to cell maturation and cell extrusion in rat...