Document Detail

Hsp70B' regulation and function.
MedLine Citation:
PMID:  18229458     Owner:  NLM     Status:  MEDLINE    
Heat shock protein (Hsp) 70B' is a human Hsp70 chaperone that is strictly inducible, having little or no basal expression levels in most cells. Using siRNAs to knockdown Hsp70B' and Hsp72 in HT-29, SW-480, and CRL-1807 human colon cell lines, we have found that the two are regulated coordinately in response to stress. We also have found that proteasome inhibition is a potent activator of hsp70B'. Flow cytometry was used to assay hsp70B' promoter activity in HT-29eGFP cells in this study. Knockdown of both Hsp70B' and Hsp72 sensitized cells to heat stress and increasing concentrations of proteasome inhibitor. These data support the conclusion that Hsp72 is the primary Hsp70 family responder to increasing levels of proteotoxic stress, and Hsp70B' is a secondary responder. Interestingly ZnSO4 induces Hsp70B' and not Hsp72 in CRL-1807 cells, suggesting a stressor-specific primary role for Hsp70B'. Both Hsp70B' and Hsp72 are important for maintaining viability under conditions that increase the accumulation of damaged proteins in HT-29 cells. These findings are likely to be important in pathological conditions in which Hsp70B' contributes to cell survival.
Emily J Noonan; Robert F Place; Charles Giardina; Lawrence E Hightower
Related Documents :
17237208 - Microscopic detection of thermogenesis in a single hela cell.
10334908 - Hsf1 activation occurs at different temperatures in somatic and male germ cells in the ...
23318638 - Par3/bazooka and phosphoinositides regulate actin protrusion formation during drosophil...
18326198 - Characterization of the low-salinity stress in vibrio vulnificus.
3287148 - Towards an understanding of the malignant transformation of diploid human fibroblasts.
942798 - Metaphase chromosome anomaly: association with drug resistance and cell-specific products.
Publication Detail:
Type:  Corrected and Republished Article; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cell stress & chaperones     Volume:  12     ISSN:  1355-8145     ISO Abbreviation:  Cell Stress Chaperones     Publication Date:  2007  
Date Detail:
Created Date:  2008-01-30     Completed Date:  2008-03-17     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  9610925     Medline TA:  Cell Stress Chaperones     Country:  United States    
Other Details:
Languages:  eng     Pagination:  393-402     Citation Subset:  IM    
Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269-3125, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Antineoplastic Agents / pharmacology
Cell Survival / drug effects
Flow Cytometry
Green Fluorescent Proteins / metabolism
HSP70 Heat-Shock Proteins / metabolism*
HSP72 Heat-Shock Proteins / metabolism
HT29 Cells
Heat-Shock Response / drug effects
Leupeptins / pharmacology
Promoter Regions, Genetic / genetics
Proteasome Endopeptidase Complex / antagonists & inhibitors
RNA, Small Interfering / metabolism
Grant Support
Reg. No./Substance:
0/Antineoplastic Agents; 0/HSP70 Heat-Shock Proteins; 0/HSP72 Heat-Shock Proteins; 0/HSPA7 protein, human; 0/Leupeptins; 0/RNA, Small Interfering; 0/enhanced green fluorescent protein; 133407-82-6/benzyloxycarbonylleucyl-leucyl-leucine aldehyde; 147336-22-9/Green Fluorescent Proteins; EC Endopeptidase Complex
Corrected and Republished From:
Cell Stress Chaperones. 2007 Autumn;12(3):219-29   [PMID:  17915554 ]

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

Previous Document:  Plasma heat shock protein 60 and cardiovascular disease risk: the role of psychosocial, genetic, and...
Next Document:  Novel insights in the treatment of diabetic nephropathy.