Document Detail


Hsp90-mediated inhibition of FKBP38 regulates apoptosis in neuroblastoma cells.
MedLine Citation:
PMID:  18036348     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The FK506-binding protein 38 (FKBP38) is a pro-apoptotic regulator of Bcl-2 in neuroblastoma cells. Hsp90 inhibits the pro-apoptotic FKBP38/CaM/Ca(2+) complex and thus prevents interactions between FKBP38 and Bcl-2. Here we show that Hsp90 increases cell survival rates of neuroblastoma cells after apoptosis induction. Depletion of FKBP38 by short interference RNA significantly decreased the anti-apoptotic effect of Hsp90 expression. In addition, the influence of high cellular Hsp90 levels was only observed in post-stimulation apoptosis that is sensitive to selective FKBP38 active site inhibition. Similar anti-apoptotic effects in neuroblastoma cells were observed after stimulation of endogenous Hsp90 expression. Hence, the inhibition of FKBP38 by Hsp90 participates in programmed cell death control of neuroblastoma cells.
Authors:
Frank Erdmann; Franziska Jarczowski; Matthias Weiwad; Gunter Fischer; Frank Edlich
Related Documents :
25255138 - Short-time exposure of hyperosmolarity triggers interleukin-6 expression in corneal epi...
25220858 - Biological quality control for extracorporeal photochemotherapy: assessing mononuclear ...
9365238 - Evidence against a functional site for bcl-2 downstream of caspase cascade in preventin...
19557638 - Targeting the bcl-2 family of proteins in hodgkin lymphoma: in vitro cytotoxicity, targ...
11498258 - Protection against experimental autoimmune encephalomyelitis by a proteasome modulator.
21933878 - Miltefosine effectively modulates the cytokine milieu in indian post kala-azar dermal l...
Publication Detail:
Type:  Journal Article     Date:  2007-11-26
Journal Detail:
Title:  FEBS letters     Volume:  581     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  2007 Dec 
Date Detail:
Created Date:  2007-12-06     Completed Date:  2008-03-26     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  5709-14     Citation Subset:  IM    
Affiliation:
Max-Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120, Halle/Saale, Germany.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Apoptosis*
Binding Sites
Calcium / metabolism
Calmodulin / metabolism
Cell Death
Cell Line, Tumor
HSP90 Heat-Shock Proteins / metabolism*
Humans
Iodoacetic Acid / pharmacology
Neuroblastoma / metabolism*
Tacrolimus Binding Proteins / antagonists & inhibitors*,  metabolism
Chemical
Reg. No./Substance:
0/Calmodulin; 0/HSP90 Heat-Shock Proteins; 64-69-7/Iodoacetic Acid; 7440-70-2/Calcium; EC 5.2.1.-/Tacrolimus Binding Proteins

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


Previous Document:  Mutations of the SM protein Sly1 resulting in bypass of GTPase requirement in vesicular transport ar...
Next Document:  Metabolic adaptations through the PGC-1 alpha and SIRT1 pathways.