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Quantitative proteomic analysis to decipher the differential apoptotic response of bortezomib-treated acute promyelocytic leukemia cells before and after retinoic acid-differentiation reveals an involvement of protein toxicity mechanisms.
MedLine Citation:
PMID:  23135970     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The ubiquitin-proteasome system allows the targeted degradation of proteins and plays a critical role in the regulation of many cellular processes. Proteasome inhibition is a recent antitumor therapeutic strategy and bortezomib was the first proteasome inhibitor approved for clinical use. In this study, we used the NB4 cell line to investigate the effects of bortezomib towards acute promyelocytic leukaemia cells before and after retinoic acid-induced differentiation. We showed that apoptosis level after bortezomib treatment is higher in NB4 cells than in differentiated NB4 cells. To compare early protein variations upon bortezomib treatment in both NB4 cell populations, we performed a quantitative proteomic analysis based on iTRAQ peptide labeling followed by data analysis with in-house developed scripts. This strategy revealed the regulation of 14 proteins principally involved in protein stress response and apoptosis in NB4 cells after proteasome inhibition. Altogether, our results suggest that the differential level of apoptosis induced by bortezomib treatment in both NB4 cell populations could result from distinct protein toxicity level.
Authors:
Sandrine Uttenweiler-Joseph; David Bouyssié; David Calligaris; Pierre G Lutz; Bernard Monsarrat; Odile Burlet-Schiltz
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-11-8
Journal Detail:
Title:  Proteomics     Volume:  -     ISSN:  1615-9861     ISO Abbreviation:  Proteomics     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-8     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101092707     Medline TA:  Proteomics     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
© 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Affiliation:
CNRS;IPBS (Institut de Pharmacologie et de Biologie Structurale), 205 route de Narbonne BP64182, F-31077, Toulouse, France; Université de Toulouse, UPS; IPBS, F-31077, Toulouse, France.
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