Document Detail


A proteomic snapshot of breast cancer cell cycle: The G1/S transition point.
MedLine Citation:
PMID:  23152136     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The biological processes that unfold during the G1-phase of the cell cycle are dependent on extracellular mitogenic factors which signal the cell to enter a state of quiescence, or commit to a cell cycle round by passing the restriction point (R-point) and enter the S-phase. Unlike normal cells, cancer cells evolved the ability to evade the R-point and continue through the cell cycle even in the presence of extensive DNA damage or absence of mitogenic signals. The purpose of this study was to perform a quantitative proteomic evaluation of the biological processes that are responsible for driving MCF-7 breast cancer cells into division even when molecular checkpoints such as the G1/S R-point are in place. Nuclear and cytoplasmic fractions of the G1 and S cell cycle phases were analyzed by LC-MS/MS to result in the confident identification of >2700 proteins. Statistical evaluation of the normalized data resulted in the selection of proteins that displayed ≥2-fold change in spectral counts in each cell state. Pathway mapping, functional annotation clustering and protein interaction network analysis revealed that the top-scoring clusters that could play a role in overriding the G1/S transition point included DNA damage response, chromatin remodeling, transcription/translation regulation and signaling proteins.
Authors:
Milagros J Tenga; Iulia M Lazar
Related Documents :
22970236 - Phosphorylation and subcellular localization of p27kip1 regulated by hydrogen peroxide ...
24142346 - Targeting mitochondria by α-tocopheryl succinate overcomes hypoxia-mediated tumor cell...
23990456 - Apicidin-resistant ha22t hepatocellular carcinoma cells massively promote pro-survival ...
24115616 - Growth kinetics and energetics of a deep-sea hyperthermophilic methanogen under varying...
22718906 - A balance of fgf and bmp signals regulates cell cycle exit and equarin expression in le...
15196816 - The low molecular weight heparan sulfate-mimetic, pi-88, inhibits cell-to-cell spread o...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-11-14
Journal Detail:
Title:  Proteomics     Volume:  -     ISSN:  1615-9861     ISO Abbreviation:  Proteomics     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-15     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:
Department of Biological Sciences, Virginia Polytechnic Institute and State University, 1981 Kraft Drive, Blacksburg, VA, 246021.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

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


Previous Document:  Decompressive Hemicraniectomy Reduces Mortality in an Animal Model of Intracerebral Hemorrhage.
Next Document:  Adsorption chromatography separation of the flavonols kaempferol, quercetin and myricetin using cros...