PMID- 21786837
OWN - NLM
STAT- MEDLINE
DCOM- 20120123
LR  - 20211203
IS  - 1535-3907 (Electronic)
IS  - 1535-3893 (Linking)
VI  - 10
IP  - 9
DP  - 2011 Sep 2
TI  - Characterization of the phosphoproteome in androgen-repressed human prostate 
      cancer cells by Fourier transform ion cyclotron resonance mass spectrometry.
PG  - 3920-8
LID - 10.1021/pr2000144 [doi]
AB  - Androgen-repressed human prostate cancer, ARCaP, grows and is highly metastatic 
      to bone and soft tissues in castrated mice. The molecular mechanisms underlying 
      the aberrant responses to androgen are not fully understood. Here, we apply 
      state-of-the-art mass spectrometry methods to investigate the phosphoproteome 
      profiles in ARCaP cells. Because protein biological phosphorylation is always 
      substoichiometric and the ionization efficiency of phosphopeptides is low, 
      selective enrichment of phosphorylated proteins/peptides is required for mass 
      spectrometric analysis of phosphorylation from complex biological samples. 
      Therefore, we compare the sensitivity, efficiency, and specificity for three 
      established enrichment strategies: calcium phosphate precipitation (CPP), 
      immobilized metal ion affinity chromatography (IMAC), and TiO(2)-modified metal 
      oxide chromatography. Calcium phosphate precipitation coupled with the TiO(2) 
      approach offers the best strategy to characterize phosphorylation in ARCaP cells. 
      We analyzed phosphopeptides from ARCaP cells by LC-MS/MS with a hybrid LTQ/FT-ICR 
      mass spectrometer. After database search and stringent filtering, we identified 
      385 phosphoproteins with an average peptide mass error of 0.32 +/- 0.6 ppm. Key 
      identified oncogenic pathways include the mammalian target of rapamycin (mTOR) 
      pathway and the E2F signaling pathway. Androgen-induced proliferation inhibitor 
      (APRIN) was detected in its phosphorylated form, implicating a molecular 
      mechanism underlying the ARCaP phenotype.
FAU - Wang, Xu
AU  - Wang X
AD  - Department of Chemistry and Biochemistry, 95 Chieftain Way, Florida State 
      University, Tallahassee, Florida 32306, United States.
FAU - Stewart, Paul A
AU  - Stewart PA
FAU - Cao, Qiang
AU  - Cao Q
FAU - Sang, Qing-Xiang Amy
AU  - Sang QX
FAU - Chung, Leland W K
AU  - Chung LW
FAU - Emmett, Mark R
AU  - Emmett MR
FAU - Marshall, Alan G
AU  - Marshall AG
LA  - eng
GR  - P01 CA098912/CA/NCI NIH HHS/United States
GR  - R01 CA122602/CA/NCI NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20110726
PL  - United States
TA  - J Proteome Res
JT  - Journal of proteome research
JID - 101128775
RN  - 0 (Calcium Phosphates)
RN  - 0 (E2F Transcription Factors)
RN  - 0 (Phosphopeptides)
RN  - 0 (Phosphoproteins)
RN  - 0 (Proteome)
RN  - 15FIX9V2JP (titanium dioxide)
RN  - 97Z1WI3NDX (calcium phosphate)
RN  - D1JT611TNE (Titanium)
RN  - EC 2.7.1.1 (MTOR protein, human)
RN  - EC 2.7.11.1 (TOR Serine-Threonine Kinases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Calcium Phosphates/chemistry
MH  - Cell Line, Tumor
MH  - Chemical Precipitation
MH  - Chromatography, Affinity
MH  - E2F Transcription Factors/metabolism
MH  - Fourier Analysis
MH  - Humans
MH  - Male
MH  - Mass Spectrometry/*methods
MH  - Molecular Sequence Data
MH  - Neoplasms, Hormone-Dependent/metabolism
MH  - Phosphopeptides/analysis/chemistry/*isolation & purification
MH  - Phosphoproteins/analysis/metabolism
MH  - Phosphorylation
MH  - Prostatic Neoplasms/*metabolism
MH  - Proteome/*analysis/chemistry
MH  - Proteomics/*methods
MH  - Reproducibility of Results
MH  - Sensitivity and Specificity
MH  - TOR Serine-Threonine Kinases
MH  - Titanium/chemistry
EDAT- 2011/07/27 06:00
MHDA- 2012/01/24 06:00
CRDT- 2011/07/27 06:00
PHST- 2011/07/27 06:00 [entrez]
PHST- 2011/07/27 06:00 [pubmed]
PHST- 2012/01/24 06:00 [medline]
AID - 10.1021/pr2000144 [doi]
PST - ppublish
SO  - J Proteome Res. 2011 Sep 2;10(9):3920-8. doi: 10.1021/pr2000144. Epub 2011 Jul 
      26.