PMID- 19351150
OWN - NLM
STAT- MEDLINE
DCOM- 20090914
LR  - 20090608
IS  - 1535-3893 (Print)
IS  - 1535-3893 (Linking)
VI  - 8
IP  - 6
DP  - 2009 Jun
TI  - Cytoplasmic proteome and secretome profiles of differently stimulated human 
      dendritic cells.
PG  - 2799-811
LID - 10.1021/pr8011039 [doi]
AB  - Dendritic cells (DCs), the most potent and specialized antigen-presenting cells, 
      play a key role in the regulation of the adaptive immunity. Immature DCs were 
      generated by in vitro culturing of peripheral blood monocytes and functionally 
      activated with the classical pathogen-associated molecular pattern 
      lipopolysaccharide (LPS). Alternative activation resulting in Th-2 polarization 
      was induced with lipid oxidation products derived from 
      1-palmitoyl-2-arachidoyl-sn-glycerol-3-phosphorylcholin (OxPAPC). Tolerogenic 
      cells were obtained by treating DCs with human rhinovirus (HRV). The aim of this 
      study was the identification of proteome profiles related to the functionally 
      different dendritic cell phenotypes. Cytoplasmic proteins were analyzed by 
      shotgun proteomics resulting in the identification of 1690 proteins. While mature 
      and alternatively activated DCs displayed highly distinct protein expression 
      profiles, HRV-treated DCs showed minor proteome alterations. As DCs exert many 
      specific functions via secretion, we investigated the secretomes by a combination 
      of 2D-PAGE and shotgun proteomics. We successfully identified a broad variety of 
      cytokines (e.g., GM-CSF, TNF-alpha, interleukin-1beta, 6, 12 beta, 28B and 29), 
      chemokines (e.g., CCL3, 5, 8, 17, 18, 19, 24, CXCL1, 2, 9 and 10) and growth 
      factors (growth/differentiation factor 8, C-type lectin domain family 11 member 
      A). The relative composition of secretome profiles, although comprising much less 
      proteins, was found to be much more affected by functional alteration of cells 
      than the cytoplasmic protein composition. In conclusion, we demonstrate that 
      functional distinct subsets of DCs display distinct proteome profiles which 
      comprise biomarker candidates. These proteins may prove useful for the 
      interpretation of complex clinical proteomics data.
FAU - Gundacker, Nina C
AU  - Gundacker NC
AD  - Department of Medicine I, Institute of Cancer Research, Medical University of 
      Vienna, Austria.
FAU - Haudek, Verena J
AU  - Haudek VJ
FAU - Wimmer, Helge
AU  - Wimmer H
FAU - Slany, Astrid
AU  - Slany A
FAU - Griss, Johannes
AU  - Griss J
FAU - Bochkov, Valery
AU  - Bochkov V
FAU - Zielinski, Christoph
AU  - Zielinski C
FAU - Wagner, Oswald
AU  - Wagner O
FAU - Stockl, Johannes
AU  - Stockl J
FAU - Gerner, Christopher
AU  - Gerner C
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Proteome Res
JT  - Journal of proteome research
JID - 101128775
RN  - 0 (Cytokines)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (Peptide Fragments)
RN  - 0 (Phosphatidylcholines)
RN  - 0 (Proteome)
RN  - 0 (oxidized-L-alpha-1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine)
SB  - IM
MH  - Cell Line
MH  - Chromatography, Liquid
MH  - Cytokines/metabolism
MH  - Cytoplasm/*metabolism
MH  - Dendritic Cells/immunology/*metabolism
MH  - Electrophoresis, Gel, Two-Dimensional
MH  - Humans
MH  - Lipopolysaccharides/immunology
MH  - Peptide Fragments/analysis
MH  - Phosphatidylcholines/immunology
MH  - Proteome/*metabolism
MH  - Proteomics/*methods
MH  - Rhinovirus/immunology
MH  - *Secretory Pathway
MH  - Tandem Mass Spectrometry
EDAT- 2009/04/09 09:00
MHDA- 2009/09/15 06:00
CRDT- 2009/04/09 09:00
PHST- 2009/04/09 09:00 [entrez]
PHST- 2009/04/09 09:00 [pubmed]
PHST- 2009/09/15 06:00 [medline]
AID - 10.1021/pr8011039 [doi]
PST - ppublish
SO  - J Proteome Res. 2009 Jun;8(6):2799-811. doi: 10.1021/pr8011039.