Proteome signatures of inflammatory activated primary human peripheral blood mononuclear cells.

Proteome signatures of inflammatory activated primary human peripheral blood mononuclear cells.
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DOI:
10.1016/j.jprot.2012.07.012
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发表时间:
2012-12-05
影响因子:
3.3
通讯作者:
Gerner C
Gerner C
中科院分区:
生物学2区
文献类型:
--
作者:
Haudek-Prinz VJ;Klepeisz P;Slany A;Griss J;Meshcheryakova A;Paulitschke V;Mitulovic G;Stöckl J;Gerner C

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Proteome profiling is the method of choice to identify marker proteins whose expression may be characteristic for certain diseases. The formation of such marker proteins results from disease-related pathophysiologic processes. In healthy individuals, peripheral blood mononuclear cells (PBMCs) circulate in a quiescent cell state monitoring potential immune-relevant events, but have the competence to respond quickly and efficiently in an inflammatory manner to any invasion of potential pathogens. Activation of these cells is most plausibly accompanied by characteristic proteome alterations. Therefore we investigated untreated and inflammatory activated primary human PBMCs by proteome profiling using a ‘top down’ 2D-PAGE approach in addition to a ‘bottom up’ LC–MS/MS-based shotgun approach. Furthermore, we purified primary human T-cells and monocytes and activated them separately. Comparative analysis allowed us to characterize a robust proteome signature including NAMPT and PAI2 which indicates the activation of PBMCs. The T-cell specific inflammation signature included IRF-4, GBP1and the previously uncharacterized translation product of GBP5; the corresponding monocyte signature included PDCD5, IL1RN and IL1B. The involvement of inflammatory activated PBMCs in certain diseases as well as the responsiveness of these cells to anti-inflammatory drugs may be evaluated by quantification of these marker proteins. This article is part of a Special Issue entitled: Integrated omics. ► Reproducible identification of marker proteins using 2D-gels and shotgun proteomics ► Application of sub-cellular fractionation including cytoplasmic, nuclear and secreted proteins ► Application of metabolic labeling of primary human cells ► Comparison of proteome profiles across different cell types ► Support of functional data interpretation of clinical proteomics studies
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