In-Depth Analysis of the Extracorporeal Proteome Adsorbed to Dialysis Membranes during Hemodialysis

被引:2
|
作者
Daniel-Fischer, Lisa [1 ,2 ]
Sobieszek, Isabel J. [1 ,2 ]
Wagner, Anja [1 ,2 ]
Sacnun, Juan Manuel [1 ,2 ]
Watschinger, Bruno [3 ]
Aufricht, Christoph [1 ]
Kratochwill, Klaus [1 ,2 ]
Herzog, Rebecca [1 ,2 ]
机构
[1] Med Univ Vienna, Comprehens Ctr Pediat, Dept Pediat & Adolescent Med, Div Pediat Nephrol & Gastroenterol, A-1090 Vienna, Austria
[2] Med Univ Vienna, Christian Doppler Lab Mol Stress Res Peritoneal D, A-1090 Vienna, Austria
[3] Med Univ Vienna, Dept Inner Med 3, Div Nephrol & Dialysis, A-1090 Vienna, Austria
基金
奥地利科学基金会;
关键词
hemodialyzer; protein loss; protein adsorption; proteome of hemodialyzer membranes; COMPLEMENT ACTIVATION; ADSORPTION; BIOCOMPATIBILITY; PROTEINS;
D O I
10.3390/membranes12111120
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Used hemodialysis membranes (HD-M) are a valuable reservoir of biological information. Proteins bind to HD-M, but whether this process depends on the type of membrane or patient factors or selectively affects specific protein classes has not been adequately elucidated. State-of-the-art proteomics techniques are capable of identifying and quantifying this therapy-specific subproteome to enable the analysis of disease- or membrane-induced pathophysiologies. We demonstrate the feasibility of the deep proteomic characterization of the extracorporeal proteome adsorbed to HD-M. A shotgun proteomics approach using nano-flow liquid chromatography coupled to mass-spectrometry identified 1648 unique proteins eluted by a chaotropic buffer from the HD-M of eight patients. In total, 995 proteins were present in all eluates; a more stringent approach showed that a core proteome of 310 proteins could be identified independently in all samples. Stability of the dialyzer proteome was demonstrated by a >90% re-identification rate on longitudinal samples of a single patient. The core proteome showed an overrepresentation of pathways of hemostasis and the immune system, and showed differences in membrane materials (polysulfone vs. helixone). This study demonstrates that optimized conditions combined with high-performance proteomics enable the in-depth exploration of the subproteome bound to HD-M, yielding a stable core proteome that can be exploited to study patient-specific factors and improve hemodialysis therapy.
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页数:13
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