1. ¹Department of Internal Medicine I, Charles University Medical School and Teaching Hospital, Plzen, Czech Republic
2. ²Medical Proteomics Unit, Office for Research, and Development Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, Thailand
3. ³Proteomic Laboratory, Charles University Medical School, Plzen, Czech Republic

Correspondence: Jan Mares, Department of Internal Medicine I, Charles University Teaching Hospital, Alej Svobody 80, 30460 Plzen, Czech Republic. E-mail: mares@fnplzen.cz

Received 16 December 2008; Revised 11 February 2009; Accepted 18 March 2009; Published online 6 May 2009.

Abstract

Dialyser bioincompatibility is an important factor contributing to complications of hemodialysis with well known systemic consequences. Here we studied the local processes that occur on dialysis membranes by eluting proteins adsorbed to the polysulfone dialyser membranes of 5 patients after 3 consecutive routine maintenance hemodialysis sessions. At the end of each procedure, a plasma sample was also collected. These eluates and their accompanying plasma samples were separated by 2-dimensional gel electrophoresis; all proteins that were present in all patients were analyzed by tandem mass spectrometry; and a ratio of the relative spot intensity of the eluate to plasma was calculated. Of 153 proteins detected, 84 were found in all patients, 57 of which were successfully identified by mass spectrometry as 38 components of 23 unique proteins. In 10 spots the relative eluate intensity differed significantly from that in the plasma, implying preferential adsorption. These proteins included ficolin-2, clusterin, complement C3c fragment, and apolipoprotein A1. Our finding of a selective binding of ficolin-2 to polysulfone membranes suggests a possible role of the lectin complement pathway in blood-dialyser interactions.