Proteomic analysis of protein adsorption capacity of different haemodialysis membranes

Andrea Urbani, Santina Lupisella, Vittorio Sirolli, Sonia Bucci, Luigi Amoroso, Barbara Pavone, Luisa Pieroni, Paolo Sacchetta, Mario Bonomini

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Protein-adsorptive properties are a key feature of membranes used for haemodialysis treatment. Protein adsorption is vital to the biocompatibility of a membrane material and influences membrane's performance. The object of the present study is to investigate membrane biocompatibility by correlating the adsorbed proteome repertoire with chemical feature of the membrane surfaces. Dialyzers composed of either cellulose triacetate (Sureflux 50 L, effective surface area 0.5 m 2; Nipro Corporation, Japan) or the polysulfone-based helixone (FX40, effective surface area 0.4 m 2; Fresenius Medical Care AG, Germany) materials were employed to develop an ex vivo apparatus to study protein adsorption. Adsorbed proteins were eluted by a strong chaotropic buffer condition and investigated by a proteomic approach. The profiling strategy was based on 2D-electrophoresis separation of desorbed protein coupled to MALDI-TOF/TOF analysis. The total protein adsorption was not significantly different between the two materials. An average of 179 protein spots was visualised for helixone membranes while a map of retained proteins of cellulose triacetate membranes was made up of 239 protein spots. The cellulose triacetate material showed a higher binding capacity for albumin and apolipoprotein. In fact, a number of different protein spots belonging to the gene transcript of albumin were visible in the cellulose triacetate map. In contrast, helixone bound only a small proportion of albumin, while proved to be particularly active in retaining protein associated with the coagulation cascade, such as the fibrinogen isoforms. Our data indicate that proteomic techniques are a useful approach for the investigation of proteins surface-adsorbed onto haemodialysis membranes, and may provide a molecular base for the interpretation of the efficacy and safety of anticoagulation treatment during renal replacement therapy.

Original languageEnglish
Pages (from-to)1029-1039
Number of pages11
JournalMolecular BioSystems
Volume8
Issue number4
DOIs
Publication statusPublished - Mar 2012

Fingerprint

Proteomics
Adsorption
Renal Dialysis
Membranes
Proteins
Albumins
Renal Replacement Therapy
Apolipoproteins
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Proteome
Fibrinogen
Germany
Electrophoresis
Japan
Buffers
Protein Isoforms
Membrane Proteins
Safety
cellulose triacetate
Therapeutics

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Biology

Cite this

Urbani, A., Lupisella, S., Sirolli, V., Bucci, S., Amoroso, L., Pavone, B., ... Bonomini, M. (2012). Proteomic analysis of protein adsorption capacity of different haemodialysis membranes. Molecular BioSystems, 8(4), 1029-1039. https://doi.org/10.1039/c2mb05393d

Proteomic analysis of protein adsorption capacity of different haemodialysis membranes. / Urbani, Andrea; Lupisella, Santina; Sirolli, Vittorio; Bucci, Sonia; Amoroso, Luigi; Pavone, Barbara; Pieroni, Luisa; Sacchetta, Paolo; Bonomini, Mario.

In: Molecular BioSystems, Vol. 8, No. 4, 03.2012, p. 1029-1039.

Research output: Contribution to journalArticle

Urbani, A, Lupisella, S, Sirolli, V, Bucci, S, Amoroso, L, Pavone, B, Pieroni, L, Sacchetta, P & Bonomini, M 2012, 'Proteomic analysis of protein adsorption capacity of different haemodialysis membranes', Molecular BioSystems, vol. 8, no. 4, pp. 1029-1039. https://doi.org/10.1039/c2mb05393d
Urbani, Andrea ; Lupisella, Santina ; Sirolli, Vittorio ; Bucci, Sonia ; Amoroso, Luigi ; Pavone, Barbara ; Pieroni, Luisa ; Sacchetta, Paolo ; Bonomini, Mario. / Proteomic analysis of protein adsorption capacity of different haemodialysis membranes. In: Molecular BioSystems. 2012 ; Vol. 8, No. 4. pp. 1029-1039.
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