The impact of pre-analytical conditions on the serum proteome: heat-stabilization versus nitrogen storage.

Autor: Gemoll T; Section for Translational Surgical Oncology and Biobanking, Department of Surgery, University of Lübeck and University Medical Center Schleswig-Holstein, Campus Lübeck, Germany. Gemoll@chirurgie.uni-luebeck.de, Löwe O, Borén M, Oberländer M, Hartwig S, Lehr S, Roblick UJ, Auer G, Jörnvall H, Habermann JK
Jazyk: angličtina
Zdroj: Archives of physiology and biochemistry [Arch Physiol Biochem] 2013 Jul; Vol. 119 (3), pp. 100-7. Date of Electronic Publication: 2013 Jul 04.
DOI: 10.3109/13813455.2013.806556
Abstrakt: Context: Biological material reflecting the in vivo composition of markers provides a high potential for biomarker discovery.
Objective: We compared the serum proteome following heat- and nitrogen-preservation, with and without subsequent storage at room temperature.
Materials and Methods: Serum samples were collected, treated and analysed by two-dimensional gel electrophoresis. Protein spots were identified and confirmed by two mass spectrometry approaches (MALDI & ESI) and subjected to Ingenuity Pathway Analysis.
Results: We revealed 24 differentially expressed proteins (p ≤ 0.05) between nitrogen and heat preservation, and 87 between nitrogen and heat preservation with subsequent storage for 120 h at room-temperature. Mass spectrometry identified 25 polypeptides. Pathway analysis resulted in networks maintaining Cellular Assembly and Organization, Movement and Maintenance.
Conclusion: Heat-stabilization does not substantially change the short-term proteome composition of serum compared with nitrogen treatment. However, heat-stabilization alone seems insufficient for long-term sample preservation for serum samples. We identified transthyretin and apolipoprotein A-IV as sample quality markers.
Databáze: MEDLINE
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