1. The impact of pre-analytical conditions on the serum proteome: heat-stabilization versus nitrogen storage.
- Author
-
Gemoll, Timo, Löwe, Oliver, Borén, Mats, Oberländer, Martina, Hartwig, Sonja, Lehr, Stefan, Roblick, Uwe J., Auer, Gert, Jörnvall, Hans, and Habermann, Jens K.
- Subjects
HEAT stability in proteins ,BLOOD proteins ,PROTEOMICS ,BIOMATERIALS ,PHYSIOLOGICAL effects of nitrogen ,BIOMARKERS ,GEL electrophoresis ,GENE expression - Abstract
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. [ABSTRACT FROM AUTHOR]
- Published
- 2013
- Full Text
- View/download PDF