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The impact of pre-analytical conditions on the serum proteome: heat-stabilization versus nitrogen storage.
- Source :
- Archives of Physiology & Biochemistry; Jul2013, Vol. 119 Issue 3, p100-107, 8p
- Publication Year :
- 2013
-
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]
Details
- Language :
- English
- ISSN :
- 13813455
- Volume :
- 119
- Issue :
- 3
- Database :
- Complementary Index
- Journal :
- Archives of Physiology & Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 88937381
- Full Text :
- https://doi.org/10.3109/13813455.2013.806556