Material surfaces affect the protein expression patterns of human macrophages: A proteomics approach

• Published in: Journal of biomedical materials research. Part A Vol. 80A; no. 4; pp. 895 - 908
• Main Authors: Dinnes, Donna Lee M., Marçal, Helder, Mahler, Stephen M., Santerre, J. Paul, Labow, Rosalind S.
• Format: Journal Article
• Language: English
• Published: Hoboken Wiley Subscription Services, Inc., A Wiley Company 15.03.2007
• Subjects: 2-dimensional electrophoresis; Biocompatible Materials; Cell Culture Techniques; Cells, Cultured; Humans; inflammation; Macrophages - cytology; Macrophages - metabolism; MALDI-ToF; Materials Testing; monocyte-derived macrophage; polyurethane; Polyurethanes; Protein Biosynthesis; Proteome - biosynthesis; proteomics; Proteomics - methods; Surface Properties
• ISSN: 1549-3296; 1552-4965
• DOI: 10.1002/jbm.a.30967

Monocyte‐derived macrophages (MDM) are key inflammatory cells and are central to the foreign body response to implant materials. MDM have been shown to exhibit changes in actin cytoskeleton, multinucleation, cell size, and function in response to small alterations in polycarbonate‐urethane (PCNU) surface chemistry. Although PCNU chemistry has an influence on de novo protein synthesis, no assessments of the protein expression profiles of MDM have yet been reported. The rapid emerging field of expression proteomics facilitates the study of changes in cellular protein profiles in response to their microenvironment. The current study applied proteomic techniques, 2‐dimensional electrophoresis (2‐DE) combined with MALDI‐ToF (matrix assisted laser desorption ionization–time of flight) mass spectrometry, to determine differences in MDM protein expression influenced by PCNU. Results indicated that MDM responded to material chemistry by modulation of structural proteins (i.e. actin, vimentin, and tubulin). Additionally, intracellular protein modulation which requires proteins responsible for trafficking (i.e. chaperone proteins) and protein structure modification (i.e. bond rearrangement and protein folding) were also altered. This study demonstrated for the first time that a proteomics approach was able to detect protein expression profile changes in MDM cultured on different material surfaces, forming the basis for utilizing further quantitative proteomics techniques that could assist in elucidation of the mechanisms involved in MDM–material interaction. © 2006 Wiley Periodicals, Inc. J Biomed Mater Res, 2006