Protein binding mediation of biomaterial-dependent monocyte activation on a degradable polar hydrophobic ionic polyurethane
Abstract
Protein adsorption is an important phenomenon influencing the cellular response to biomaterials. Previous studies comparing monocyte activation on a degradable polar hydrophobic ionic polyurethane (D-PHI) indicated a reduced pro-inflammatory monocyte response relative to tissue culture polystyrene (TCPS) and poly(lactide-co-glycolide) (PLGA) substrates. The present study investigated the influence of protein binding in order to gain further insight into the observed differential monocyte activation. Several proteins, identified in different relative amounts within the bound protein layers on D-PHI vs. PLGA and TCPS, were evaluated for their effect on monocyte activation. It was found that, in general, both non-coated and protein pre-adsorbed D-PHI supported a reduced pro-inflammatory response relative to PLGA, as indicated by lower levels of tumor necrosis factor-α (TNF-α) release. An initial increase in TNF-α release occurred when α(2)-macroglobulin (A2M) was pre-adsorbed to D-PHI, which was shown to involve the α(2)-macroglobulin receptor and was active on D-PHI but not on the two other biomaterials. This response was not observed during competitive protein binding in the presence of fetal bovine serum (FBS), suggesting that a more complex arrangement of the bound proteins and their interactions with one another, as well as with the surface chemistry of the individual biomaterials, resulted in the low-activating character of D-PHI when interacting with human monocytes.
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Variation in protein adsorption, as a function of surface chemistry, leads to varied cytokine release profile of adhered MDM on different surfaces.
“To understand a potential mechanism for this surface chemistry dependent immune response, a follow-up study by the same group demonstrated that the variation in protein adsorption, which was a function of surface chemistry, led to the varied cytokine release profile of adhered MDM on different surfaces [56].”
From Biomaterial based modulation of macrophage polarization: a review and suggested design principles (2015) · cites this paper as [56]
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Proteomic and Advanced Biochemical Techniques to Study Protein Adsorption
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Hemocompatibility of Degradable Polar Hydrophobic Ionic Polyurethane for Blood Contact Applications
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3.3 Proteomic and Advanced Biochemical Techniques to Study Protein Adsorption ☆
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- Authors
- Battiston, K. G., Labow, R. S., & Santerre, J. P.
- Affiliations
- University of Toronto (CA)
- University of Ottawa (CA)
- Corresponding author
- Santerre, J. Paul
- ORCID
- Santerre, J. Paul
- Venue
- Biomaterials
- Publisher
- Elsevier BV
- Published
- 2012-11
- Volume
- 33
- Issue
- 33
- Pages
- 8316-8328
- ISSN
- 0142-9612 (ISSN-L)
- OpenAlex
- W2008962117
- Cited by
- 53
- References
- 68
- Citations by year
- 2026: 2 · 2024: 1 · 2023: 2 · 2022: 2 · 2021: 6 · 2020: 4 · 2019: 10 · 2018: 4 · 2017: 5 · 2016: 4 · 2015: 7 · 2014: 4 · 2013: 1
- FWCI
- 1.70
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Biomaterials (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research (#230762, 337246/83459, STP53877)
- Natural Sciences and Engineering Research Council of Canada
- Topics
- Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
- Physical Sciences › Materials Science › Biomaterials › biodegradable polymer synthesis and properties
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Hydrogels: synthesis, properties, applications
- Keywords
- protein adsorption, monocyte activation, biodegradable biomaterials, pro-inflammatory response, TNF-α, alpha2-macroglobulin, alpha2-macroglobulin receptor, fetal bovine serum, PLGA, tissue culture polystyrene
- MeSH terms
- Biocompatible Materials, Chromatography, Liquid, Enzyme-Linked Immunosorbent Assay, Monocytes, Polyurethanes, Protein Binding, Mass Spectrometry, Electrophoresis, Gel, Two-Dimensional, Hydrophobic and Hydrophilic Interactions
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