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Potential use of mucins as biomaterial coatings. II. Mucin coatings affect the conformation and neutrophil-activating properties of adsorbed host proteins – Towards a mucosal mimic
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry. (Ytbioteknik)
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry. (Ytbioteknik)
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry. (Ytbioteknik)
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry. (Ytbioteknik)
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2009 (English)In: Journal of Biomedical Materials Research: Part A, ISSN 1549-3296(Printed); 1552-4965(Online), Vol. 91A, no 3, 773-785 p.Article in journal (Refereed) Published
Abstract [en]

In continuation of our recent fractionation and characterization study   on mucins of bovine salivary (BSM), porcine gastric (PGM), and human   salivary (MG1) origin, this study evaluates the effect of mucin   precoating on the conformation and neutrophil-activating properties of   host proteins adsorbed to a polyethylene terephthalate-based model   biomaterial. Microscopy combined with assays for the neutrophil   releases of reactive oxygen species and human neutrophil lipocalin   showed that mucin precoating greatly reduced the strong immune-response   normally induced by adsorbed immunoglobulin G (IgG) and secretory   immunoglobulin A (sIgA), respectively. A similar finding was made for   the proinflammatory fibrinogen. Although the total uptakes of these   proteins depended on the mucin surface concentration, a detailed   composite analysis suggested the fraction Of surface-exposed protein to   be a stronger determinant of coating performance. The unexpectedly low   neutrophil activation showed by composites containing near-monolayer   concentrations of exposed IgG and sIgA, respectively, suggested that   these act synergistically with mucin on the surface. In support of this   hypothesis, quartz crystal microbalance with dissipation monitoring   measurements revealed that a preadsorbed BSM layer stabilizes IgG   through complexation on a polymeric model surface. Our findings link   well to the complex in vivo situation and suggest that functional   mucosal mimics can be created in situ for improved biomaterials   performance.

Place, publisher, year, edition, pages
2009. Vol. 91A, no 3, 773-785 p.
Keyword [en]
mucin-based surface coatings, human neutrophil lipocalin (HNL), surface-exposed protein, protein stabilization, quartz crystalmicrobalance with dissipation monitoring (QCM-D)
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:uu:diva-97904DOI: doi:10.1002/jbm.a.32315ISI: 000271588800015PubMedID: 19051307OAI: oai:DiVA.org:uu-97904DiVA: diva2:173009
Available from: 2008-11-28 Created: 2008-11-28 Last updated: 2010-06-29Bibliographically approved
In thesis
1. On the Development of Mucin-based Biomaterial Coatings
Open this publication in new window or tab >>On the Development of Mucin-based Biomaterial Coatings
2008 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Owing to their key role in mucosal functioning as surface barriers with biospecific interaction potentials, the mucins are interesting candidates for use as surface modifiers in biomaterials applications.

In this work, “mild” fractionation procedures were used to prepare mucins of bovine (BSM), porcine (PGM), and human (MG1) origin. Biophysicochemical analysis showed the prepared mucins to differ in size, charge, conformation, and composition. In turn, these factors were shown to govern mucin adsorption on hydrophilic and hydrophobic model surfaces.

To enable for detailed coating analysis, methods for the qualitative and quantitative analysis of mucin-based coatings were developed. Of particular interest, a method for the determination of the fraction of surface-exposed, presumed bioactive proteins in a complex mucin coating was described.

It was shown, using microscopy and activation assays, that mucin precoating effectively suppresses the neutrophil response towards a polymeric model biomaterial. Under optimal coating conditions, all mucins performed equally well, thus indicating them to be functionally similar. Coating analysis suggested that efficient mucin surface-shielding is critical for good mucin coating performance.

Following a study on the complexation of albumin with preadsorbed mucin, we investigated the effect of mucin precoating on the conformation and neutrophil-activating properties of adsorbed host proteins. We found that mucin precoating greatly reduces the strong immune-response normally caused by adsorbed proinflammatory proteins (IgG and sIgA). Detailed coating analysis revealed that the fraction of surface-exposed protein in the mucin-protein composite influences the neutrophil response. Unexpectedly low neutrophil activation for composites containing near-monolayer concentrations of exposed IgG, suggested IgG to act synergistically with mucin on the surface. Conformational analysis supported this by showing that a preadsorbed mucin layer could stabilize adsorbed IgG through complexation. Our findings link well to the complex in vivo situation and suggest that functional mucosal mimics can be created in situ for improved biomaterials performance.

Place, publisher, year, edition, pages
Uppsala: Universitetsbiblioteket, 2008. 83 p.
Series
Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology, ISSN 1651-6214 ; 583
Keyword
Mucin, Biomaterial, Surface-exposed protein, XPS, Neutrophil, Cell morphology, SEM, QCM-D, Viscoelasticity, Protein-stabilization, HNL, Coating, MG1, BSM, PGM, SEC-MALS-RI, Mucin quantification, Protein adsorption, Ellipsometry
National Category
Dentistry
Identifiers
urn:nbn:se:uu:diva-9439 (URN)978-91-554-7368-6 (ISBN)
Public defence
2008-12-19, B21, BMC, Husargatan 3, 75123, Uppsala, 13:15
Opponent
Supervisors
Available from: 2008-11-28 Created: 2008-11-28 Last updated: 2010-12-14Bibliographically approved

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