uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Mucin coatings suppress neutrophil adhesion to a polymeric model biomaterial
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
2007 (English)In: Microscopy research and technique (Print), ISSN 1059-910X, E-ISSN 1097-0029, Vol. 70, no 10, 864-868 p.Article in journal (Refereed) Published
Abstract [en]

Following our recent study on the fractionation, characterization, and model adsorption of mucins derived from bovine salivary glands (BSM), porcine stomach scrapings (PGM), and human whole saliva (MG1), we here present a microscopic evaluation of the interactions between mucin-coated substrates and human neutrophils. Our results show that surface-coating with BSM, PGM, and MG1 can be effectively used to suppress the adhesion of neutrophils to a polymeric model biomaterial (Thermanox). Neutrophil morphologies found on Thermanox substrates coated with mucins resemble those observed for nonactivated neutrophils found in circulation. Notably, low neutrophil adhesion can be obtained at a significantly lower coating concentration (0.125 mg/mL) for the compositionally complex MG1 mucin than for the relatively pure BSM and PGM mucins (1 mg/mL). Furthermore, since coating at a low BSM and PGM concentration (0.25 mg/mL) results in higher cell counts and more spread cells than in the high-concentration case, we suggest that dense mucin surface packing is critical for good coating performance. In conclusion, the present study demonstrates how mucins from three different sources, of different compositional and structural status, efficiently can be used to suppress neutrophil adhesion and activation. This finding makes them potent candidates for use as biomaterial coatings.

Place, publisher, year, edition, pages
2007. Vol. 70, no 10, 864-868 p.
Keyword [en]
BSM, PGM, MG1, polymorphonuclear leukocyte, cell morphology, Thermanox, SEM
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:uu:diva-97901DOI: 10.1002/jemt.20489ISI: 000250150500004PubMedID: 17576123OAI: oai:DiVA.org:uu-97901DiVA: diva2:173006
Available from: 2008-11-28 Created: 2008-11-28 Last updated: 2011-01-20Bibliographically 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

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Authority records BETA

Sandberg, TomasCarlsson, Jan

Search in DiVA

By author/editor
Sandberg, TomasCarlsson, Jan
By organisation
Surface Biotechnology
In the same journal
Microscopy research and technique (Print)
Chemical Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 499 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf