lnu.sePublikasjoner
Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Inhibition of complement activation on a model biomaterial surface by streptococcal M protein-derived peptides
Högskolan i Kalmar, Naturvetenskapliga institutionen.
Högskolan i Kalmar, Naturvetenskapliga institutionen.
Högskolan i Kalmar, Naturvetenskapliga institutionen.
Lund University.ORCID-id: 0000-0002-1075-4346
Vise andre og tillknytning
2009 (engelsk)Inngår i: Biomaterials, ISSN 0142-9612, E-ISSN 1878-5905, Vol. 30, nr 13, s. 2653-2659Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The aim of this study was to evaluate a new approach to inhibit complement activation triggered by biomaterial surfaces in contact with blood. In order to inhibit complement activation initiated by the classical pathway (CP), we used streptococcal M protein-derived peptides that specifically bind human C4BP, an inhibitor of the CP. The peptides were used to coat polystyrene microtiter wells which served as a model biomaterial. The ability of coated peptides to bind C4BP and to attenuate complement activation via the CP (monitored as generation of fluid-phase C3a and binding of fragments of C3 and C4 to the surface) was investigated using diluted normal human serum, where complement activation by the AP is minimal, as well as serum from a patient lacking alternative pathway activation. Complement activation (all parameters) was significantly decreased in serum incubated in well surfaces coated with peptides. Total inhibition of complement activation was obtained at peptide coating concentrations as low as 1-5 mu g/mL. Successful use of Streptococcus-derived peptides shows that it is feasible to control complement activation at a model biomaterial surface by capturing autologous complement regulatory molecules from plasma. (C) 2009 Elsevier Ltd. All rights reserved.

sted, utgiver, år, opplag, sider
Elsevier, 2009. Vol. 30, nr 13, s. 2653-2659
Emneord [en]
Blood compatibility, Complement, C4b-binding protein (C4BP), In vitro test, Regulator of complement activation (RCA), Streptococcal M proteins
HSV kategori
Forskningsprogram
Biomedicinsk vetenskap, Immunologi
Identifikatorer
URN: urn:nbn:se:lnu:diva-73088DOI: 10.1016/j.biomaterials.2009.01.001ISI: 000264691200026PubMedID: 19171378OAI: oai:DiVA.org:lnu-73088DiVA, id: diva2:1199048
Tilgjengelig fra: 2018-04-19 Laget: 2018-04-19 Sist oppdatert: 2018-04-19bibliografisk kontrollert
Inngår i avhandling
1. Biomaterials and Hemocompatibility
Åpne denne publikasjonen i ny fane eller vindu >>Biomaterials and Hemocompatibility
2010 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

Biomaterials are commonly used in the medical clinic today; however, artificial materials can activate the cascade systems in the blood (complement-, coagulation-, contact- and fibrinolytic systems) as well as the platelets to various degrees. When an artificial surface comes in contact with blood, plasma proteins will be adsorbed to the surface within seconds. The composition of the layer of proteins differs between materials and is crucial for the hemocompatibility of the material.

This thesis includes five projects.

In Paper I the anticoagulants heparin and the thrombin inhibitor hirudin were evaluated in a whole blood model. Hirudin was found to be superior to low dose heparin since it did not affect the activation of the complement system nor the leukocytes. The most interesting observation was that expression of TF was seen on surface-attached monocytes in hirudin- treated blood but not heparin blood.

In Paper II peptides from the streptococcal M-protein, which has affinity for the human complement inhibitor C4BP, were attached to a polymeric surface. When being exposed to blood the endogenous complement regulator was enriched at the surface of the material, via the M-peptides. With this new approach we created a self-regulatory surface, showing significant lowered material-induced complement activation.

In Paper III apyrase, an enzyme which hydrolyzes nucleoside ATP and ADP, was immobilized on a polymer surface. Lower platelet activation and platelet-induced coagulation activation was seen for the apyrase-coated surface compared to control surfaces after exposure to whole human blood, due to the enzymes capability to degrade ADP released from activated platelets.

In Paper IV and V we synthesized an array of polymeric materials which were characterized regarding physical-chemical properties, adsorption of plasma proteins, and hemocompatibility. The polymers showed widely heterogeneous protein adsorption. Furthermore, when the polymers were exposed to whole blood, two of the materials showed superior hemocompatibility (monitored as complement- and coagulation activation), compared to the reference poly(vinyl chloride).

sted, utgiver, år, opplag, sider
Kalmar, Växjö: Linnaeus University Press, 2010. s. 167
Serie
Linnaeus University Dissertations ; 2/2010
Emneord
Complement, Coagulation, Whole blood, Biomaterials, Polymers and Hemocompatibility
HSV kategori
Forskningsprogram
Naturvetenskap, Biomedicinsk vetenskap
Identifikatorer
urn:nbn:se:lnu:diva-5437 (URN)978-91-86491-01-7 (ISBN)
Disputas
2010-01-29, N2007, Smålandsgatan 26, Kalmar, 09:30 (engelsk)
Opponent
Veileder
Tilgjengelig fra: 2010-04-30 Laget: 2010-04-29 Sist oppdatert: 2018-04-19bibliografisk kontrollert

Open Access i DiVA

Fulltekst mangler i DiVA

Andre lenker

Forlagets fulltekstPubMed

Personposter BETA

Engberg, Anna E.Sandholm, KerstinBexborn, FredrikNilsson Ekdahl, Kristina

Søk i DiVA

Av forfatter/redaktør
Engberg, Anna E.Sandholm, KerstinBexborn, FredrikPersson, JennyNilsson, BoNilsson Ekdahl, Kristina
Av organisasjonen
I samme tidsskrift
Biomaterials

Søk utenfor DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric

doi
pubmed
urn-nbn
Totalt: 21 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf