Interactions between surface-bound actin and complement, platelets, and neutrophils
2003 (English)In: Journal of Biomedical Materials Research, ISSN 0021-9304, E-ISSN 1097-4636, Vol. 66A, no 1, 162-175 p.Article in journal (Refereed) Published
Actin exists as globular (G) monomers or polymeric filaments (F) in the cytoplasm of eukaryotic cells, mediating cell morphologic changes and motility. Large amounts of this protein may be released out to the extracellular compartment during tissue injury, but little is known about its role in biomaterial-related inflammation. We immobilized actin to methylated glass, methylated and aminated silicon, and gold model surfaces and studied the subsequent blood serum deposition and complement activation, generation of reactive oxygen species (ROS), and adhesion and aggregation of neutrophils and platelets. Null ellipsometry showed that approximately one monolayer of G-actin can be immobilized onto the model surfaces and that actin in buffer polymerized on top of this by the addition of K+ and Mg2+ ions to form a thicker layer of firmly bound F-actin. After serum incubation, F-actin bound low amounts of anti-complement factor 1q (anti-C1q). Cell responses upon contact with actin-coated surfaces were analyzed by luminol-amplified chemiluminescence, lumi-aggregometry, and fluorescence microscopy. It was shown that surface-triggered aggregation, spreading, and generation of ROS are down-regulated and comparable to the response by adsorbed albumin. However, F-actin on gold surfaces recruited platelets in a C1q-dependent manner. We conclude that in vitro adsorbed actin is a weak complement, platelet, and neutrophil activator, but that F-actin associates with both C1q and platelets. © 2003 Wiley Periodicals, Inc. J Biomed Mater Res 66A: 162–175, 2003
Place, publisher, year, edition, pages
2003. Vol. 66A, no 1, 162-175 p.
reactive oxygen species, aggregation, biomaterials, cytoskeleton, plasma proteins
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:liu:diva-47776DOI: 10.1002/jbm.a.10591OAI: oai:DiVA.org:liu-47776DiVA: diva2:268672