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Interactions between surface‐bound actin and complement, platelets, and neutrophils
Author(s) -
Wetterö Jonas,
Askendal Agneta,
Tengvall Pentti,
Bengtsson Torbjörn
Publication year - 2003
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.10591
Subject(s) - actin binding protein , biophysics , actin , platelet , materials science , fluorescence microscope , platelet activation , chemistry , actin cytoskeleton , microbiology and biotechnology , fluorescence , cytoskeleton , biochemistry , cell , biology , immunology , physics , quantum mechanics
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 Mg 2+ 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