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Postadsorptive behavior of plasma proteins on poly(propylene oxide)-segmented nylon-610 surfaces and its implication in preventing contact-induced activation of platelets on these surfaces

1995; Taylor & Francis; Volume: 6; Issue: 2 Linguagem: Inglês

10.1163/156856294x00284

1568-5624

Yoshiyuki G. Takei, Nobuhiko Yui, Teruo Okano, Atsushi Maruyama, Kohei Sanui, Yasuhisa Sakurai, Naoya Ogata,

Dendrimers and Hyperbranched Polymers

The influence of adsorbed plasma proteins on preventing contact-induced activation of platelets on poly(propylene oxide) (PPO)-segmented nylon-610 surfaces was investigated by monitoring changes in cytoplasmic free Ca2+ concentrations in platelets and adsorption/desorption of albumin and fibrinogen on these copolymer surfaces. Direct measurement of cytoplasmic free Ca2+ concentration in platelets in contact with copolymer surfaces was achieved by monitoring spectral changes of a fluorescent indicator dye, Fura 2. These copolymers were characterized by a surface microstructure composed of coexisting crystalline and amorphous phases. An increase in cytoplasmic free Ca2+ concentration in platelets interacting with polymer surfaces was observed, and this increase was found to be strongly reduced both by the adsorption of plasma proteins onto the polymer surface and by modifying the surface microstructure of the polymer itself. Transient changes in cytoplasmic free Ca2+ concentration were observed in platelets in contact with the surface of copolymer 61P3-25, which exhibited excellent nonthrombogenicity in our previous studies, depending on the residence time of plasma and plasma concentration. Additionally, adsorption/desorption of albumin and fibrinogen on copolymer surfaces was estimated using 125I-labeled proteins. Exchange of the adsorbed albumin with fibrinogen and minimum fibrinogen adsorption were observed particularly on the 61P3-25 surface. Exchange of adsorbed fibrinogen with plasma proteins and/or increased fibrinogen adsorption were also observed on all other polymer surfaces examined. Finally, we conclude that controlled formation of a defined protein adsorption layer on the 61P3-25 surface via the transient exchange of adsorbed albumin with fibrinogen from plasma, can be a dominant factor in preventing platelet adhesion and activation on this surface.