Complement activation and cytokine production as consequences of immunological bioincompatibility of extracorporeal circuits

Jahns, G; Haeffner‐Cavaillon, Nicole; Nydegger, Urs E.; Kazatchkine, Michel D.

doi:10.1016/0267-6605(93)90017-2

Cited by 38 publications

(12 citation statements)

References 152 publications

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“…The bands at 75 kDa for C3 in Figure 7 represent the intact beta chain of C3, and the bands at 40 kDa most likely represent a fragment from cleavage of the alpha chain of C3b by factor I in the activation process. [40] With the notable exception of PEG350-ATH, AT was not detected on any of the surfaces, again in accord with the radiolabeling data which showed that ATH surfaces bound significantly more AT than any of the others. The strong AT response for the PEG350-ATH surface is striking, and suggests that this surface may be expected to have significant thrombin neutralizing activity in contact with blood.…”

Section: Ath Surface Density and Stabilitysupporting

confidence: 87%

Surface modification of polydimethylsiloxane with a covalent antithrombin–heparin complex to prevent thrombosis

Leung

Berry

Chan

et al. 2014

Journal of Biomaterials Science, Polymer Edition

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To prevent coagulation in contact with blood, polydimethylsiloxane (PDMS) was modified with an antithrombin-heparin (ATH) covalent complex using polyethylene glycol (PEG) as a linker/spacer. Using NHS chemistry, ATH was attached covalently to the distal chain end of the immobilized PEG linker. Surfaces were characterized by contact angle and X-ray photoelectron spectroscopy; attachment was confirmed by decrease in contact angles and an increase in nitrogen content as determined by X-ray photoelectron spectroscopy. Protein interactions in plasma were investigated using radiolabeled proteins added to plasma as tracers, and by immunoblotting of eluted proteins. Modification of PDMS with PEG alone was effective in reducing non-specific protein adsorption; attachment of ATH at the distal end of the PEG chains did not significantly affect protein resistance. It was shown that surfaces modified with ATH bound antithrombin selectively from plasma through the pentasaccharide sequence on the heparin moiety of ATH, indicating the ability of the ATH-modified surfaces to inhibit coagulation. Using thromboelastography, the effect of ATH modification on plasma coagulation was evaluated directly. It was found that initiation of coagulation was delayed and the time to clot was prolonged on PDMS modified with ATH/PEG compared to controls. For comparison, surfaces modified in a similar way with heparin were prepared and investigated using the same methods. The data suggest that the ATH-modified surfaces have superior anticoagulant properties compared to those modified with heparin.

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Section: Ath Surface Density and Stabilitysupporting

confidence: 87%

Surface modification of polydimethylsiloxane with a covalent antithrombin–heparin complex to prevent thrombosis

Leung

Berry

Chan

et al. 2014

Journal of Biomaterials Science, Polymer Edition

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“…Usually biomaterials activate the complement through the alternative pathway, even though the involvement of the classic pathway cannot be excluded (Jahns et al, 1993). Following transportation of the activated factors along the bloodstream, systemic effects are reported.…”

Section: Complementmentioning

confidence: 99%

Inflammatory Response to Metals and Ceramics

Pizzoferrato

Cenni

Ciapetti

et al. 2002

Integrated Biomaterials Science

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“…The activation of the complement system may occur as a surface-mediated immune response and is initiated, e.g., by adsorbed immunoglobulins (Igs)G and A, or other plasma proteins and carbohydrates. 1,2 The consequences of activation by natural or artificial surfaces are fairly well understood and are considered to be important for the control of propagation and extent of hemostasis 3,4 and inflammatory activation and clearance processes in blood and tissues. 1,2 Also, in a recent study it was indicated in mice that C3d, a surface-bound degradation fragment of the third complement protein (C3) bridges the complement system to acquired immunity via a strong potentiation of the immunogenicity when used as a molecular adjuvant.…”

Section: Introductionmentioning

confidence: 99%

Temporal studies on the deposition of complement on human colostrum IgA and serum IgG immobilized on methylated silicon

Tengvall

Askendal

Lundström

1997

J. Biomed. Mater. Res.

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The temporal deposition of selected complement proteins from human serum onto immobilized human colostrum immunoglobulin (Ig)A and human IgG on hydrophobic silicon was studied by ellipsometry-antibody techniques after incubations at 37 degrees C for up to 1 h. In parallel experiments the serum soluble iC3b, C4d, and Bb were detected by enzyme-linked immunosorbent assay techniques. The IgA-coated surfaces showed activation via the alternative pathway, and displayed a lag phase in the deposition of increased amounts of serum proteins, and anti-C3c and antiproperdin. Anti-IgG, -C1q, -C4, -factor H and -factor B were not deposited at any time to IgA surfaces. Upon coating of the surface with IgG, the classical pathway was rapidly activated and bound, then anti-C3c, antiproperdin, and after short serum incubation times, also anti-C1q and anti-IgG. When factor B-depleted or heat-treated sera were used, the observation was that properdin deposited onto IgG-coated surfaces from both. Ellipsometry and antibody techniques offer a convenient and rapid way to indicate the activation of the complement system on solid surfaces and facilitates a time-resolved determination of the activation pathway(s).

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Complement activation and cytokine production as consequences of immunological bioincompatibility of extracorporeal circuits

Cited by 38 publications

References 152 publications

Surface modification of polydimethylsiloxane with a covalent antithrombin–heparin complex to prevent thrombosis

Surface modification of polydimethylsiloxane with a covalent antithrombin–heparin complex to prevent thrombosis

Inflammatory Response to Metals and Ceramics

Temporal studies on the deposition of complement on human colostrum IgA and serum IgG immobilized on methylated silicon

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