Complement activation by sulfonated poly(ethylene glycol)-acrylate copolymers through alternative pathway

Jang, Hong Seok; Ryu, Kyu Eun; Ahn, Woong Shick; Chun, Heung Jae; Park, Hyung Dal; Парк, Ки Донг; Kim, Young Ha

doi:10.1016/j.colsurfb.2006.03.024

Cited by 12 publications

(10 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The effect of end groups of the PEOs on complement activation was reported recently. Poly(ethylene glycol) (PEG)–acrylate films were found to be more complement activating than sulfonated PEG–acrylate films,20 which was attributed to the exposed hydroxyl group on the PEG–acrylate films. Both intact and cleaved C3 adsorb on PEO‐thiols on gold surfaces21 after incubation with plasma.…”

Section: Introductionmentioning

confidence: 99%

Complement activation on poly(ethylene oxide)‐like radiofrequency glow discharge–deposited surfaces

Szott

Stein

Ratner

et al. 2010

J Biomedical Materials Res

View full text Add to dashboard Cite

Non-specific protein adsorption, particularly fibrinogen (Fg), is thought to be an initiating step in the foreign body response (FBR) to biomaterials by promoting phagocyte attachment. In previous studies, we therefore prepared radio frequency glow discharge (RFGD) polyethylene oxide (PEO)-like tetraglyme coatings (CH 3 O(CH 2 CH 2 O) 4 CH 3 ) adsorbing less than 10 ng/cm 2 Fg and showed that they had the expected low monocyte adhesion in vitro. However, when these were implanted in vivo, many adherent inflammatory cells and a fibrous capsule were found, suggesting the role of alternative proteins, such as activated complement proteins, in the FBR to these materials. We therefore investigated complement interactions with the tetraglyme surfaces. First, because of its well known role in complement C3 activation, we measured the hydroxyl group (-OH) content of tetraglyme, but found it to be very low. Second, we measured C3 adsorption to tetraglyme from plasma. Low amounts of C3 adsorbed on tetraglyme, though it displayed higher binding strength than the control surfaces. Finally, complement activation was determined by measuring C3a and SC5b-9 levels in serum after incubating with tetraglyme, as well as other surfaces that served as positive and negative controls, namely poly(vinyl alcohol) hydrogels, Silastic sheeting, and poly(ethylene glycol) self-assembled monolayers with different end groups. Despite displaying low hydroxyl group concentration, relatively high C3a and SC5b-9 levels were found in serum exposed to tetraglyme, similar to the values due to our positive control, PVA. Our results support the conclusion that complement activation by tetraglyme is a possible mechanism involved in the FBR to these biomaterials.

show abstract

Section: Introductionmentioning

confidence: 99%

Complement activation on poly(ethylene oxide)‐like radiofrequency glow discharge–deposited surfaces

Szott

Stein

Ratner

et al. 2010

J Biomedical Materials Res

View full text Add to dashboard Cite

show abstract

“…However, the presence of hydroxyl and amine groups is not necessary for the adsorption of C3 to a biomaterial,28 and recent studies have shown that C3 adsorbs to PEO‐thiols on gold surfaces from plasma solutions24 and to PEG‐hydrogels from serum solutions 29. Furthermore, a number of studies have recently reported the effect of end groups of PEO surfaces on complement activation 24, 30–32. Thus, the studies presented here were primarily designed to elucidate the role of complement C3 in monocyte adhesion to tetraglyme coatings in vitro.…”

Section: Introductionmentioning

confidence: 99%

“…29 Furthermore, a number of studies have recently reported the effect of end groups of PEO surfaces on complement activation. 24,[30][31][32] Thus, the studies presented here were primarily designed to elucidate the role of complement C3 in monocyte adhesion to tetraglyme coatings in vitro. Radiolabeled Fg and pure C3 were used to measure the amount of adsorption of each protein to tetraglyme coated and the uncoated control surfaces.…”

Section: Introductionmentioning

confidence: 99%

The role of complement C3 and fibrinogen in monocyte adhesion to PEO‐like plasma deposited tetraglyme

Szott

Horbett

2010

J Biomedical Materials Res

View full text Add to dashboard Cite

The role of complement C3 in mediating adhesion of monocytes to plasma deposited tetraglyme surfaces was studied. Although fibrinogen (Fg) is usually considered the main factor in mediating phagocyte attachment, plasma deposited PEO-like tetraethylene glycol dimethyl ether (tetraglyme) coatings that have ultra-low Fg adsorption (< 10 ng/cm 2 ) from low concentration solutions and low monocyte adhesion in vitro still show high phagocyte adhesion after short implantations and later become encapsulated when tested in vivo. To test whether higher Fg adsorption under in vivo conditions could explain the higher in vivo reactivity, we again measured the resistance of tetraglyme films to Fg adsorption. We found a surprising and previously unreported increased amount of adsorbed Fg on tetraglyme surfaces from higher concentration protein solutions. However, monocyte adhesion to tetraglyme did not markedly increase despite the increased Fg adsorption. We thus suspected proteins other than Fg must be responsible for the increased in vivo reactivity. We found that on tetraglyme pre-adsorbed with C3-depleted serum, monocyte adhesion was greatly reduced as compared to samples adsorbed with normal serum. Addition of exogenous pure C3 to the serum used to pre-adsorb the surfaces restored monocyte adhesion to tetraglyme coatings. While Fg clearly plays an important role in mediating monocyte adhesion to tetraglyme surfaces, the results show an additional role for adsorbed C3 in monocyte adhesion.

show abstract

“…Complement activation by biomaterials has been studied using enzyme-linked immunosorbent assay (ELISA) [8][9][10][11][12][13][14]. In these experiments, complement fragments, such as C3a, iC3b, C5a, and SC5b-9, released into serum were determined after exposure of sample surfaces to human serum.…”

Section: Comparison To Other Analytical Techniquesmentioning

confidence: 99%

“…Complement fragments, such as C3a, iC3b, C5a, and SC5b-9, are released when artificial surfaces are exposed to serum. The interaction of complement proteins with material surfaces has been studied using enzyme-linked immunosorbent assay (ELISA) for these complement fragments study [8][9][10][11][12][13][14]. Recently, various analytical techniques have been examined to study biomaterials, but few of these are able to monitor dynamic interactions under physiological conditions.…”

Section: Introductionmentioning

confidence: 99%

Surface plasmon resonance in monitoring of complement activation on biomaterials

Arima

Toda

Iwata

2011

Advanced Drug Delivery Reviews

View full text Add to dashboard Cite

When artificial materials come into contact with blood, various biological responses are induced. For successful development of biomaterials used in biomedical devices that will be exposed to blood, understanding and control of these interactions are essential. Surface plasmon resonance (SPR) spectroscopy is one of the surface-sensitive optical methods to monitor biological interactions. SPR enables real-time and in situ analysis of interfacial events associated with biomaterials research. In this review, we describe an SPR biosensor and its application to monitor complement activation onto biomaterials surface. We also discuss the effect of surface properties of the material on complement activation.

show abstract

Complement activation by sulfonated poly(ethylene glycol)-acrylate copolymers through alternative pathway

Cited by 12 publications

References 23 publications

Complement activation on poly(ethylene oxide)‐like radiofrequency glow discharge–deposited surfaces

Complement activation on poly(ethylene oxide)‐like radiofrequency glow discharge–deposited surfaces

The role of complement C3 and fibrinogen in monocyte adhesion to PEO‐like plasma deposited tetraglyme

Surface plasmon resonance in monitoring of complement activation on biomaterials

Contact Info

Product

Resources

About