Conformational changes of a model protein (complement factor 3) adsorbed on hydrophilic and hydrophobic solid surfaces

Elwing, Hans; Nilsson, Bo; Svensson, K.-E.; Askendahl, Agneta; Nilsson, Ulf; Lundström, Ingemar

doi:10.1016/0021-9797(88)90062-8

Cited by 98 publications

(47 citation statements)

References 25 publications

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“…This finding raises the question of whether adsorbed C3 is autoactivated and is able to trigger alternative pathway activation by binding factor B, thereby generating a surface-bound initiating C3,Bb convertase. In previous studies it has been suggested that adsorbed C3 can mediate alternative pathway activation in serum that is in contact with a polystyrene surface (19,21). In this work we show, by using a quartz microbalance technique (quartz crystal microbalance-dissipation (QCM-D)), that polystyrene-adsorbed purified C3 in the presence of factor B and properdin can form an initiating alternative pathway convertase that is able to cleave native C3.…”

mentioning

confidence: 72%

“…The binding of anti-C3(D) Abs to C3 adsorbed on a plastic surface can be completely inhibited by soluble SDS-denatured C3 but not by native C3 (19). This finding raises the question of whether adsorbed C3 is autoactivated and is able to trigger alternative pathway activation by binding factor B, thereby generating a surface-bound initiating C3,Bb convertase.…”

mentioning

confidence: 98%

“…It is interesting that the C3(D) epitopes of both purified C3 and C3b become exposed upon direct adsorption to a biomaterial surface, such as the plastic surface of a microtiter plate (19) or a nitrocellulose membrane (20). The binding of anti-C3(D) Abs to C3 adsorbed on a plastic surface can be completely inhibited by soluble SDS-denatured C3 but not by native C3 (19).…”

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confidence: 99%

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C3 Adsorbed to a Polymer Surface Can Form an Initiating Alternative Pathway Convertase

Andersson

Ekdahl

Larsson

et al. 2002

The Journal of Immunology

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134

109

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Contact between blood and a biomaterial surface induces an immediate complement-mediated inflammatory response. Under these conditions, the alternative pathway of complement is often initiated and amplified on the biomaterial surface. Adsorption of a protein such as C3 to a polymer surface induces conformational changes in the protein. Based on the expression on adsorbed C3 of conformational neoepitopes specific for bound C3 fragments, we have hypothesized that adsorbed C3 is able to bind factor B and form a functional C3,Bb convertase. Using a quartz crystal microbalance to monitor binding of proteins to a polymer surface, we have demonstrated that a functional C3-containing alternative pathway convertase can be formed, in particular, in the presence of properdin. These data indicate that adsorption of C3 induces conformational changes that turn C3 into a C3b-like molecule that is able to participate in the functioning of the alternative convertase, and they suggest a new mechanism for complement activation on a biomaterial surface.

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confidence: 72%

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confidence: 98%

mentioning

confidence: 99%

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C3 Adsorbed to a Polymer Surface Can Form an Initiating Alternative Pathway Convertase

Andersson

Ekdahl

Larsson

et al. 2002

The Journal of Immunology

Self Cite

134

109

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“…Proteins typically interact nonspecifically with foreign interfaces through hydrophobic and protein-material charge interactions often resulting in the unfolding of the native protein structure [65,66,71]. Disruption of protein conformation most often causes diminished or abolished native function and can trigger undesirable side effects at the implant surface.…”

Section: Chemical Surface Patterning Followed By Protein Adsorptionmentioning

confidence: 99%

“…Conversely, in the human body, specific molecular recognition events dictate protein interactions with native interfaces such as the basal lamina, cell surfaces, and the extracellular matrix. Such specific protein-protein interfacial interactions are a necessity of normal biological function and direct extracellular organization and define homeostasis.Proteins typically interact nonspecifically with foreign interfaces through hydrophobic and protein-material charge interactions often resulting in the unfolding of the native protein structure [65,66,71]. Disruption of protein conformation most often causes diminished or abolished native function and can trigger undesirable side effects at the implant surface.…”

mentioning

confidence: 99%

The effects of proteoglycan surface patterning on neuronal pathfinding

Hlady

Hodgkinson

2007

Materialwissenschaft Werkst

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Protein micropatterning techniques are increasingly applied in cell choice assays to investigate fundamental biological phenomena that contribute to the host response to implanted biomaterials, and to explore the effects of protein stability and biological activity on cell behavior for in vitro cell studies. In the area of neuronal regeneration the protein micropatterning and cell choice assays are used to improve our understanding of the mechanisms directing nervous system during development and regenerative failure in the central nervous system (CNS) wound healing environment. In these cell assays, protein micropatterns need to be characterized for protein stability, bioactivity, and spatial distribution and then correlated with observed mammalian cell behavior using appropriate model system for CNS development and repair. This review provides the background on protein micropatterning for cell choice assays and describes some novel patterns that were developed to interrogate neuronal adaptation to inhibitory signals encountered in CNS injuries. Rationale for studying the role of proteoglycans in CNS injuriesNeurons from the central nervous system (CNS) possess a limited capacity to regenerate beyond scar tissue formation barriers in injuries even in the presence of minimal trauma to tissue organization [1,2]. A major culprit in CNS neuronal regenerative failure are the inihibitory proteoglycans (PGs), which are upregulated at the site of CNS injuries. PGs are composed of a core protein with varying numbers of attached glycosaminoglycan (GAG) side chains [3,4]. Proteoglycans are first translated intracellularly into proteins in the endoplasmic reticulum, and then GAG chains are later attached in the Golgi apparatus before secretion into the extracellular space [5][6][7][8]. The study of PGs has particularly been pronounced in the field of neurobiology and development of the nervous system. Numerous studies have concluded that PGs act as barriers that direct the migration of neural crest cells and the outgrowth direction of pathfinding neurons during development [9][10][11][12][13][14][15][16][17]. A number of these studies have additionally shown that cell guidance by PGs is based on an inhibitory signal located within the chondroitin sulfate GAG chains [9,18,19], with the result that the artificial addition of chondroitin sulfate (CS) sugars to the developing nervous system disrupts normal pathfinding [20] as well as does the removal of chondroitin sulfate chains through enzymatic treatment [9,19]. Davies et al. found that chondroitin sulfate proteoglycans (CSPG) are a major constituent of the glial scar and that dorsal root ganglion (DRG) outgrowth termination coincided with an increase in CSPG expression density [21]. Other sources have also shown that CSPGs are upregulated after CNS injuries [22][23][24][25].Interestingly, native adult CNS neurons actually posses the intrinsic ability to regenerate when the wound healing environment is prepared by eliminating inhibitory factors [23,26,27]. In additi...

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In vitro evaluation of the inflammatory potential of the silk fibroin

Santin

Motta²,

Freddi³

et al. 1999

J. Biomed. Mater. Res.

415

230

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Silk fibroin membranes recently have been suggested as matrices for biomedical applications, such as guided tissue regeneration and burn wound dressings. The aim of this study was to evaluate the inflammatory potential of fibroin films and to compare the fibroin films with two model materials with completely different physico-chemical properties: poly(styrene) and poly(2-hydroxyethyl methacrylate). Fibroin bound lower levels of fibrinogen than did the two synthetic polymers while the same amounts of adsorbed human plasma complement fragment C3 and IgG were detected. Studies of the binding strength of C3 to fibroin, evaluated by a novel experimental procedure, indicated the occurrence of strong hydrophobic interactions at the interface. The activation of the mononuclear cells by fibroin, measured as interleukin 1beta production, was lower than the reference materials. Adhesion experiments showed the ability of the macrophages to adhere to fibroin by filopodia without a complete spreading of the cells. The results achieved in this study demonstrate that the interactions of fibroin with the humoral components of the inflammatory system were comparable with those of the two model surfaces while the degree of activation and adhesion of the immunocompetent cells appeared more limited.

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Conformational changes of a model protein (complement factor 3) adsorbed on hydrophilic and hydrophobic solid surfaces

Cited by 98 publications

References 25 publications

C3 Adsorbed to a Polymer Surface Can Form an Initiating Alternative Pathway Convertase

C3 Adsorbed to a Polymer Surface Can Form an Initiating Alternative Pathway Convertase

The effects of proteoglycan surface patterning on neuronal pathfinding

In vitro evaluation of the inflammatory potential of the silk fibroin

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