Immunoglobulin G and secretory fibronectin adsorption to silica

Jönsson, Ulf; Lundström, Ingemar; Rönnberg, Inger

doi:10.1016/0021-9797(87)90175-5

Cited by 48 publications

(29 citation statements)

References 20 publications

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“…24 This has been attributed to the ability of these cells to utilize several domains within fibronectin for attachment. 18,19 It is therefore possible that the unfolding of Fn that is likely to take place on a hydrophobic substrate 35,46 may expose multiple binding sites that could be exploited by HBDC even if access to the cell-binding region of Fn were compromised. In this context it is of great interest to observe that by far the highest potency for HBDC attachment was achieved by Fn when adsorbed onto the PEMA/THFMA substrate, implying a similar conformational change in the adsorbed protein.…”

Section: Discussionmentioning

confidence: 99%

“…A likely explanation is that when adsorbed onto these polymers, Vn adopts a conformation that is less favorable for cell attachment than when on TCPS. Surface chemistry plays a critical role in determining the conformation of adsorbed proteins, [35][36][37] , which then can reflect on their ability to bind cells: 15,19,[38][39][40][41][42][43] this conformational dependence has been demonstrated for both Fn 44 and Vn. 45 The surface densities of Vn and Fn adsorbed onto TCPS and PS from pure solution are consistent with previous studies, 24,37 showing Langmuir isotherms consistent with the low coating concentrations used.…”

Section: Discussionmentioning

confidence: 99%

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Attachment of cultured human bone cells to novel polymers

McFarland

Mayer

Scotchford

et al. 1999

J. Biomed. Mater. Res.

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The initial attachment of human bone-derived cells (HBDC) to several polymer systems has been studied in vitro. A novel polymer system based on poly(ethyl methacrylate) polymer and tetrahydrofurfuryl methacrylate monomer (PEMA/THFMA) was compared with a variant in which THFMA was replaced by 2-hydroxyethyl methacrylate (PEMA/HEMA). Tissue culture polystyrene (TCPS) and polystyrene (PS) were used as reference materials. The ability of the substrates to adsorb the attachment glycoproteins fibronectin (Fn) and vitronectin (Vn) from serum and the subsequent effect on radiolabeled HBDC attachment were examined. Initial cell attachment from the medium containing 10% (v/v) serum was highest on TCPS; on PEMA/THFMA and PEMA/HEMA substrates it was about 25% of this level, and on PS it was only 10% of that on TCPS. Attachment of HBDC to all substrates was dependent on the presence of Vn, which, unlike Fn, was able to adsorb in the face of competition from other serum components. Both Vn and Fn were able to support cell attachment when precoated onto all substrates. In comparison to TCPS, PEMA/THFMA did not show enhanced adsorption of either Fn or Vn from serum, and this was reflected in the level of cell attachment. Interestingly, the potency of preadsorbed Fn for cell attachment was much higher on this substrate than on any other: 45 ng/cm2 Fn when adsorbed to PEMA/THFMA gave a level of cell attachment 1.6-fold higher than the same density of Fn on PS or TCPS. The maximum Fn surface density achieved on HEMA/PEMA was 16 ng/cm2. Cells on PEMA/THFMA showed typical clustering of the alpha5 beta1 Fn receptor, but this was not evident in cells attached to PEMA/HEMA even when precoated with Fn. This study indicates that the initial attachment of HBDC to all substrates was Vn dependent. It also indicates that on PEMA/THFMA the favorable presentation of subsequently adsorbed Fn may assist matrix assembly.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Attachment of cultured human bone cells to novel polymers

McFarland

Mayer

Scotchford

et al. 1999

J. Biomed. Mater. Res.

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“…Adsorption studies of immunoglobulins to surfaces mainly involve IgG and its affinity for different surfaces, both hydrophobic and hydrophilic, investigated by various techniques (1)(2)(3)(4). Some work has been directed toward revealing how proteins interact with solid interfaces on a molecular level, for example, regarding their orientation and spatial distribution.…”

Section: Introductionmentioning

confidence: 99%

TM-AFM Threshold Analysis of Macromolecular Orientation: A Study of the Orientation of IgG and IgE on Mica Surfaces

Bergkvist

Carlsson

Karlsson

et al. 1998

Journal of Colloid and Interface Science

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“…These changes in conformation are more drastic on hydrophobic surfaces than on hydrophilic substrates (Iwamoto et al, 1985;Jonsson et al, 1987;Pitt et al, 1987;Narasimhan and Lai, 1989) and reflect differences in surface properties, such as surface energy and charge, which influence the Fn-substrate interaction. These changes in Fn conformation have been correlated with differences in antibody binding and cell adhesion and spreading rates (Grinnell and Feld, 1981;Iuliano et al, 1993;Underwood et al, 1993;Pettit et al, 1994;García et al, 1998a).…”

Section: Substrate-dependent Changes In Fn Conformationmentioning

confidence: 99%

Modulation of Cell Proliferation and Differentiation through Substrate-dependent Changes in Fibronectin Conformation

Garcı́a

Vega

Boettiger

1999

MBoC

615

549

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Integrin-mediated cell adhesion to extracellular matrices provides signals essential for cell cycle progression and differentiation. We demonstrate that substrate-dependent changes in the conformation of adsorbed fibronectin (Fn) modulated integrin binding and controlled switching between proliferation and differentiation. Adsorption of Fn onto bacterial polystyrene (B), tissue culture polystyrene (T), and collagen (C) resulted in differences in Fn conformation as indicated by antibody binding. Using a biochemical method to quantify bound integrins in cultured cells, we found that differences in Fn conformation altered the quantity of bound ␣ 5 and ␤ 1 integrin subunits but not ␣ v or ␤ 3 . C2C12 myoblasts grown on these Fn-coated substrates proliferated to different levels (B Ͼ T Ͼ C). Immunostaining for muscle-specific myosin revealed minimal differentiation on B, significant levels on T, and extensive differentiation on C. Differentiation required binding to the RGD cell binding site in Fn and was blocked by antibodies specific for this site. Switching between proliferation and differentiation was controlled by the levels of ␣ 5 ␤ 1 integrin bound to Fn, and differentiation was inhibited by anti-␣ 5 , but not anti-␣ v , antibodies, suggesting distinct integrin-mediated signaling pathways. Control of cell proliferation and differentiation through conformational changes in extracellular matrix proteins represents a versatile mechanism to elicit specific cellular responses for biological and biotechnological applications. INTRODUCTIONThe adhesion of cells to their substrate through an extracellular matrix provides signals that influence their ability to survive, proliferate, and express specific developmental phenotypes (Menko and Boettiger, 1987;Werb et al., 1989;Adams and Watt, 1990;Streuli et al., 1991;Zhu et al., 1996;Chen et al., 1997). One of the early examples was the development of in vitro culture conditions that permitted the differentiation of avian myogenic cells into contracting myotubes (Hauschka and Konigsberg, 1966;Bischoff and Holtzer, 1968). The critical element for this system was the precoating of tissue culture surfaces with rat tail collagen. This general principle of providing an appropriate substrate to permit the expression of developmental phenotypes has been applied to a wide variety of cells. These include systems that allow the maintenance of neurons and outgrowth of growth cones (Westerfield, 1987) and the recapitulation of the stages of mammary gland development and involution (Li et al., 1987;Barcellos-Hoff et al., 1989). These findings indicate that critical elements of the message directing the expression of a differentiated phenotype are encoded in the extracellular matrix.Cells interact with extracellular matrices primarily through integrins, a widely expressed family of cell surface receptors (Hynes, 1987), and integrin binding to its extracellular ligand is responsible for the downstream effects of the matrix on cell function. For example, in the muscle differentiation syste...

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Immunoglobulin G and secretory fibronectin adsorption to silica

Cited by 48 publications

References 20 publications

Attachment of cultured human bone cells to novel polymers

Attachment of cultured human bone cells to novel polymers

TM-AFM Threshold Analysis of Macromolecular Orientation: A Study of the Orientation of IgG and IgE on Mica Surfaces

Modulation of Cell Proliferation and Differentiation through Substrate-dependent Changes in Fibronectin Conformation

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