Polystyrene chemistry affects vitronectin activity: An explanation for cell attachment to tissue culture polystyrene but not to unmodified polystyrene

Steele, John G.; Dalton, B. A.; Johnson, Graham; Underwood, P.A.

doi:10.1002/jbm.820270712

Cited by 135 publications

(112 citation statements)

References 46 publications

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“…Cell adhesion to several material surfaces is dependent on the prior adsorption of specific serum proteins, including fibronectin and vitronectin, 53 which support cell attachment to the surface and influence cell morphology. [54][55][56] In this study, we demonstrated that hMSC morphology was affected by the underlying surface topography, specifically in terms of cell spread and the number of filopodia. Differences in the amount of serum proteins deposited on the investigated surfaces may account for the observed variation in cell morphology.…”

Section: Discussionmentioning

confidence: 71%

Osteogenic response of human mesenchymal stem cells to well-defined nanoscale topography in vitro

Peppo¹,

Agheli²,

Karlsson³

et al. 2014

IJN

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Background Patterning medical devices at the nanoscale level enables the manipulation of cell behavior and tissue regeneration, with topographic features recognized as playing a significant role in the osseointegration of implantable devices. Methods In this study, we assessed the ability of titanium-coated hemisphere-like topographic nanostructures of different sizes (approximately 50, 100, and 200 nm) to influence the morphology, proliferation, and osteogenic differentiation of human mesenchymal stem cells (hMSCs). Results We found that the proliferation and osteogenic differentiation of hMSCs was influenced by the size of the underlying structures, suggesting that size variations in topographic features at the nanoscale level, independently of chemistry, can be exploited to control hMSC behavior in a size-dependent fashion. Conclusion Our studies demonstrate that colloidal lithography, in combination with coating technologies, can be exploited to investigate the cell response to well defined nanoscale topography and to develop next-generation surfaces that guide tissue regeneration and promote implant integration.

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Section: Discussionmentioning

confidence: 71%

Osteogenic response of human mesenchymal stem cells to well-defined nanoscale topography in vitro

Peppo¹,

Agheli²,

Karlsson³

et al. 2014

IJN

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“…However, ␣ v ␤ 3 integrin is a major contributor in adhesion of HSCs to tissue culture plastic as our previous studies showed that echistatin effectively blocks adhesion of HSCs to this substrate (31). The HSCs in our studies were routinely plated in media containing relatively high concentrations of FCS, a rich source of soluble fibronectin and vitronectin, which bind to tissue culture plastic and might act as an ␣ v ␤ 3 -dependent adhesive layer for the cells (60).…”

Section: Discussionmentioning

confidence: 92%

Engagement of αvβ3 Integrin Regulates Proliferation and Apoptosis of Hepatic Stellate Cells

Zhou¹,

Murphy²,

Gehdu³

et al. 2004

Journal of Biological Chemistry

202

160

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Hepatic stellate cells are the major source of the extracellular matrix that accumulates in fibrotic liver. During progressive liver fibrosis, hepatic stellate cells proliferate, but during resolution of fibrosis there is extensive stellate cell apoptosis that coincides with degradation of the liver scar. We have examined the possibility that the fate of stellate cells is influenced by the extracellular matrix through the intermediary of ␣ v ␤ 3 integrin. ␣ v ␤ 3 integrin was expressed by activated, myofibroblastic rat and human stellate cells in culture. Antagonism of this integrin using neutralizing antibodies, echistatin, or small inhibitory RNA to silence ␣ v subunit expression inhibited stellate cell proliferation and their expression of proliferating cell nuclear antigen and activated forms of p44 and p42 MAPK. These ␣ v ␤ 3 antagonists also increased apoptosis of cultured stellate cells, and this was associated with an increase in the BAX/ BCL-2 protein ratio, induction of nuclear DNA fragmentation, and activation of intracellular caspase-3. Expression of tissue inhibitor of metalloproteinases-1 by activated stellate cells was reduced by the ␣ v ␤ 3 antagonists, while matrix metalloproteinase-9 synthesis was enhanced. Stellate cells incubated with active recombinant matrix metalloproteinase-9 showed enhanced apoptosis, while cells treated with a synthetic inhibitor of this protease showed increased survival. Our studies suggest that ␣ v ␤ 3 integrin regulates the fate of hepatic stellate cells. Degradation of ␣ v ␤ 3 ligands surrounding activated stellate cells during resolution of liver fibrosis might decrease ␣ v ␤ 3 integrin ligation, suppressing stellate cell proliferation and inducing a fibrolytic, matrix metalloproteinase-secreting phenotype that may prime stellate cells for apoptosis.

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“…Subsequently, vitronectin was specifically bound via the corresponding epitope recognized by the solidphase antibody. Immobilizing vitronectin in an immunospecific fashion such as this avoids conformational perturbations that are known to occur when vitronectin is adsorbed to plastic surfaces (37)(38)(39). This was reasoned to be a better approach for testing effects of blocking both epitopes on vitronectin because all vitronectin bound to the solid-phase is, by design, blocked at one epitope.…”

Section: Monoclonal Antibodies Specific For Different Epitopes On Vitmentioning

confidence: 99%

New Insights into the Size and Stoichiometry of the Plasminogen Activator Inhibitor Type-1·Vitronectin Complex

Podor¹,

Shaughnessy²,

Blackburn³

et al. 2000

Journal of Biological Chemistry

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Plasminogen activator inhibitor-type 1 (PAI-1) is the primary inhibitor of endogenous plasminogen activators that generate plasmin in the vicinity of a thrombus to initiate thrombolysis, or in the pericellular region of cells to facilitate migration and/or tissue remodeling. It has been shown that the physiologically relevant form of PAI-1 is in a complex with the abundant plasma glycoprotein, vitronectin. The interaction between vitronectin and PAI-1 is important for stabilizing the inhibitor in a reactive conformation. Although the complex is clearly significant, information is vague regarding the composition of the complex and consequences of its formation on the distribution and activity of vitronectin in vivo. Most studies have assumed a 1:1 interaction between the two proteins, but this has not been demonstrated experimentally and is a matter of some controversy since more than one PAI-1-binding site has been proposed within the sequence of vitronectin. To address this issue, competition studies using monoclonal antibodies specific for separate epitopes confirmed that the two distinct PAI-1-binding sites present on vitronectin can be occupied simultaneously. Analytical ultracentrifugation was used also for a rigorous analysis of the composition and sizes of complexes formed from purified vitronectin and PAI-1. The predominant associating species observed was high in molecular weight (M r ϳ 320,000), demonstrating that self-association of vitronectin occurs upon interaction with PAI-1. Moreover, the size of this higher order complex indicates that two molecules of PAI-1 bind per vitronectin molecule. Binding of PAI-1 to vitronectin and association into higher order complexes is proposed to facilitate interaction with macromolecules on surfaces.Vitronectin is a versatile glycoprotein that is found in circulation, in the extracellular matrix of endothelial cells, in platelets, and within various tissues of the human body. Circulating at micromolar levels, vitronectin participates in the regulation of humoral responses such as coagulation, fibrinolysis, and the complement cascade (reviewed in Ref. [1][2][3][4]. Other functions of the protein that are confined to surfaces or tissues include cell-adhesion and regulation of pericellular proteolysis. Interactions with an assortment of biological molecules are responsible for the multiple functions exhibited by vitronectin. Defining the binding sites for these various biomolecules, along with determining the molecular mechanism of regulation, constitutes an active area of research on the protein. Work to date has focused on binding sites for several ligands, including heparin, PAI-1, 1 and integrins; a working model representing the domain structure of vitronectin has been recently reported from this laboratory (5).Arguably, one of the most important interactions known for vitronectin occurs with the serine protease inhibitor, PAI-1. PAI-1 is the physiological inhibitor of plasminogen activators, both tPA and uPA, the enzymes responsible for generating plasmin from...

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Polystyrene chemistry affects vitronectin activity: An explanation for cell attachment to tissue culture polystyrene but not to unmodified polystyrene

Cited by 135 publications

References 46 publications

Osteogenic response of human mesenchymal stem cells to well-defined nanoscale topography in vitro

Osteogenic response of human mesenchymal stem cells to well-defined nanoscale topography in vitro

Engagement of αvβ3 Integrin Regulates Proliferation and Apoptosis of Hepatic Stellate Cells

New Insights into the Size and Stoichiometry of the Plasminogen Activator Inhibitor Type-1·Vitronectin Complex

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