Bone Sialoprotein Coated on Glass and Plastic Surfaces Is Recognized by Different β3Integrins

Flores, Myra E.; Reinholt, Finn P.; Andersson, Göran

doi:10.1006/excr.1996.0247

Cited by 31 publications

(8 citation statements)

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“…Nevertheless, we have to emphasize that the precise mechanism behind this is still unknown. For example, conformational changes in adsorbed proteins may result in the protein being recognized by different integrins or may change the binding properties of the integrins 44. Evaluation of our cultures demonstrated that integrin subunits expressed by the U2OS cells include α2, α3, α5, α6, αv, and β1.…”

Section: Discussionmentioning

confidence: 91%

Initial interaction of U2OS cells with noncoated and calcium phosphate coated titanium substrates

Brugge

Dieudonné

Jansen

2002

J. Biomed. Mater. Res.

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From previous studies, we know that calcium phosphate (CaP) coated implants stimulate bone formation compared to uncoated implants. Nevertheless, the mechanism by which substrate surface characteristics affect cell function is unclear. In this study, we examined the initial interaction (30 min to 24 h) of U2OS cells with titanium substrates with or without a CaP coating. The effect of substrate roughness was also studied. When cell attachment was studied, we found that cells attached more readily to rough than to smooth surfaces. Also, more cells attached to the uncoated than to the CaP coated surface. After 24 h, cell numbers were similar for all substrate surfaces. Further, cells spread to a larger area on noncoated titanium than on the CaP coated substrates. At 24 h, the sequence of cell size was smooth titanium > rough titanium > CaP coated titanium. Shape measurements showed differences in cell shape between the cells on the different materials only at 7 h, not at different culture times. Cells expressed alpha2, alpha3, alpha5, alpha6, alphav, and beta1 subunits. Expression of alpha1, alpha4, alphavbeta3, beta3, beta4, and beta7 was extremely low or was not found. The beta1 integrin expression was higher on the coated than on the noncoated titanium at 3 h, but not on the other studied times. Expression of alpha2, alpha5, alpha6, and alphav expression was found to be upregulated at 24 h compared to earlier culture times on coated titanium, but not on uncoated titanium substrates. From this we conclude that the surface characteristics of a material (roughness and composition) can affect the initial interaction of cells with the material.

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Section: Discussionmentioning

confidence: 91%

Initial interaction of U2OS cells with noncoated and calcium phosphate coated titanium substrates

Brugge

Dieudonné

Jansen

2002

J. Biomed. Mater. Res.

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“…The multi-specific αVβ3 integrin was first identified as a vitronectin receptor, but has since been shown to bind several additional ECM ligands including fibrinogen, fibronectin, thrombospondin and bone sialoproteins (Lawler and Hynes, 1989;Horton, 1995;Flores et al, 1996). αVβ3 integrin has been heavily implicated in tumor development (Brooks et al, 1994(Brooks et al, , 1995, was correlated to reduced patient survival in colon carcinoma and melanoma (Albelda et al, 1990;Hieken et al, 1996), and has been associated with breast cancer cell metastasis to bone (Pecheur et al, 2002).…”

Section: Introductionmentioning

confidence: 96%

The type I collagen induction of MT1-MMP-mediated MMP-2 activation is repressed by αVβ3 integrin in human breast cancer cells

et al. 2007

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“…Proline arginine‐rich, end leucine‐rich repeat protein (PRELP) is a member of the leucine‐rich repeat family of proteoglycans that has been reported to be implicated in cell binding involving also heparan sulphate [16]. Bone sialoprotein (BSP) constitutes a bone ECM protein containing an Arg–Gly–Asp (RGD) sequence, which also has cell‐binding properties [17].…”

Section: Introductionmentioning

confidence: 99%

Differential Adherence of Osteoarthritis and Rheumatoid Arthritis Synovial Fibroblasts to Cartilage and Bone Matrix Proteins and its Implication for Osteoarthritis Pathogenesis

et al. 2004

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In osteoarthritis (OA), cartilage and bone fragments have been described within the synovial tissue which are surrounded by synovial cells (i.e. detritus synovitis). These cells appear to attach actively to the cartilage and bone fragments. In rheumatoid arthritis (RA), on the other hand, synovial fibroblasts (SF) have also been shown to be localized at sites of invasion into cartilage and bone and to degrade extracellular matrix (ECM) by secreting proteolytic enzymes. One prerequisite for exerting their aggressive properties is the attachment to cartilage and bone ECM. This attachment appears to be mediated by the expression of different adhesion molecules for which corresponding binding sites on ECM components are known. As it has not been addressed to which ECM proteins SF adhere and with which affinity this process takes place, we investigated the adherence of SF from patients with OA and RA to different cartilage and bone matrix proteins. Synovial tissue samples were obtained during synovectomy or arthroplastic surgery and used for isolating and culturing SF. Synovial cells attaching to cartilage/bone fragments were characterized using immunohistochemistry. The adherence of SF to ECM proteins was examined using an adhesion assay with the following proteins coated on 96-well plates: aggrecan (AGG), bone sialoprotein (BSP), cartilage oligomeric matrix protein (COMP), collagen type I, II and VI, proline arginine-rich, end leucine-rich repeat protein (PRELP

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Bone Sialoprotein Coated on Glass and Plastic Surfaces Is Recognized by Different β3Integrins

Cited by 31 publications

References 0 publications

Initial interaction of U2OS cells with noncoated and calcium phosphate coated titanium substrates

Initial interaction of U2OS cells with noncoated and calcium phosphate coated titanium substrates

The type I collagen induction of MT1-MMP-mediated MMP-2 activation is repressed by αVβ3 integrin in human breast cancer cells

Differential Adherence of Osteoarthritis and Rheumatoid Arthritis Synovial Fibroblasts to Cartilage and Bone Matrix Proteins and its Implication for Osteoarthritis Pathogenesis

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