Monoclonal Antibody Against Human Fibronectin Which Inhibits Cell Attachment

Schoen, Robert C.; Bentley, Kevin L.; Klebe, Robert J.

doi:10.1089/hyb.1.1982.1.99

Cited by 102 publications

(63 citation statements)

References 24 publications

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“…2, region 2 and integrin-binding sites on adjacent monomer). This may relate to the observation that, at least for certain cell types, one mode of attachment to native type I collagen is fibronectin-dependent and is mediated by these integrin receptors (34). Moreover, the site of binding of the decorin core protein (35), which has been shown to interact with fibronectin (36), is also adjacent to several of the integrin-binding sites (19) (Fig.…”

Section: Distribution Of Ligand-binding Sites and Functional Domains mentioning

confidence: 97%

Mapping the Ligand-binding Sites and Disease-associated Mutations on the Most Abundant Protein in the Human, Type I Collagen

Lullo¹,

Sweeney²,

Körkkö³

et al. 2002

Journal of Biological Chemistry

817

546

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Type I collagen is the most abundant protein in humans, and it helps to maintain the integrity of many tissues via its interactions with cell surfaces, other extracellular matrix molecules, and growth and differentiation factors. Nearly 50 molecules have been found to interact with type I collagen, and for about half of them, binding sites on this collagen have been elucidated. In addition, over 300 mutations in type I collagen associated with human connective tissue disorders have been described. However, the spatial relationships between the known ligand-binding sites and mutation positions have not been examined. To this end, here we have created a map of type I collagen that includes all of its ligand-binding sites and mutations. The map reveals the existence of several hot spots for ligand interactions on type I collagen and that most of the binding sites locate to its C-terminal half. Moreover, on the collagen fibril some potentially relevant relationships between binding sites were observed including the following: fibronectin-and certain integrin-binding regions are near neighbors, which may mechanistically relate to fibronectin-dependent cell-collagen attachment; proteoglycan binding may potentially impact upon collagen fibrillogenesis, cell-collagen attachment, and collagen glycation seen in diabetes and aging; and mutations associated with osteogenesis imperfecta and other disorders show apparently nonrandom distribution patterns within both the monomer and fibril, implying that mutation positions correlate with disease phenotype. These and other observations presented here may provide novel insights into evaluating type I collagen functions and the relationships between its binding partners and mutations.

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Section: Distribution Of Ligand-binding Sites and Functional Domains mentioning

confidence: 97%

Mapping the Ligand-binding Sites and Disease-associated Mutations on the Most Abundant Protein in the Human, Type I Collagen

Lullo¹,

Sweeney²,

Körkkö³

et al. 2002

Journal of Biological Chemistry

817

546

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“…40,41 The antibody used (HFN7.1) was directed against the flexible linker between the 9 th and 10 th type III repeats of FN. 42 The antibody mAb1937 is directed against the 8 th type III repeat of FN. It has been previously demonstrated that HFN7.1 is a receptor-mimetic probe for integrin binding and cell adhesion.…”

Section: à2mentioning

confidence: 99%

Role of superhydrophobicity in the biological activity of fibronectin at the cell–material interface

et al. 2011

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Protein adsorption and cellular behavior depend strongly on the wettability of substrates. Such studies are scarce for surfaces exhibiting extreme values of contact angles. Fibronectin (FN) adsorption and adhesion of MC3T3-E1 cells were investigated on superhydrophobic polystyrene (SH-PS) surfaces and compared with the corresponding smooth polystyrene (PS) substrate and the control glass. The FN surface density was lower on the SH-PS than on PS, and the adsorbed protein showed altered conformation of cell adhesion domains, as obtained by ELISA with monoclonal antibodies. Cell adhesion occurred on the SH-PS without the formation of mature focal adhesions, as assessed by immunofluorescence for vinculin, talin and paxillin. Correspondingly, the development of the actin cytoskeleton was delayed and without the presence of defined F-actin fibers. FAK phosphorylation was reduced on SH-PS, as compared with PS and the control glass. Also, cell contractility was diminished on the SH-PS as revealed by phosphorylation of myosin light chain (pMLC). Likewise, FN reorganization and secretion were impaired on the superhydrophobic surfaces. Cell proliferation was significantly lower in SH-PS as compared with PS up to 21 days of culture.

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“…2C,F); fibroblasts seeded on FNIII 8,9,10 cross-linked glass (or plastic) remained spread in the presence or absence of TGF-β treatment (data not shown). As a complementary approach, we also pre-incubated pFNPAGs with HFN7.1, a monoclonal antibody that binds to the synergy site in FNIII 9 [16,17]. In contrast to control cultures, we observed that fibroblast contraction was inhibited and the cells retained a spread morphology in the presence of TGF-β (Fig.…”

Section: The Synergy/cell Binding Domain In Fn III 8-10 Supports Fibrmentioning

confidence: 97%

The fibronectin synergy site modulates TGF-β-dependent fibroblast contraction

Meckmongkol

Harmon

McKeown‐Longo

et al. 2007

Biochemical and Biophysical Research Communications

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Tissue remodeling following injury involves TGF-β-mediated fibroblast contraction. While these cells are embedded in a fibronectin (FN)-rich matrix, the role of FN-cell interactions in this process is not fully understood. To explore the role of FN matrix presentation, we analyzed the effect of TGF-β on fibroblasts adhered to FN-coated polyacrylamide gel (PAG). Surprisingly, under these conditions TGF-β triggered cell rounding/contraction. This was accompanied by increased Rho activation and MLCK phosphorylation and was reversed by inhibition of Rho kinase. Although fibroblasts are known to bind to fibronectin's RGD and synergy sites, their relative contribution to cell function is not clear. MLC phosphorylation was reduced and cell contraction was reversed when FN's synergy site was blocked, indicating that contraction requires signals from the synergy site in addition to TGF-β mediated Rho activation. Thus, regulating the FN synergy site therapeutically may provide a mechanism for modulating contractile forces during tissue repair.

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Monoclonal Antibody Against Human Fibronectin Which Inhibits Cell Attachment

Cited by 102 publications

References 24 publications

Mapping the Ligand-binding Sites and Disease-associated Mutations on the Most Abundant Protein in the Human, Type I Collagen

Mapping the Ligand-binding Sites and Disease-associated Mutations on the Most Abundant Protein in the Human, Type I Collagen

Role of superhydrophobicity in the biological activity of fibronectin at the cell–material interface

The fibronectin synergy site modulates TGF-β-dependent fibroblast contraction

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