A second cell-binding domain on fibronectin (RGDS-independent) for neurite extension of human neuroblastoma cells

Waite, Kathleen A.; Mugnai, Gabriele; Culp, Lloyd A.

doi:10.1016/0014-4827(87)90193-5

Cited by 42 publications

(44 citation statements)

References 53 publications

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“…Along its homology-repeat sequence with some diversity caused by alternative splicing of FN's pre-mRNA (Hynes, 19851, cellular FNs and plasma FN (pFN) share binding domains for matrix and cell surface moieties (Yamada, 1983;Buck and Horowitz, 1987;Culp et al, 1989). Analyses of the potential receptors for FNs have identified several cell surface molecules: the glycoprotein complex integrin (Tamkun et al, 1986;Ruoslahti and Pierschbacher, 1987), heparan sulfate proteoglycans (Laterra et al, 1983;Izzard et al, 1986;Woods et al, 1986;Culp et al, 1989), gangliosides (Kleinman et al, 1979;Yamada et al, 1981;Spie-gel et al, 1984;Cheresh et al, 1987;Mugnai et al, 1988b,c), and possibly others (Waite et al, 1987;Humphries et al, 1987).…”

Section: Fibronectin (Fn) Mediates Adhesion Of Mesenchymalmentioning

confidence: 99%

Modulation of fibronectin adhesive functions for fibroblasts and neural cells by chemically derivatized substrata

Lewandowska

Balachander

Sukenik

et al. 1989

Journal Cellular Physiology

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Adhesion responses of fibroblasts (Balb/c 3T3 cells) and human neuron-derived (Platt neuroblastoma) cells have been examined with plasma fibronectin (pFN) adsorbed to glass surfaces derivatized with an alkyl chain and six chemical end groups interfacing with the bound pFN to test regulation of pFN function. Using new derivatization protocols, the following surfaces have been tested in order of increasing polarity: [CH3], [C = C], [Br], [CN], [Diol], [COOH], and underivatized glass [( SiOH]). For all substrata, pFN bound equivalently using either a supersaturating amount of pFN or a subsaturating amount in competition with bovine albumin. Attachment of both cell types was also equivalent on all substrata. However, spreading/differentiation responses varied considerably. F-actin reorganization was tested in 3T3 cells with rhodamine-phalloidin staining. While stress fibers formed effectively on pFN-coated [SiOH] and [Br] substrata, only small linear bundles of F-actin and a few thin stress fibers were observed on the [COOH], [Diol], and [CN] substrata; the hydrophobic substrata [( CH3] and [C = C]) gave an intermediate response. When a synthetic peptide containing the Arg-Gly-Asp-Ser sequence required for integrin binding to FNs was included in the medium as an inhibitor, additional differences were noted: Stress fiber formation was completely inhibited on [SiOH] but not on [Br] and stress fiber formation was very sensitive to inhibition on the hydrophobic substrata while the F-actin patterns on the [CN] and [COOH] substrata were unaffected. Evaluation of neurite outgrowth by neuroblastoma cells on these substrata revealed both qualitative and quantitative differences as follows: [Diol] = [COOH] greater than [SiOH] much greater than [CN] = [Br] greater than [CH3] = [C = C]. While there was poor cytoplasmic spreading and virtually no neurites formed on the hydrophobic surfaces when pFN alone was adsorbed, neurite formation could be "rescued" if a mixture of pFN with an excess of bovine albumin was adsorbed, demonstrating complex conformational interactions between substratum-bound pFN and adhesion-inert neighboring molecules. In summary, these studies demonstrate that different chemical end groups on the substratum modulate pFN functions for cell adhesion, principally by affecting the conformation of these molecules rather than the amounts bound. Furthermore, these studies confirm multiple-receptor interactions with the FN molecules in cell type-specific adhesion patterns.(ABSTRACT TRUNCATED AT 400 WORDS)

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Section: Fibronectin (Fn) Mediates Adhesion Of Mesenchymalmentioning

confidence: 99%

Modulation of fibronectin adhesive functions for fibroblasts and neural cells by chemically derivatized substrata

Lewandowska

Balachander

Sukenik

et al. 1989

Journal Cellular Physiology

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“…In this type of investigation, neuroblastoma cells represent a particularly useful model, since differentiation, easily assayed on the basis of neurite emission, may be induced under well-controlled conditions, such as treatment with appropriate pharmacological agents (Abemayor and Sidell, 1989), and adhesion to matrix-adhesive proteins, e.g., fibronectin (Waite et al, 1987;Mugnai et al, 1988a,b;Arcangeli et al, 1993), vitronectin (Arcangeli et al, 1993) and laminin (Rossino et al, 1991).…”

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confidence: 99%

“…The LaN1 and Platt lines differentiate upon adhesion to fibronectin-coated substrata (Waite et al, 1987), while SY5Y cells are inducible to differentiation by retinoic acid (Pahlman et al, 1984).…”

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confidence: 99%

Inverse relationship between invasiveness and differentiative capacity in different human neuroblastoma cell lines

1997

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In order to clarify the relationship between invasiveness and loss of cellular differentiation in tumor cells, we studied the invasive properties on Matrigel of (a) a series of clones we isolated from human neuroblastoma LaN1 and Platt cell lines inducible to differentiation by adhesion on fibronectin, and (b) SY5Y human neuroblastoma cells inducible to differentiation by retinoic acid. We found that, regardless of the parental line, the more differentiated clones were scarcely invasive, while the less differentiated clones showed a higher degree of invasiveness. Differences in invasiveness between differentiated and non-differentiated neuroblastoma clones did not reflect differences in adhesiveness to laminin, the major component of Matrigel. The retinoic acid-sensitive SY5Y human neuroblastoma cells also reduced their invasiveness on Matrigel after differentiation induced by growth in media supplemented with retinoic acid. These results point to an inverse relationship between differentiative properties and invasiveness in human neuroblastoma cell lines.

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“…As a result, anti-gp 140 may be perturbing only one of the interactions involved in PC12 binding to FN. Selective interactions with RGDS-independent sites in F N has been demonstrated in neurite formation in peripheral and central nervous system cells (McCarthy et al, 1986;Rogers et al, 1987;Waite et al, 1987).…”

Section: Discussionmentioning

confidence: 99%

Modulation of growth factor induced fiber outgrowth in rat pheochromocytoma (PC12) cells by a fibronectin receptor antibody

Schwarz

Brown²,

Eveleth

et al. 1989

Journal Cellular Physiology

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Rat pheochromocytoma PC12 cells respond to the binding of nerve growth factor (NGF) and basic fibroblast growth factor (bFGF) by extending neurites in a manner resembling sympathetic neurons. This response requires cell attachment to an appropriate substratum (Fujii et al., J. Neurosci., 2:1157, 1982); attachment factors which function in this capacity include the adhesive proteins fibronectin and laminin. Incubating PC12 cells with a polyclonal antiserum directed against a putative 140-kDa fibroblast cell surface fibronectin receptor (anti-gp140) perturbed spreading but not attachment of the cells to fibronectin and laminin substrates. However, in the presence of anti-gp 140 or its Fab fragments, NGF-stimulated neurite outgrowth was dramatically reduced. The antibody also caused a retraction of previously extended neurites. SDS-PAGE analysis of immunoprecipitates of PC12 cells surface labeled with 125I identified a prominent 120-140-kDa band, suggesting that the site of anti-gp140 action in PC12 cells is also through a fibronectin receptor.

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A second cell-binding domain on fibronectin (RGDS-independent) for neurite extension of human neuroblastoma cells

Cited by 42 publications

References 53 publications

Modulation of fibronectin adhesive functions for fibroblasts and neural cells by chemically derivatized substrata

Modulation of fibronectin adhesive functions for fibroblasts and neural cells by chemically derivatized substrata

Inverse relationship between invasiveness and differentiative capacity in different human neuroblastoma cell lines

Modulation of growth factor induced fiber outgrowth in rat pheochromocytoma (PC12) cells by a fibronectin receptor antibody

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