2008
DOI: 10.1242/jcs.029819
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Abstract: Newly deposited microfibrils strongly colocalise with fibronectin in primary fibroblasts. Microfibril formation is grossly inhibited by fibronectin depletion, but rescued by supplementation with exogenous cellular fibronectin. As integrin receptors are key determinants of fibronectin assembly, we investigated whether they also influenced microfibril deposition. Analysis of β1-integrin-receptor-null fibroblasts, blockage of cell surface integrin receptors that regulate fibronectin assembly and disruption of Rho… Show more

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Cited by 122 publications
(141 citation statements)
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“…fibronectin (16,17), have been implicated in the initial stage of fibrillin-1 microfibril assembly. Thus, depletion of fibronectin fibrils, by either small interfering RNA knockdown or the peptide that blocks fibronectin matrix assembly, inhibited fibrillin-1 microfibril formation, although exogenously added fibronectin restored fibrillin-1 fibrils to the cells in which endogenous expression of fibronectin was knocked down (16,17). Fibrillin-1 is capable of binding to fibronectin through its C-terminal region, where it forms multimers (12) and thereby potentiates its fibronectin binding activity (16).…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…fibronectin (16,17), have been implicated in the initial stage of fibrillin-1 microfibril assembly. Thus, depletion of fibronectin fibrils, by either small interfering RNA knockdown or the peptide that blocks fibronectin matrix assembly, inhibited fibrillin-1 microfibril formation, although exogenously added fibronectin restored fibrillin-1 fibrils to the cells in which endogenous expression of fibronectin was knocked down (16,17). Fibrillin-1 is capable of binding to fibronectin through its C-terminal region, where it forms multimers (12) and thereby potentiates its fibronectin binding activity (16).…”
Section: Discussionmentioning
confidence: 99%
“…Fibrillin-1 and -2 have been shown to bind to fibronectin at their C-terminal regions (16). Interaction of fibrillin-1 with cell surface fibronectin deposits is critical for fibrillin-1 microfibril assembly, as inhibition of fibronectin matrix assembly results in diminished fibrillin-1 microfibril assembly (16,17). Fibrillin-1 also binds to heparin and heparan sulfate chains at multiple sites, of which the N-terminal region encoded by exons 1-11 exhibits the highest affinity for heparin (18,19).…”
mentioning
confidence: 99%
“…This suggests that collagenmatrix assembly is controlled by the signals from integrins and SFKs that stimulate RhoA-mediated contractility and drive fibronectin fibrillogenesis. Similarly, fibrillin-microfibril assembly is preceded by fibronectin fibrillogenesis and strongly depends on the binding of integrin α5β1 to fibronectin and subsequent RhoA-mediated cytoskeletal contractility (Kinsey et al, 2008).…”
Section: Extracellular-matrix Assemblymentioning
confidence: 99%
“…Similar to assembly of fibronectin, microfibril assembly requires 51 integrin (Kinsey et al, 2008), and fibronectin dimers further assemble into higher-order arrays through non-covalent associations with matrix, especially with fibrillin microfibrils (Ohashi and Erickson, 2009). In skin fibroblast cultures, assembly of fibrillin microfibrils is dependent upon fibronectin fibrillogenesis, and microfibrils colocalize with fibronectin during early matrix deposition in particular, whereas fibrillin-1 can also interact with fibronectin (Kinsey et al, 2008;Sabatier et al, 2009). LTBP-1 also colocalizes initially with fibronectin but subsequently adopts a distinct fibrillar arrangement (Taipale et al, 1996;Dallas et al, 2005).…”
Section: +mentioning
confidence: 99%