The First Type III Repeat in Fibronectin Activates an Inflammatory Pathway in Dermal Fibroblasts

You, Ran; Zheng, Mingzhe; McKeown‐Longo, Paula J.

doi:10.1074/jbc.c110.176990

Cited by 46 publications

(57 citation statements)

References 31 publications

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“…It was shown that exposure of fibroblasts to FNIII1c, a stable unfolded intermediate of FNIII1, can elicit TLR4-dependent inflammatory signaling and induce cytokine synthesis. 41,42 This region of the fibronectin molecule is exposed through tensional forces within the rigid fibrotic microenvironment. These observations have clear implications for fibrosis, since fibrotic tissue is characterized by increased stiffness and mechanical forces.…”

Section: The Alternately-spliced Fibronectin Isoform Acts As An Endogmentioning

confidence: 99%

Toll-Like Receptor-4 Signaling Drives Persistent Fibroblast Activation and Prevents Fibrosis Resolution in Scleroderma

Bhattacharyya

Midwood

Yin

et al. 2017

Advances in Wound Care

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Section: The Alternately-spliced Fibronectin Isoform Acts As An Endogmentioning

confidence: 99%

Toll-Like Receptor-4 Signaling Drives Persistent Fibroblast Activation and Prevents Fibrosis Resolution in Scleroderma

Bhattacharyya

Midwood

Yin

et al. 2017

Advances in Wound Care

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“…50 Thus, in addition to integrins, Fn-fs, as an endogenous ligand of Toll-like receptors 2 and 4, could act through its engagement, given that both receptors are present in SF. 48,51 Moreover, both stimuli induce the activation of MAPK signaling, implicated in the activation of Runx2 and other transcription factors, such as the NF-kB, 13e15,46,52 which also induce the expression of Wnt. 53,54 Therefore, we can hypothesize that IL-1b and 45-kDa Fn-fs induce aggrecanases expression by activation of the transcription factor Runx2, mainly through the ERK-MAPK signaling.…”

Section: Q18mentioning

confidence: 99%

Healthy and Osteoarthritic Synovial Fibroblasts Produce a Disintegrin and Metalloproteinase with Thrombospondin Motifs 4, 5, 7, and 12

Pérez‐García

Gutiérrez‐Cañas

Seoane

et al. 2016

The American Journal of Pathology

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Current description of osteoarthritis includes the involvement of synovial inflammation. Studies contributing to understanding the mechanisms of cross-talk and feedback among the joint tissues could be relevant to the development of therapies that block disease progression. During osteoarthritis, synovial fibroblasts exposed to anomalous mechanical forces and an inflammatory microenvironment release factors such as a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) metalloproteinases that mediate tissue damage and perpetuate inflammation. We therefore studied the production of ADAMTS by synovial fibroblasts and their contribution to cartilage degradation. Moreover, we analyzed the implication of two mediators present in the osteoarthritis joint, IL-1b as proinflammatory cytokine, and 45-kDa fibronectin fragments as products of matrix degradation. We reported that synovial fibroblasts constitutively express and release ADAMTS 4, 5, 7, and 12. Despite the contribution of both mediators to the stimulation of Runx2 and Wnt/b-catenin signaling pathways, as well as to ADAMTS expression, promoting the degradation of aggrecan and cartilage oligomeric matrix protein from cartilage, fibronectin fragments rather than IL-1b played the major pathological role in osteoarthritis, contributing to the maintenance of the disease. Moreover, higher levels of ADAMTS 4 and 7 and a specific regulation of ADAMTS-12 were observed in osteoarthritis, suggesting them as new potential therapeutic targets. Therefore, synovial fibroblasts provide the biochemical tools to the chronicity and destruction of the osteoarthritic joints. (Am J Pathol 2016, -: 1e13; http:// dx

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“…9,[14][15][16][17] Upon adsorption to solid surfaces, the conformation of Fn at the interface appears to depend largely on the characteristics of the surface. Fn has been seen to adopt an extended conformations on hydrophilic surfaces and compact, globular conformations on hydrophobic surfaces 18,19 Furthermore, other factors such as surface chemistry and topography have been found to play an important role.…”

Section: Introductionmentioning

confidence: 99%

Experimental and computational examination of anastellin (FnIII1c)–polymer interactions

Mallinson

Cheung

Simionesie

et al. 2016

J Biomedical Materials Res

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Using a combination of experimental and computational approaches, the interaction between anastellin, a recombinant fragment of fibronectin, and representative biomaterial surfaces has been examined. Anastellin and superfibronectin, have been seen to exhibit anti-angiogenic properties and other properties that may make it suitable for consideration for incorporation into biomaterials. The molecular interaction was directly quantified by atomic force microscope (AFM) based force spectroscopy, complemented by adsorption measurements using quartz crystal microbalance (QCM). By AFM, it was found that the anastellin molecule facilitates a stronger adhesion on polyurethane films (72.0 pN nm -1 ) than on poly (methyl methacrylate) films (68.6 pN nm -1 ). However, this is not consistent with the QCM adsorption measurements which shows no significant difference.Molecular dynamics simulations of the behaviour of anastellin on polyurethane in aqueous solution were performed to rationalise the experimental data, and show that anastellin is capable of rapid adsorption to PU while its secondary structure is stable upon adsorption in water.

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The First Type III Repeat in Fibronectin Activates an Inflammatory Pathway in Dermal Fibroblasts

Cited by 46 publications

References 31 publications

Toll-Like Receptor-4 Signaling Drives Persistent Fibroblast Activation and Prevents Fibrosis Resolution in Scleroderma

Toll-Like Receptor-4 Signaling Drives Persistent Fibroblast Activation and Prevents Fibrosis Resolution in Scleroderma

Healthy and Osteoarthritic Synovial Fibroblasts Produce a Disintegrin and Metalloproteinase with Thrombospondin Motifs 4, 5, 7, and 12

Experimental and computational examination of anastellin (FnIII1c)–polymer interactions

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