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- W2783296263 abstract "Dysregulated secretion and extracellular activation of TGF-β1 stimulates myofibroblasts to accumulate disordered and stiff extracellular matrix (ECM) in fibrosis. Fibronectin immobilizes latent TGF-β binding protein-1 (LTBP-1) and thus stores TGF-β1 in the ECM. Because the ED-A fibronectin splice variant is prominently expressed in fibrosis and supports myofibroblast activation, we investigated whether ED-A promotes LTBP-1-fibronectin interactions. Using stiffness-tuneable substrates for human dermal fibroblast cultures, we showed that high ECM stiffness promotes expression and co-localization of LTBP-1 and ED-A fibronectin. When rescuing fibronectin-depleted fibroblasts with specific fibronectin splice variants, LTBP-1 bound more efficiently to ED-A fibronectin than to ED-B fibronectin and fibronectin lacking splice domains. Function blocking of the ED-A domain using antibodies and competitive peptides resulted in reduced LTBP-1 binding to ED-A fibronectin, reduced LTBP-1 incorporation into the fibroblast ECM, and reduced TGF-β1 activation. Similar results were obtained by blocking the heparin-binding stretch FNIII12-13-14 (HepII), adjacent to the ED-A domain in fibronectin. Collectively, our results suggest that the ED-A domain enhances association of the latent TGF-β1 by promoting weak direct binding to LTBP-1 and by enhancing heparin-mediated protein interactions through HepII in fibronectin." @default.
- W2783296263 created "2018-01-26" @default.
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- W2783296263 date "2018-01-01" @default.
- W2783296263 modified "2023-10-02" @default.
- W2783296263 title "The ED-A domain enhances the capacity of fibronectin to store latent TGF-β binding protein-1 in the fibroblast matrix" @default.
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- W2783296263 doi "https://doi.org/10.1242/jcs.201293" @default.
- W2783296263 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5897715" @default.
- W2783296263 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29361522" @default.
- W2783296263 hasPublicationYear "2018" @default.
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