The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
The fibronectin ED-A domain enhances recruitment of latent TGF-β-binding protein-1 to the fibroblast matrix
Open accessAbstract
Dysregulated secretion and extracellular activation of TGF-β1 stimulates myofibroblasts to accumulate disordered and stiff extracellular matrix (ECM) leading to 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 during 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 colocalization of LTBP-1 and ED-A-containing fibronectin. When rescuing fibronectin-depleted fibroblasts with specific fibronectin splice variants, LTBP-1 bound more efficiently to ED-A-containing fibronectin than to ED-B-containing 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-containing 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.
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Myofibroblasts and mechano-regulation of connective tissue remodelling
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Self-citationMechanisms of fibrosis: therapeutic translation for fibrotic disease
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Myofibroblast contraction activates latent TGF-β1 from the extracellular matrix
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Self-citationLatent TGF-β structure and activation
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An essential role for fibronectin extra type III domain A in pulmonary fibrosis
Muro, A. F., Moretti, F. A., Moore, B. B., Yan, M., Atrasz, R. G., Wilke, C. A., Flaherty, K. R., Martinez, F. J., Tsui, J. L., Sheppard, D., et al. (2008) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200708-1291oc · Cited by 297
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Transforming growth factor–β in tissue fibrosis
Frangogiannis, N. G. (2020) · Journal of Experimental Medicine · doi:10.1084/jem.20190103 · Cited by 1,278
Frangogiannis, N. G. (2021) · Cardiovascular Research · doi:10.1093/cvr/cvaa324 · Cited by 1,229
TGF-β in Hepatic Stellate Cell Activation and Liver Fibrogenesis—Updated 2019
Dewidar, B., Meyer, C., Dooley, S., & Meindl-Beinker, A. N. (2019) · Cells · doi:10.3390/cells8111419 · Cited by 837
The extracellular matrix as a multitasking player in disease
Theocharis, A. D., Manou, D., & Karamanos, N. K. (2019) · The FEBS Journal · doi:10.1111/febs.14818 · Cited by 511
TGF-β1 – A truly transforming growth factor in fibrosis and immunity
Lodyga, M., & Hinz, B. (2020) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2019.12.010 · Cited by 458
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Metadata
- Authors
- Klingberg, F., Chau, G., Walraven, M., Boo, S., Koehler, A., Chow, M. L., Olsen, A. L., Im, M., Lodyga, M., Wells, R. G., White, E. S., & Hinz, B.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2018-03-01
- Volume
- 131
- Issue
- 5
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2783296263
- Cited by
- 169
- References
- 11
- FWCI
- 5.34
- Type
- journal article
- Language
- en
- Open access
- green
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- Klingberg, F., Chau, G., Walraven, M., Boo, S., Koehler, A., Chow, M. L., Olsen, A. L., Im, M., Lodyga, M., Wells, R. G., White, E. S., & Hinz, B. (2018). The fibronectin ED-A domain enhances recruitment of latent TGF-β-binding protein-1 to the fibroblast matrix. Journal of Cell Science. https://doi.org/10.1242/jcs.201293
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