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Mechanical regulation of myofibroblast phenoconversion and collagen contraction
Abstract
Activated fibroblasts promote physiological wound repair following tissue injury. However, dysregulation of fibroblast activation contributes to the development of fibrosis by enhanced production and contraction of collagen-rich extracellular matrix. At the peak of their activities, fibroblasts undergo phenotypic conversion into highly contractile myofibroblasts by developing muscle-like features, including formation of contractile actin-myosin bundles. The phenotype and function of fibroblasts and myofibroblasts are mechanically regulated by matrix stiffness using a feedback control system that is integrated with the progress of tissue remodelling. The actomyosin contraction machinery and cell-matrix adhesion receptors are critical elements that are needed for mechanosensing by fibroblasts and the translation of mechanical signals into biological responses. Here, we focus on mechanical and chemical regulation of collagen contraction by fibroblasts and the involvement of these factors in their phenotypic conversion to myofibroblasts.
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“During fibroblast-to-myofibroblast transition, a complex mechanochemical signaling is activated involving profibrotic secreted factors such as TGFβ and Wnt and ECM-degrading enzymes and intracellular effectors required for stress fiber contractility [127,131].”
From Cellular and Molecular Mechanisms in the Pathogenesis of Classical, Vascular, and Hypermobile Ehlers‒Danlos Syndromes (2019) · cites this paper as [131]
Citations
Cites
Myofibroblasts and mechano-regulation of connective tissue remodelling
Tomasek, J. J., Gabbiani, G., Hinz, B., Chaponnier, C., & Brown, R. A. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm809 · Cited by 4,290
Self-citationTGF-β: the master regulator of fibrosis
Meng, X.-M., Nikolic-Paterson, D. J., & Lan, H. Y. (2016) · Nature Reviews Nephrology · doi:10.1038/nrneph.2016.48 · Cited by 3,528
Mechanotransduction Across the Cell Surface and Through the Cytoskeleton
Wang, N., Butler, J. P., & Ingber, D. E. (1993) · Science · doi:10.1126/science.7684161 · Cited by 3,007
Non-muscle myosin II takes centre stage in cell adhesion and migration
Vicente‐Manzanares, M., Ma, X., Adelstein, R. S., & Horwitz, A. R. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2786 · Cited by 2,137
Mechanotransduction and extracellular matrix homeostasis
Humphrey, J. D., Dufresne, E. R., & Schwartz, M. A. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3896 · Cited by 2,124
Cell adhesion: integrating cytoskeletal dynamics and cellular tension
Parsons, J. T., Horwitz, A. R., & Schwartz, M. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2957 · Cited by 2,081
Hinz, B., Phan, S. H., Thannickal, V. J., Galli, A., Bochaton-Piallat, M.-L., & Gabbiani, G. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.070112 · Cited by 2,068
Self-citationROCKs: multifunctional kinases in cell behaviour
Riento, K., & Ridley, A. J. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1128 · Cited by 1,941
Cardiac Fibrosis: The Fibroblast Awakens
Travers, J. G., Kamal, F. A., Robbins, J., Yutzey, K. E., & Blaxall, B. C. (2016) · Circulation Research · doi:10.1161/circresaha.115.306565 · Cited by 1,596
Stretching Single Talin Rod Molecules Activates Vinculin Binding
Hernández, A. E. D. R., Pérez‐Jiménez, R., Liu, R., Roca‐Cusachs, P., Fernández, J. M., & Sheetz, M. P. (2009) · Science · doi:10.1126/science.1162912 · Cited by 1,492
Research works printed but not linked: 7
- Martinez, 2017, Idiopathic pulmonary fibrosis, Nature reviews, Dis. Prim., 3, 17074
- Ampe, 2017, vol. 235, 1
- Coelho, 2016, Contribution of collagen adhesion receptors to tissue fibrosis, Cell Tissue Res., 365, 521, 10.1007/s00441-016-2440-8 · DOI
- Coelho, 2018, Mechanical signaling through the discoidin domain receptor 1 plays a central role in tissue fibrosis, Cell Adhes. Migrat., 12, 348
- Leitinger, 2014, 310, 39
- Froese, 2016, Stretch induced activation of TGF-beta1 in pulmonary fibrosis, Am. J. Respir. Crit. Care Med., 194, 84, 10.1164/rccm.201508-1638OC · DOI · Paper page
- Piersma, 2015, YAP1 is a driver of myofibroblast differentiation in normal and diseased fibroblasts, Am. J. Pathol., 185, 3326, 10.1016/j.ajpath.2015.08.011 · DOI · Paper page
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Frangogiannis, N. G. (2019) · The Journal of Experimental Medicine · doi:10.1084/jem.20190103 · Cited by 1,377
Fibroblast and myofibroblast activation in normal tissue repair and fibrosis
Younesi, F. S., Miller, A. E., Barker, T. H., Rossi, F. M. V., & Hinz, B. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00716-0 · Cited by 755
“anti-fibrotic therapies to break this loop, which has evolved multiple redundancies to promote rapid healing of injured tissues at the expense of functionality 72 .”
InfluentialSelf-citationEvasion of apoptosis by myofibroblasts: a hallmark of fibrotic diseases
Hinz, B., & Lagares, D. (2019) · Nature Reviews Rheumatology · doi:10.1038/s41584-019-0324-5 · Cited by 642
Self-citationRole of fibroblasts in wound healing and tissue remodeling on Earth and in space
Cialdai, F., Risaliti, C., & Monici, M. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.958381 · Cited by 390
Pakshir, P., Noskovicova, N., Lodyga, M., Son, D. O., Schuster, R., Goodwin, A., Karvonen, H., & Hinz, B. (2020) · Journal of Cell Science · doi:10.1242/jcs.227900 · Cited by 293
“…recent strategies tackle different components of the TGF-β1 activation machinery, which provide cell- and context-specificity (Akhurst, 2017; de Gramont et al., 2017; Friedman et al., 2013; Ganesh and Massague, 2018; Hinz, 2016c; Huynh et al., 2019; Lodyga and Hinz, 2019; Varga and Pasche, 2009).”
BackgroundSelf-citationThe Role of Myofibroblasts in Physiological and Pathological Tissue Repair
Schuster, R., Younesi, F., Ezzo, M., & Hinz, B. (2023) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041231 · Cited by 232
Self-citationPlatelet-rich plasma accelerates skin wound healing by promoting re-epithelialization
Xu, P., Wu, Y., Zhou, L., Yang, Z., Zhang, X., Hu, X., Yang, J., Wang, M., Wang, B., Luo, G., et al. (2020) · Burns & Trauma · doi:10.1093/burnst/tkaa028 · Cited by 226
“In the middle and late stages, the differentiation of fibroblasts into myofibroblasts gradually increased with the formation of granulation tissue, which will drive the effective contraction of the wound margin [51, 52].”
BackgroundImplant Fibrosis and the Underappreciated Role of Myofibroblasts in the Foreign Body Reaction
Noskovicova, N., Hinz, B., & Pakshir, P. (2021) · Cells · doi:10.3390/cells10071794 · Cited by 184
Self-citationThe inflammatory speech of fibroblasts
Schuster, R., Rockel, J. S., Kapoor, M., & Hinz, B. (2021) · Immunological Reviews · doi:10.1111/imr.12971 · Cited by 181
Self-citationNoskovičová, N., Schuster, R., van Putten, S., Ezzo, M., Koehler, A., Boo, S., Coelho, N. M., Griggs, D. W., Ruminski, P., McCulloch, C. A., et al. (2021) · Nature Biomedical Engineering · doi:10.1038/s41551-021-00722-z · Cited by 180
Self-citationYu, Z., Xu, C., Song, B., Zhang, S., Chen, C., Li, C., & Zhang, S. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04554-0 · Cited by 191
“Some α-SMA-negative myofibroblasts can also contribute to tissue fibrosis by producing stress fibers made up of β-actin [26].”
BackgroundMultipotent stromal cells: One name, multiple identities
Soliman, H., Theret, M., Scott, W., Hill, L., Underhill, T. M., Hinz, B., & Rossi, F. M. V. (2021) · Cell Stem Cell · doi:10.1016/j.stem.2021.09.001 · Cited by 147
Self-citationKeloid disorder: Fibroblast differentiation and gene expression profile in fibrotic skin diseases
Macarak, E. J., Wermuth, P. J., Rosenbloom, J., & Uitto, J. (2020) · Experimental Dermatology · doi:10.1111/exd.14243 · Cited by 143
Condorelli, A. G., Dellambra, E., Logli, E., Zambruno, G., & Castiglia, D. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225707 · Cited by 134
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BackgroundPassive myocardial mechanical properties: meaning, measurement, models
Emig, R., Zgierski-Johnston, C. M., Timmermann, V., Taberner, A. J., Nash, M. P., Kohl, P. K., & Peyronnet, R. (2021) · Biophysical Reviews · doi:10.1007/s12551-021-00838-1 · Cited by 139
“…of Engineering, University of Freiburg, Freiburg, Germany Extracellular stiffness affects all cardiac cell types The stiffness of the extracellular environment influences a host of cellular processes, including direction of cell migration, cell division and differentiation (Hinz et al. 2019, Fig.”
BackgroundEmig, R., Knodt, W., Krussig, M. J., Zgierski-Johnston, C. M., Gorka, O., Groß, O., Kohl, P. K., Ravens, U., & Peyronnet, R. (2021) · Cells · doi:10.3390/cells10030663 · Cited by 107
“The mechanical properties of the extracellular matrix (ECM) in particular, act as a driver for a number of cell functions including differentiation, motility, myofibroblast phenoconversion, and collagen production [1].”
BackgroundChiarelli, N., Ritelli, M., Zoppi, N., & Colombi, M. (2019) · Genes · doi:10.3390/genes10080609 · Cited by 82
“During fibroblast-to-myofibroblast transition, a complex mechanochemical signaling is activated involving profibrotic secreted factors such as TGFβ and Wnt and ECM-degrading enzymes and intracellular effectors required for stress fiber contractility [127,131].”
BackgroundHealing the diabetic wound: Unlocking the secrets of genes and pathways
Kamal, R., Awasthi, A., Pundir, M., & Thakur, S. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176645 · Cited by 78
Cellular and Molecular Mechanisms of Wound Repair: From Biology to Therapeutic Innovation
Jin, C., Jin, Y., Ding, Z., Nuch, K. S., Han, M., Shim, J., Chien, P. N., & Heo, C. Y. (2025) · Cells · doi:10.3390/cells14231850 · Cited by 94
“…integrin-and DNA damage response (DDR)-mediated activation of FAK–YAP/TAZ pathways, they sense matrix stiffness, while interacting with type 2 immune signaling, such as interleukin-33 (IL-33), interleukin-4 (IL-4), and interleukin-13 (IL-13) to shape the inflammatory-to-repair transition [74–77].”
Diversity of Fibroblasts and Their Roles in Wound HealingPreprint
Jiang, D., Guo, R., Machens, H., & Rinkevich, Y. (2022) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041222 · Cited by 80
Collagen Fibril Density Modulates Macrophage Activation and Cellular Functions during Tissue Repair
Sapudom, J., Mohamed, W. K. E. A., Garcia‐Sabaté, A., Alatoom, A., Karaman, S., Mahtani, N., & Teo, J. C. M. (2020) · Bioengineering · doi:10.3390/bioengineering7020033 · Cited by 72
“It suggests that a dense fibrillar matrix might act as a negative feedback for myofibroblasts to prevent an excessive production of matrix proteins and remodeling in physiological conditions [74].”
BackgroundCondorelli, A. G., Hachem, M. E., Zambruno, G., Nyström, A., Candi, E., & Castiglia, D. (2021) · Journal of Biomedical Science · doi:10.1186/s12929-021-00732-8 · Cited by 71
“α-SMA, α-smooth muscle actin) and secretion of ECM matricellular proteins [70, 71].”
BackgroundEpithelial–Mesenchymal Transition Mechanisms in Chronic Airway Diseases: A Common Process to Target?
Mottais, A., Riberi, L., Falco, A., Soccal, S., Gohy, S. T., & Rose, V. D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512412 · Cited by 75
Myofibroblast Markers and Microscopy Detection Methods in Cell Culture and Histology
Younesi, F. S., Son, D. O., de Firmino, J. B., & Hinz, B. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1382-5_3 · Cited by 69
Self-citationZinc sulfide nanoparticles improve skin regeneration
Han, B., FANG, W. H., Zhao, S., Yang, Z., & Hoang, B. X. (2020) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2020.102263 · Cited by 62
Astrocyte responses to experimental glaucoma in mouse optic nerve head
Quillen, S. E., Schaub, J. A., Quigley, H. A., Pease, M. E., Korneva, A., & Kimball, E. (2020) · PLoS ONE · doi:10.1371/journal.pone.0238104 · Cited by 57
Arif, S., Attiogbe, E., & Moulin, V. J. (2021) · Wound Repair and Regeneration · doi:10.1111/wrr.12919 · Cited by 56
“A review of what is known about this functionality has been recently published by Hinz et al.(4)”
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Froom, Z. S. C. S., Callaghan, N. I., & Huyer, L. D. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110203 · Cited by 64
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Stewart, D. C., Brisson, B. K., Yen, W. K., Liu, Y., Wang, C., Ruthel, G. T., Gullberg, D., Mauck, R. L., Maden, M., Han, L., et al. (2024) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2024.08.013 · Cited by 58
Cardiac Fibroblast to Myofibroblast Phenotype Conversion—An Unexploited Therapeutic Target
Czubryt, M. P. (2019) · Journal of Cardiovascular Development and Disease · doi:10.3390/jcdd6030028 · Cited by 49
“However, it is cell contractility and the production of stress fibers that truly defines the “myo”fibroblast phenotype, as not all cells that secrete increased ECM levels are necessarily myofibroblasts, although increased ECM production appears to be a general hallmark of these cells for the most part [40].”
BackgroundChen, Z., Ezzo, M., Zondag, B., Rakhshani, F., Ma, Y., Hinz, B., & Kumacheva, E. (2023) · Advanced Materials · doi:10.1002/adma.202305964 · Cited by 49
Self-citationEremichev, R. Y., Kulebyakina, M., Alexandrushkina, N. A., Nimiritsky, P., Basalova, N. A., Grigorieva, O., Egiazaryan, M., Dyikanov, D. T., Va, T., & Макаревич, П. И. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.616893 · Cited by 41
“In SCs, mentioned molecular targets comprise a system necessary for mechanosensing, mediating resistance to mechanical forces and subsequent transformation into myofibroblasts (Hinz et al., 2019).”
BackgroundInfluentialVerteporfin inhibits the persistent fibrotic phenotype of lesional scleroderma dermal fibroblasts
Shiwen, X., Racanelli, M., Ali, A., Simon, A., Quesnel, K., Stratton, R. J., & Leask, A. (2021) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-020-00596-x · Cited by 41
Integrin Regulation of CAF Differentiation and Function
DiPersio, C. M., & Water, L. V. D. (2019) · Cancers · doi:10.3390/cancers11050715 · Cited by 39
“As discussed below, roles for specific integrin-ECM interactions in controlling myofibroblast differentiation and ECM rigidity are clear [42,43].”
BackgroundNADPH oxidase 4 is dispensable for skin myofibroblast differentiation and wound healing
Siedlar, A. M., Seredenina, T. S., Faivre, A., Cambet, Y., Stasia, M. J., André‐Lévigne, D., Bochaton‐Piallat, M., Pittet-Cuenod, B. M., de Seigneux, S., Krause, K., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102609 · Cited by 36
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Ezzo, M., & Hinz, B. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108528 · Cited by 39
Self-citationFibrosis in burns: an overview of mechanisms and therapies
Faour, S., Farahat, M., Aijaz, A., & Jeschke, M. G. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00254.2023 · Cited by 40
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Benn, M. C., Weber, W., Klotzsch, E., Viola Vogel, B., & Pot, S. A. (2019) · Current Opinion in Biomedical Engineering · doi:10.1016/j.cobme.2019.06.003 · Cited by 36
Yang, J., Liu, X., Wang, W., Chen, Y., Liu, J., Zhang, Z., Wu, C., Jiang, X., Liang, Y., & Zhang, J. (2022) · Bioelectrochemistry · doi:10.1016/j.bioelechem.2022.108247 · Cited by 35
A story of fibers and stress: Matrix‐embedded signals for fibroblast activation in the skin
Sawant, M., Hinz, B., Schönborn, K., Zeinert, I., Eckes, B., Krieg, T., & Schuster, R. (2021) · Wound Repair and Regeneration · doi:10.1111/wrr.12950 · Cited by 36
“lattices do not experience the strains required to activate into mature myofibroblast phenotypes.(118,122) A comprehensive comparison of human dermal fibroblasts grown in retracting versus strained collagen”
BackgroundInfluentialSelf-citationAhuja, S., & Zaheer, S. (2023) · Cell Biology International · doi:10.1002/cbin.12097 · Cited by 33
“In addition, these cells also express more structural collagen and synthesize cytokines, growth factors, and matrix proteins (Carthy, 2018; Hinz et al., 2019; Klingberg et al., 2013).”
BackgroundSui, J., Pragnère, S., & Kurniawan, N. A. (2025) · Biomaterials Science · doi:10.1039/d5bm00210a · Cited by 35
Chen, Y., Zhang, X., Liu, Z., Yang, J., Chen, C., Wang, J., Yang, Z., He, L., Xu, P., Hu, X., et al. (2021) · Burns & Trauma · doi:10.1093/burnst/tkab004 · Cited by 30
“To our knowledge, moderated collagen coordinates the interaction of growth factors, cytokines and chemokines, which affects cell behavior as a consequence of their binding to specific cell surface receptors or ECM proteins([34,35]).”
BackgroundLiu, Z., Cao, Y., Liu, G., Yin, S., Ma, J., Liu, J., Zhang, M., & Wang, Y. (2019) · Experimental Cell Research · doi:10.1016/j.yexcr.2019.111504 · Cited by 30
Fang, C., Zeng, Z., Ni, B., Wen, X., Fang, Z., Zou, J., & Zhang, G. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1681875 · Cited by 29
“This ECM stiffening further promotes TGF-β1 release and biomechanical activation of myofibroblasts, forming a vicious positive feedback loop that drives fibrosis progression (Hinz et al., 2019; Hinz, 2009).”
Squecco, R., Chellini, F., Idrizaj, E., Tani, A., Garella, R., Pancani, S., Pavan, P., Bambi, F., Zecchi‐Orlandini, S., & Sassoli, C. (2020) · Cells · doi:10.3390/cells9051199 · Cited by 29
“Obviously, the in vitro experimentation eliminates many paracrine/juxtacrine mechanisms, possibly regulating in situ intercellular interactions and cell functionality as well as the mechanical forces exerted by the surrounding microenvironment, including ECM stiffness, affecting cell behavior [16,18,109].”
BackgroundInfluentialAndo, R., Sakai, A., Iida, T., Kataoka, K., Mizutani, Y., & Enomoto, A. (2022) · Cancers · doi:10.3390/cancers14143315 · Cited by 31
“expression is downregulated by a soft substrate, but the detailed mechanisms by which Col1α1 expression is regulated in rCAFs are not well known [35,60].”
BackgroundThe Human Dermis as a Target of Nanoparticles for Treating Skin Conditions
Salazar, J., Carmona, T., Zacconi, F. C. M., Venegas-Yazigi, D. A., Cabello‐Verrugio, C., Choi, W. I., & Vilos, C. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics15010010 · Cited by 29
Pakshir, P., Younesi, F. S., Wootton, K.-A., Battiston, K. G., Whitton, G., Ilagan, B., Louka, D., Statham, M., Mackey, G., Daley, A. B., et al. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2022.121586 · Cited by 29
Self-citationChang, K., Zhang, X., Lin, S., Lin, S., Lin, Y., Akhrymuk, I. V., Lin, S., & Lin, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011152 · Cited by 27
Hamilton, D. W., Walker, J. T., Tinney, D., Grynyshyn, M., El‐Warrak, A. O., Truscott, E. A., & Flynn, L. E. (2021) · Wound Repair and Regeneration · doi:10.1111/wrr.12981 · Cited by 27
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Liu, H., Fan, P., Jin, F., Huang, G., Guo, X., & Xu, F. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.1042030 · Cited by 30
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BackgroundThe role of immunosuppressive myofibroblasts in the aging process and age-related diseases
Salminen, A. (2023) · Journal of Molecular Medicine · doi:10.1007/s00109-023-02360-1 · Cited by 26
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Myofibroblast Gene Expression Profile after Tooth Extraction in the Rabbit
Marconcini, S., Denaro, M., Cosola, S., Gabriele, M., Toti, P., Mijiritsky, E., Proietti, A., Basolo, F., Giammarinaro, E., & Covani, U. (2019) · Materials · doi:10.3390/ma12223697 · Cited by 24
“Myofibroblasts, like smooth muscle cells and fibroblasts, develop contractile force upon phosphorylation of myosin light chains, which allows the myosin head to interact with actin filaments [12].”
BackgroundDas, S. J., Wishart, T. F. L., Jandeleit-Dahm, K. A. M., & Lovicu, F. J. (2020) · Experimental Eye Research · doi:10.1016/j.exer.2020.107918 · Cited by 25
Kim, S., Lee, H., Kim, J. A., & Park, T. H. (2022) · Biomaterials Advances · doi:10.1016/j.bioadv.2022.212780 · Cited by 24
Li, Z., & Bratlie, K. M. (2021) · Materials Science and Engineering C · doi:10.1016/j.msec.2021.111915 · Cited by 25
Animal and Human Models of Tissue Repair and Fibrosis: An Introduction
Lagares, D., & Hinz, B. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1382-5_20 · Cited by 23
Self-citationKindlin-2 Mediates Mechanical Activation of Cardiac Myofibroblasts
Godbout, E., Son, D. O., Hume, S., Boo, S., Sarrazy, V., Clément, S., Kapùs, A., Wehrle‐Haller, B., Bruckner‐Tuderman, L., Has, C., et al. (2020) · Cells · doi:10.3390/cells9122702 · Cited by 23
“Two main factors control myofibroblast activation: transforming growth factor beta (TGF-β1) and mechanical stress [47,48].”
BackgroundSelf-citationWang, Y., Zhang, Y., Lu, B., Xi, J., Ocansey, D. K. W., Mao, F., Hao, D., & Yan, Y. (2023) · Stem Cells International · doi:10.1155/2023/2828981 · Cited by 23
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BackgroundLeask, A. (2021) · Wound Repair and Regeneration · doi:10.1111/wrr.12889 · Cited by 22
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Atiba, A. S., Abdo, W. S., Ali, E. K., Abd-Elsalam, M. M., Amer, M. E., Monsef, A. S. A., Taha, R. S., Antar, S. A., & Mahmoud, A. M. (2022) · Biomarkers · doi:10.1080/1354750x.2022.2085800 · Cited by 21
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BackgroundDing, N., Fu, X., Gui, Q., Wu, M., Niu, Z., Du, A., Liu, J., Wu, H., Wang, Y., Yue, X., et al. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202303192 · Cited by 21
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Son, D. O., & Hinz, B. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1382-5_27 · Cited by 20
Self-citationSchussler, O., Chachques, J. C., Alifano, M., & Lecarpentier, Y. (2021) · Journal of Cardiovascular Translational Research · doi:10.1007/s12265-021-10154-4 · Cited by 21
Sassoli, C., Nistri, S., Chellini, F., & Bani, D. (2021) · Current Molecular Medicine · doi:10.2174/1566524021666210309113650 · Cited by 20
Matera, D. L., Lee, A. T., Hiraki, H. L., & Baker, B. M. (2021) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-021-00698-5 · Cited by 23
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“It is widely known that myofibroblasts that secrete excessive collagen into the ECM are involved in the pathogenesis of hypertrophic scars (1, 9).”
BackgroundInfluentialZhao, J., Yang, S., Xu, Y., Qin, S., Bie, F., Chen, L., Zhou, F., Xie, J., Liu, X., Shu, B., et al. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.04.014 · Cited by 19
Li, C., Peng, Z., Zhou, Y., Su, Y., Bu, P., Meng, X., Li, B., & Xu, Y. (2021) · Bone and Joint Research · doi:10.1302/2046-3758.109.bjr-2020-0421.r2 · Cited by 18
Grigorieva, O., Basalova, N. A., Vigovskiy, M. A., Arbatskiy, M. S., Dyachkova, U., Kulebyakina, M., Kulebyakin, K. Y., Tyurin‐Kuzmin, P. A., Kalinina, N., & Efimenko, A. Y. (2023) · Biomedicines · doi:10.3390/biomedicines11030840 · Cited by 17
“When cultivating MSCs on dECM derived from dermal fibroblasts with the addition of TGFβ-1 for 96 h (F), the number of cells including αSMA in the stress fibers increased in culture, which represents a classic attribute of myofibroblast differentiation (Figure 2A).”
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“, non-physiological surface rigidity of culture dishes [30,31].”
BackgroundMechanosensing model of fibroblast cells adhered on a substrate with varying stiffness and thickness
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Chellini, F., Tani, A., Zecchi‐Orlandini, S., Giannelli, M., & Sassoli, C. (2020) · Applied Sciences · doi:10.3390/app10217878 · Cited by 17
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“The contraction of these fibers generates tension within the ECM, drawing the wound margins inward and promoting faster closure [41].”
Mendoza, F. A., & Jiménez, S. A. (2021) · Rheumatology · doi:10.1093/rheumatology/keab762 · Cited by 14
Zhang, L., Yan, H., Tai, Y., Xue, Y., Wei, Y., Wang, K., Zhao, Q., Wang, S., Kong, D., & Midgley, A. C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041575 · Cited by 14
“However, the synthesis and deposition of fibrillar collagen I in progressive fibrosis appears to take over the role of the predominant source of ECM mechanical stress and becomes the principal driver of the myofibroblast phenotype [62].”
BackgroundSapao, P., Roberson, E. D. O., Shi, B., Assassi, S., Skaug, B. A., Lee, F., Naba, A., White, B. E. P., Córdova-Fletes, C., Tsou, P., et al. (2022) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2022.08.052 · Cited by 14
Angelini, A., Trial, J., Saltzman, A. B., Malovannaya, A., & Cieslik, K. A. (2023) · iScience · doi:10.1016/j.isci.2023.107283 · Cited by 13
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“When fibroblasts are activated, the cytoskeleton is remodeled, which contributes to a number of cell functions (Hinz et al. 2001; Hinz et al. 2019).”
BackgroundGonzález‐Pérez, M., Camasão, D. B., Mantovani, D., Alonso, M., & Rodríguez‐Cabello, J. C. (2021) · Biomaterials Science · doi:10.1039/d0bm02197k · Cited by 13
Nucleocytoplasmic Shuttling of the Mechanosensitive Transcription Factors MRTF and YAP/TAZ
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Sbrana, F., Chellini, F., Tani, A., Parigi, M., Garella, R., Palmieri, F., Zecchi‐Orlandini, S., Squecco, R., & Sassoli, C. (2024) · Microscopy Research and Technique · doi:10.1002/jemt.24648 · Cited by 11
“In particular, the filamentous structures are referable to (Hinz et al., 2019; Pakshir et al., 2020).”
Schoberleitner, I., Lackner, M., Coraça-Huber, D. C., Augustin, A., Imsirovic, A., Sigl, S., & Wolfram, D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252111675 · Cited by 11
“The contractile activity of myofibroblasts, driven by sustained TGF-β signaling [40,79], contributes significantly to capsule contraction and rigidity [23,29,86].”
BackgroundEngineered microenvironment for the study of myofibroblast mechanobiology
Xu, Y. D., Koya, R. C., Ask, K., & Zhao, R. (2021) · Wound Repair and Regeneration · doi:10.1111/wrr.12955 · Cited by 12
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“Upon tissue injury, CFs exposed to high strain or ECM stiffness undergo differentiation int myofibroblasts, in which α-SMA is the most used myofibroblast biomarker and represents th activation degree of CFs [34].”
BackgroundWei, S., Chen, P., Tsai, M., Hsu, T., Hsieh, C., Fan, H., Chen, T., Xie, R., Chen, G., & Chen, Y. (2024) · Advanced Healthcare Materials · doi:10.1002/adhm.202303320 · Cited by 10
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Yisireyili, M., Wubulikasimu, W., Aili, A., Li, Y., Aziguli, A., Aipire, A., Maimaitiaili, A., Zhang, W., Cao, Z., Abulajiang, M., et al. (2019) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2019.7669 · Cited by 10
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“Fibroblasts and myofibroblasts are responsive to mechanical stimuli, particularly through a feedback control system via the extracellular matrix (Hinz et al., 2019).”
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Condorelli, A. G., Nobili, R., Muglia, A., Scarpelli, G., Marzuolo, E., Stefanis, C. D., Rota, R., Diociaiuti, A., Alaggio, R., Castiglia, D., et al. (2024) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2023.10.045 · Cited by 8
Metadata
- Authors
- Hinz, B., McCulloch, C. A., & Coelho, N. M.
- Affiliations
- University of Toronto (CA)
- Corresponding author
- Coelho, Nuno M.
- Venue
- Experimental Cell Research
- Publisher
- Elsevier BV
- Published
- 2019-06
- Volume
- 379
- Issue
- 1
- Pages
- 119-128
- ISSN
- 0014-4827 (ISSN-L)
- OpenAlex
- W2934133090
- Semantic Scholar
- 6f2d57f6aad8ed5a88713504974535d1eb19f620
- Cited by
- 182
- References
- 211
- Citations by year
- 2026: 23 · 2025: 19 · 2024: 28 · 2023: 27 · 2022: 20 · 2021: 38 · 2020: 14 · 2019: 13
- FWCI
- 2.47
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Experimental Cell Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research CIHR (#375597)
- Canada Foundation for Innovation and Ontario Research Fund (#36050)
- E-Rare Joint Transnational Program ‘Development of Innovative Therapeutic Approaches for Rare Diseases’ (# ERL-138395)
- CMC is supported by a CIHR Operating grant (MOP416228)
- Canada Research Chair in Matrix Dynamics
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Health Sciences › Medicine › Surgery › Wound Healing and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Keywords
- collagen contraction, fibroblast activation, extracellular matrix stiffness, mechanotransduction, actomyosin contractility, fibrosis, tissue remodeling, wound healing
- MeSH terms
- Animals, Collagen, Extracellular Matrix, Fibrosis, Humans, Phenotype, Wound Healing, Myofibroblasts
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