Integrin–TGF‐β crosstalk in fibrosis, cancer and wound healing
Open accessAbstract
Accumulating evidence indicates that there is extensive crosstalk between integrins and TGF-beta signalling. TGF-beta affects integrin-mediated cell adhesion and migration by regulating the expression of integrins, their ligands and integrin-associated proteins. Conversely, several integrins directly control TGF-beta activation. In addition, a number of integrins can interfere with both Smad-dependent and Smad-independent TGF-beta signalling in different ways, including the regulation of the expression of TGF-beta signalling pathway components, the physical association of integrins with TGF-beta receptors and the modulation of downstream effectors. Reciprocal TGF-beta-integrin signalling is implicated in normal physiology, as well as in a variety of pathological processes including systemic sclerosis, idiopathic pulmonary fibrosis, chronic obstructive pulmonary disease and cancer; thus, integrins could provide attractive therapeutic targets to interfere with TGF-beta signalling in these processes.
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By disrupting mechanical force transmission between cells and the ECM, integrin inhibitors attenuate TGF-b activation and modulate immune cell adhesion and migration, dampening pro-fibrotic inflammation at its source.
“By disrupting mechanical force transmission between cells and the ECM, integrin inhibitors not only attenuate TGF-b activation but also modulate immune cell adhesion and migration, effectively dampening pro-fibrotic inflammation at its source (129).”
From The mechanotransduction-immune axis in organ fibrosis: dual regulatory mechanisms and translational therapeutic perspectives (2025) · cites this paper as [129]
Integrins activate TGF-β.
“integrins are known to activate TGF-β”
From Integrin Beta 3 Regulates Cellular Senescence by Activating the TGF-β Pathway (2017) · cites this paper as Margadant and Sonnenberg, 2010
Cross-talk between integrins and TGF-β exists, particularly to regulate fibrosis, wound healing, and cancer.
“Accumulating evidence indicates that a cross-talk between integrins and TGF-β exists, in particular to regulate fibrosis, wound healing, and cancer (Asano et al., 2005, Margadant and Sonnenberg, 2010).”
From Integrin Beta 3 Regulates Cellular Senescence by Activating the TGF-β Pathway (2017) · cites this paper as Margadant and Sonnenberg, 2010
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“Furthermore, integrins and TGF-β receptors sustain each other’s expression and jointly modulate gene expression, providing additional mechanisms for positive reinforcement (Margadant and Sonnenberg, 2010).”
BackgroundDynamic interplay between the collagen scaffold and tumor evolution
Egeblad, M., Rasch, M. G., & Weaver, V. M. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.08.015 · Cited by 898 · see citing works
“Organ fibrosis and cancer are associated, although the association may simply reflect collagen accumulation due to increased activity of inflammatory and tumorigenic factors such as TGF-b [9].”
BackgroundThe Impact of TGF-β on Lung Fibrosis: From Targeting to Biomarkers
Fernandez, I. E., & Eickelberg, O. (2012) · Proceedings of the American Thoracic Society · doi:10.1513/pats.201203-023aw · Cited by 682 · see citing works
Kapp, T. G., Rechenmacher, F., Neubauer, S., Maltsev, O. V., Cavalcanti‐Adam, E. A., Zarka, R., Reuning, U., Notni, J., Wester, H., Mas‐Moruno, C., et al. (2017) · Scientific Reports · doi:10.1038/srep39805 · Cited by 623 · see citing works
Targeting TGF-β Mediated SMAD Signaling for the Prevention of Fibrosis
Walton, K. L., Johnson, K. E., & Harrison, C. A. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00461 · Cited by 545 · see citing works
“…(PAI-1; Dennler et al., 1998; Hua et al., 1998), various proteoglycans (Schonherr et al., 1991; Romaris et al., 1995; Dadlani et al., 2008), integrins (Margadant and Sonnenberg, 2010), connective tissue growth factor (Chen et al., 2002), and matrix metalloproteases (MMPs; Yuan and Varga, 2001).”
BackgroundEmerging therapeutic opportunities for integrin inhibitors
Slack, R. J., Macdonald, S. J. F., Roper, J. A., Jenkins, G. R., & Hatley, R. J. D. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00284-4 · Cited by 550 · see citing works
Mu, Y., Gudey, S. K., & Landström, M. (2011) · Cell and Tissue Research · doi:10.1007/s00441-011-1201-y · Cited by 545 · see citing works
“Cross-talk with integrin signaling pathways Several recent observations indicate that crosstalk exists between integrins and TGFβ, particularly in scenarios such as fibrosis, cancer, and wound healing (Margadant and Sonnenberg 2010).”
BackgroundApoptotic cell: linkage of inflammation and wound healing
Wu, Y.-S., & Chen, S.-N. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00001 · Cited by 500 · see citing works
“Accumulating evidence indicates that TGF-β affects integrin-mediated cell adhesion and migration by regulating the expression of integrins, their ligands and integrin-associated proteins (Margadant and Sonnenberg, 2010).”
BackgroundCutaneous wound healing: recruiting developmental pathways for regeneration
Bielefeld, K. A., Amini‐Nik, S., & Alman, B. A. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1152-9 · Cited by 484 · see citing works
“TGF-bs exert cell-specific effects by binding to serine/ threonine kinase TGF-b receptor I and TGF-b-receptor II heterodimers, leading to the activation (phosphorylation) of Smads 2 and 3, their association with the common mediator Smad 4, and the subsequent translocation of this complex to the nucleus where they may…”
BackgroundInfluentialHinz, B. (2016) · Experimental Eye Research · doi:10.1016/j.exer.2015.07.009 · Cited by 424 · see citing works
Cheng, F., Shen, Y., Mohanasundaram, P., Lindström, M., Ivaska, J., Ny, T., & Eriksson, J. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519197113 · Cited by 432 · see citing works
Forcing Stem Cells to Behave: A Biophysical Perspective of the Cellular Microenvironment
Sun, Y., Chen, C. S., & Fu, J. (2012) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-042910-155306 · Cited by 425 · see citing works
“Margadant C, Sonnenberg A. 2010.”
Extracellular matrix, integrins, and growth factors as tailors of the stem cell niche
Brizzi, M. F., Tarone, G., & Defilippi, P. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.07.001 · Cited by 412 · see citing works
“Integrins belonging to the beta1, alphav, beta7 and beta4 subfamilies have been shown to potentiate signalling pathways in response to many growth factors (reviewed in [2–5]), IL-3 [6,7] and TGFbeta (reviewed in [5,8]).”
BackgroundUnderstanding fibrosis in systemic sclerosis: shifting paradigms, emerging opportunities
Bhattacharyya, S., Wei, J., & Varga, J. (2012) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2011.149 · Cited by 381 · see citing works
“Integrin signaling and TGF-β crosstalk By binding to the extracellular matrix outside the cell and to the cytoskeleton intracellularly, the integrin family of transmembrane receptors integrate the extracellular environment with cellular behavior, and are essential for adhesive signaling”
Integrins as therapeutic targets
Goodman, S. L., & Picard, M. A. (2012) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2012.04.002 · Cited by 376 · see citing works
Navab, R., Strumpf, D., Bandarchi, B., Zhu, C., Pintilie, M., Ramnarine, V. R., Ibrahimov, E., Radulovich, N., Leung, L., Barczyk, M. M., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014506108 · Cited by 364 · see citing works
“ITGA11, together with other differentially expressed genes, including CTHRC1, SULF1, MFAP5, CLU, and THBS2, are known to be regulated by the TGF-β1 signaling pathway (18, 19), central to CAF differentiation and epithelial mesenchymal transition (28).”
BackgroundTransforming growth factor-β in myocardial disease
Frangogiannis, N. G. (2022) · Nature Reviews Cardiology · doi:10.1038/s41569-021-00646-w · Cited by 348 · see citing works
The role of TGF-β in the pathogenesis of primary open-angle glaucoma
Fuchshofer, R., & Tamm, E. R. (2011) · Cell and Tissue Research · doi:10.1007/s00441-011-1274-7 · Cited by 289 · see citing works
“TGF-β might also be activated in vitro by binding to specific integrins via LAP, a mechanism that is only relevant for TGF-β1 and –β3 as their LAPs contain an RGD motif (Nishimura 2009; Margadant and Sonnenberg 2010) but not for TGF-β2.”
BackgroundTargeting TGF-β signaling for the treatment of fibrosis
Györfi, A., Matei, A., & Distler, J. H. W. (2018) · Matrix Biology · doi:10.1016/j.matbio.2017.12.016 · Cited by 277 · see citing works
The pathogenesis of idiopathic pulmonary fibrosis
Coward, W. R., Saini, G., & Jenkins, G. R. (2010) · Therapeutic Advances in Respiratory Disease · doi:10.1177/1753465810379801 · Cited by 271 · see citing works
“…molecules involved in repair and development including integrins and components of the WNT signalling pathway [Konigshoff and Eickelberg, 2010; Margadant and Sonnenberg, 2010] and recently, it has been shown that specific ATII cell injury is sufficient to promote pulmonary fibrosis in a model…”
BackgroundVimentin Diversity in Health and Disease
Danielsson, F., Peterson, M. P., Caldeira, H., Lautenschläger, F., & Gad, A. K. B. (2018) · Cells · doi:10.3390/cells7100147 · Cited by 262 · see citing works
Potential Applications of Nanomaterials and Technology for Diabetic Wound Healing
Bai, Q., Han, K., Dong, K., Zheng, C., Zhang, Y., Long, Q., & Lu, T. (2020) · International Journal of Nanomedicine · doi:10.2147/ijn.s276001 · Cited by 266 · see citing works
The wound healing, chronic fibrosis, and cancer progression triad
Rybinski, B., Franco‐Barraza, J., & Cukierman, E. (2014) · Physiological Genomics · doi:10.1152/physiolgenomics.00158.2013 · Cited by 255 · see citing works
Targeting TGF-β Signaling for Therapeutic GainPreprint
Akhurst, R. J. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022301 · Cited by 243 · see citing works
“The fibrotic response to TGF-b is highly relevant to cancer progression, because a desmoplastic response is seen in many cancer types, especially pancreatic cancers and mesothelioma (Kano et al. 2007; Margadant and Sonnenberg 2010; Fujii et al. 2012a,b).”
BackgroundIntegrins as Therapeutic Targets: Successes and Cancers
Raab-Westphal, S., Marshall, J. F., & Goodman, S. L. (2017) · Cancers · doi:10.3390/cancers9090110 · Cited by 242 · see citing works
Tumor Targeting via Integrin Ligands
Marelli, U. K., Rechenmacher, F., Sobahi, T. R., Mas‐Moruno, C., & Kessler, H. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00222 · Cited by 239 · see citing works
Kiefel, H., Bondong, S., Hazin, J., Ridinger, J., Schirmer, U. B., Riedle, S., & Altevogt, P. (2012) · Cell Adhesion & Migration · doi:10.4161/cam.20832 · Cited by 228 · see citing works
Myofibroblast differentiation and survival in fibrotic disease
Kis, K., Liu, X., & Hagood, J. S. (2011) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399411001967 · Cited by 225 · see citing works
The evolving relationship of wound healing and tumor stroma.
Foster, D. S., Jones, R. E., Ransom, R. C., Longaker, M., & Norton, J. A. (2018) · JCI Insight · doi:10.1172/jci.insight.99911 · Cited by 202 · see citing works
Mechanical regulation of gene expression in cardiac myocytes and fibroblasts
Saucerman, J. J., Tan, P. M., Buchholz, K. S., McCulloch, A. D., & Omens, J. H. (2019) · Nature Reviews Cardiology · doi:10.1038/s41569-019-0155-8 · Cited by 223 · see citing works
Dynamics of cellular states of fibro-adipogenic progenitors during myogenesis and muscular dystrophy
Malecová, B., Gatto, S., Etxaniz, U., Passafaro, M., Cortez, A., Nicoletti, C., Giordani, L., Torcinaro, A., Bardi, M. D., Bicciato, S., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06068-6 · Cited by 221 · see citing works
TGFβ: a sleeping giant awoken by integrins
Worthington, J. J., Klementowicz, J. E., & Travis, M. A. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.08.002 · Cited by 217 · see citing works
The role and regulation of integrins in cell migration and invasion
Chastney, M. R., Kaivola, J., Leppänen, V., & Ivaska, J. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00777-1 · Cited by 224 · see citing works
“Together, these changes facilitate tumour cell plasticity, thereby promoting the ability to adapt to different microenvironments, priming the cells to migrate into surrounding tissues 12,135,137 .”
Adapala, R. K., Thoppil, R. J., Luther, D. J., Paruchuri, S. M., Meszaros, J. G., Chilian, W. M., & Thodeti, C. K. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.10.016 · Cited by 215 · see citing works
“TGF-β1 treatment has been demonstrated to induce the expression and activity of integrins during the differentiation of fibroblasts to myofibroblasts [26–28].”
Suppression of the Epithelial–Mesenchymal Transition by Grainyhead-like-2
Cieply, B. W., Riley, P., Pifer, P. M., Widmeyer, J., Addison, J., Ivanov, A. V., Denvir, J., & Frisch, S. M. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-4038 · Cited by 210 · see citing works
Ahn, S., Chantre, C. O., Gannon, A. R., Lind, J. U., Campbell, P. H., Grevesse, T., O’Connor, B. B., & Parker, K. K. (2018) · Advanced Healthcare Materials · doi:10.1002/adhm.201701175 · Cited by 209 · see citing works
Shao, X., Li, C., Yang, H., Lu, X., Liao, J., Qian, J., Wang, K., Cheng, J., Yang, P., Chen, H., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32111-8 · Cited by 201 · see citing works
Biochemical role of the collagen-rich tumour microenvironment in pancreatic cancer progression
Shields, M. A., Dangi-Garimella, S. Y., Redig, A. J., & Munshi, H. G. (2011) · Biochemical Journal · doi:10.1042/bj20111240 · Cited by 203 · see citing works
Integrin Beta 3 Regulates Cellular Senescence by Activating the TGF-β Pathway
Rapisarda, V., Borghesan, M., Miguela, V., Encheva, V., Snijders, A. P., Lujambio, A., & O’Loghlen, A. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.012 · Cited by 190 · see citing works
“Accumulating evidence indicates that a cross-talk between integrins and TGF-b exists, in particular to regulate fibrosis, wound healing, and cancer (Asano et al., 2005; Margadant and Sonnenberg, 2010).”
Mechanotransduction and fibrosis
Duscher, D., Maan, Z. N., Wong, V., Rennert, R. C., Januszyk, M., Rodrigues, M., Hu, M. S.-M., Whitmore, A. J., Whittam, A. J., Longaker, M. T., et al. (2014) · Journal of Biomechanics · doi:10.1016/j.jbiomech.2014.03.031 · Cited by 202 · see citing works
“the extracellular latent complex (Margadant and Sonnenberg 2010; Buscemi et al., 2011; Shi et al., 2011).”
BackgroundSun, K.-H., Chang, Y., Reed, N. I., & Sheppard, D. (2016) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00350.2015 · Cited by 200 · see citing works
Glinka, Y., Stoilova, S., Mohammed, N., & Prud'homme, G. (2011) · Carcinogenesis · doi:10.1093/carcin/bgq281 · Cited by 186 · see citing works
Human diseases through the lens of network biology
Furlong, L. I. (2012) · Trends in Genetics · doi:10.1016/j.tig.2012.11.004 · Cited by 194 · see citing works
Pivotal Role of TGF-β/Smad Signaling in Cardiac Fibrosis: Non-coding RNAs as Effectual Players
Saadat, S., Noureddini, M., Mahjoubin‐Tehran, M., Nazemi, S., Shojaie, L., Aschner, M., Maleki, B., Abbasi‐Kolli, M., Moghaddam, H. R., Alani, B., et al. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2020.588347 · Cited by 198 · see citing works
“Smad2/3 activation affects various profibrotic gene expression, consisting of collagens [COL1A1, COL3A1, COL5A2, COL6A1, COL6A3, COL7A1, (32)], PAI-1 (33, 34), various proteoglycans (35–37), integrins (38), connective tissue growth factor (CTGF) (39), and MMPs (27, 40).”
BackgroundSchnittert, J., Bansal, R., Storm, G., & Prakash, J. (2018) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2018.01.020 · Cited by 186 · see citing works
Bauer‐Mehren, A., Bundschus, M., Rautschka, M., Mayer, M. Á., Sanz, F., & Furlong, L. I. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020284 · Cited by 188 · see citing works
“related to several human pathologies including systemic sclerosis, idiopathic pulmonary fibrosis, chronic obstructive pulmonary disease and cancer [38].”
BackgroundFOXO1 promotes wound healing through the up-regulation of TGF-β1 and prevention of oxidative stress
Ponugoti, B., Xu, F., Zhang, C., Tian, C., Pacios, S., & Graves, D. T. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201305074 · Cited by 185 · see citing works
“TGF- 1 promotes keratinocyte migration by stimulating the expression of various integrins including integrin 6 (Gailit et al., 1994; Zambruno et al., 1995; Margadant and Sonnenberg, 2010).”
Sandbo, N. K., & Dulin, N. O. (2011) · Translational research · doi:10.1016/j.trsl.2011.05.004 · Cited by 178 · see citing works
Herum, K. M., Lunde, I. G., McCulloch, A. D., & Christensen, G. (2017) · Journal of Clinical Medicine · doi:10.3390/jcm6050053 · Cited by 183 · see citing works
“Comprehensive reviews of integrin cross-talk in the context of fibrosis have been published previously [119,121,122].”
BackgroundLiposome-Based Drug Delivery Systems in Cancer Immunotherapy
Gu, Z., Silva, C. G. D., van der Maaden, K., OSSENDORP, F. A., & Cruz, L. J. (2020) · Pharmaceutics · doi:10.3390/pharmaceutics12111054 · Cited by 177 · see citing works
Fibrosis: recent advances in myofibroblast biology and new therapeutic perspectives
Hinz, B., & Gabbiani, G. (2010) · F1000 Biology Reports · doi:10.3410/b2-78 · Cited by 172 · see citing works
“In addition, integrins avb3, avb8, and avb5 play a role in latent TGF-b1 activation by fibroblastic cells, either directly or in a process involving proteases [11,36-40].”
BackgroundHe, J., Fang, B., Shan, S., Xie, Y., Wang, C., Zhang, Y., Zhang, X., & Li, Q. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03481-6 · Cited by 172 · see citing works
An, S. Y., Jang, Y. J., Lim, H.-J., Han, J., Lee, J., Lee, G., Park, J. Y., Park, S.-Y., Kim, J. H., Do, B.-R., et al. (2017) · Gastroenterology · doi:10.1053/j.gastro.2016.12.003 · Cited by 193 · see citing works
Altorok, N., Tsou, P., Coit, P., Khanna, D., & Sawalha, A. H. (2014) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2014-205303 · Cited by 162 · see citing works
Rosacea: the Cytokine and Chemokine Network
Gerber, P. A., Buhren, B. A., Steinhoff, M. S., & Homey, B. (2011) · Journal of Investigative Dermatology Symposium Proceedings · doi:10.1038/jidsymp.2011.9 · Cited by 163 · see citing works
“Next to its role in development and morphogenesis, TGF-β signaling has been associated with fibrosis in systemic sclerosis, idiopathic pulmonary fibrosis, keloids, and notably phymatous tissues (Pu et al., 2000; Payne et al., 2002, 2006; Margadant and Sonnenberg, 2010).”
BackgroundLo, P.-K., Kanojia, D., Liu, X., Singh, U. P., Berger, F. G., Wang, Q., & Chen, H. (2011) · Oncogene · doi:10.1038/onc.2011.439 · Cited by 160 · see citing works
“It has been shown that integrins are involved in activation of TGFb signaling (Margadant and Sonnenberg, 2010).”
Integrin signaling in cancer: bidirectional mechanisms and therapeutic opportunities
Li, S., Sampson, C., Liu, C., Piao, H., & Liu, H. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01264-4 · Cited by 162 · see citing works
Unique and redundant functions of integrins in the epidermis
Margadant, C., Charafeddine, R. A., & Sonnenberg, A. (2010) · The FASEB Journal · doi:10.1096/fj.09-151449 · Cited by 157 · see citing works
“Besides directly activating TGF-β, integrins can also regulate TGF-β signaling in a variety of cell types (146).”
BackgroundSelf-citationChen, C., Chen, J., Wang, Y., Fang, L., Guo, C., Sang, T., Peng, H., Zhao, Q., Chen, S., Lin, X., et al. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154626 · Cited by 161 · see citing works
Targeting Integrins for Cancer Therapy - Disappointments and Opportunities
Bergonzini, C., Kroese, K., Zweemer, A. J. M., & Danen, E. H. J. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.863850 · Cited by 149 · see citing works
Amini‐Nik, S., Yousuf, Y., & Jeschke, M. G. (2017) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2017.07.017 · Cited by 147 · see citing works
Serrano, I., McDonald, P. C., Lock, F. E., & Dedhar, S. (2012) · Oncogene · doi:10.1038/onc.2012.30 · Cited by 144 · see citing works
Mechano-therapeutics: Targeting Mechanical Signaling in Fibrosis and Tumor Stroma
Tschumperlin, D. J., & Lagares, D. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107575 · Cited by 142 · see citing works
“In CAFs, αvβ6, αvβ3 and αvβ5 integrins have been shown to promote TGF-β1 activation, fibrosis and tumor progression(Jang & Beningo, 2019), indicating that targeting αv-integrins may interrupt the feedforward loop of matrix stiffening and TGFβ1 activation described several times in this review.”
BackgroundInfluentialCorneal myofibroblasts and fibrosis
Wilson, S. E. (2020) · Experimental Eye Research · doi:10.1016/j.exer.2020.108272 · Cited by 143 · see citing works
“Also likely important is the necessary activation of TGFβ that is produced as a precursor and must be activated by proteolysis and by interaction with integrins (Margadant and Sonnenberg, 2010; Dong et al., 2017).”
BackgroundRapid disorganization of mechanically interacting systems of mammary acini
Shi, Q., Ghosh, R. P., Engelke, H., Rycroft, C. H., Cassereau, L., Sethian, J. A., Weaver, V. M., & Liphardt, J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311312110 · Cited by 138 · see citing works
Kuninty, P. R., Bansal, R., de Geus, S. W. L., Mardhian, D. F., Schnittert, J., van Baarlen, J., Storm, G., Bijlsma, M. F., van Laarhoven, H. W. M., Metselaar, J. M., et al. (2019) · Science Advances · doi:10.1126/sciadv.aax2770 · Cited by 133 · see citing works
An αv‐RGD Integrin Inhibitor Toolbox: Drug Discovery Insight, Challenges and Opportunities
Hatley, R. J. D., Macdonald, S. J. F., Slack, R. J., Le, J., Ludbrook, S. B., & Lukey, P. T. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201707948 · Cited by 132 · see citing works
Mechanobiology of annulus fibrosus and nucleus pulposus cells in intervertebral discs
Molladavoodi, S., McMorran, J. G., & Gregory, D. E. (2019) · Cell and Tissue Research · doi:10.1007/s00441-019-03136-1 · Cited by 130 · see citing works
Matrix‐dependent perturbation of TGFβ signaling and disease
Doyle, J. J., Gerber, E. E., & Dietz, H. C. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.05.027 · Cited by 127 · see citing works
Stromal POSTN induced by TGF-β1 facilitates the migration and invasion of ovarian cancer
Yue, H., Li, W., Chen, R., Wang, J., Lu, X., & Li, J. (2020) · Gynecologic Oncology · doi:10.1016/j.ygyno.2020.11.026 · Cited by 126 · see citing works
Shields, M. A., Dangi-Garimella, S. Y., Krantz, S. B., Bentrem, D. J., & Munshi, H. G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.195628 · Cited by 124 · see citing works
Developmental pathways associated with cancer metastasis: Notch, Wnt, and Hedgehog
Kamdje, A. H. N., Kamga, P. T., Simo, R. T., Vecchio, L., Etet, P. F. S., Jm, M., Bassi, G., Lukong, K. E., Goel, R. K., Mbo, A. J., et al. (2017) · Cancer Biology and Medicine · doi:10.20892/j.issn.2095-3941.2016.0032 · Cited by 124 · see citing works
Reviewing the Regulators of COL1A1
Devos, H., Zoidakis, J., Roubelakis, M. G., Latosinska, A., & Vlahou, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241210004 · Cited by 119 · see citing works
“Our literature search highlighted transcription factors with existing evidence for direct binding to the upstream regions of COL1A1, namely Nuclear factor kappa-light-chainenhancer of activated B cells (NF-κB) [44] and Sma and Mad related protein 2/3 complex (Smad2/3 complex) in the context of the TGFβ signalling path…”
BackgroundSoft tissue mechanotransduction in wound healing and fibrosis
Wong, V., Longaker, M. T., & Gurtner, G. C. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.09.010 · Cited by 123 · see citing works
CDK5 is essential for TGF-β1-induced epithelial-mesenchymal transition and breast cancer progression
Liang, Q. Y., Li, L., Zhang, J., Yang, L., Wang, L., Liu, D., Feng, J., Hou, P., Yao, R., Zhang, Y., et al. (2013) · Scientific Reports · doi:10.1038/srep02932 · Cited by 123 · see citing works
Zhou, Y., Hagood, J. S., Lu, B., Merryman, W. D., & Murphy-Ullrich, J. E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.126227 · Cited by 118 · see citing works
Kopf, J., Petersen, A., Duda, G. N., & Knaus, P. I. (2012) · BMC Biology · doi:10.1186/1741-7007-10-37 · Cited by 119 · see citing works
“Especially integrins crosstalk to TGFb and BMP signalling pathways [33].”
BackgroundArnold, K. M., Opdenaker, L. M., Flynn, D. C., & Sims‐Mourtada, J. (2015) · Cancer Growth and Metastasis · doi:10.4137/cgm.s11286 · Cited by 118 · see citing works
Irifuku, T., Doi, S., Sasaki, K., Doi, T., Nakashima, A., Ueno, T., Yamada, K., Arihiro, K., Kohno, N., & Masaki, T. (2015) · Kidney International · doi:10.1038/ki.2015.291 · Cited by 118 · see citing works
Kimura, R. H., Wang, L., Shen, B., Huo, L., Tummers, W. S. F. J., Filipp, F. V., Guo, H. H., Haywood, T., Abou‐Elkacem, L., Baratto, L., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11863-w · Cited by 120 · see citing works
Integrin-Mediated TGFβ Activation Modulates the Tumour Microenvironment
Brown, N. F., & Marshall, J. F. (2019) · Cancers · doi:10.3390/cancers11091221 · Cited by 116 · see citing works
Richardson, R. J., Metzger, M., Knyphausen, P., Ramezani, T., Slanchev, K., Kraus, C., Schmelzer, E., & Hammerschmidt, M. (2016) · Development · doi:10.1242/dev.130492 · Cited by 113 · see citing works
“…of focal adhesion proteins such as 5 1, 2 1, 3 1, v 5 and / or v 6 integrins that mediate cell movement via the dynamic binding of extracellular matrix (ECM) components such as fibronectin and collagen to cell surfaces (Margadant and Sonnenberg, 2010; Tsuruta et al., 2011).”
BackgroundThe role of integrins in TGFβ activation in the tumour stroma
Khan, Z. A., & Marshall, J. F. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2474-y · Cited by 115 · see citing works
“…activates via phosphorylation the SMAD2 and SMAD3 transcription factors, which now can bind SMAD4 promoting their translocation to the nucleus in which the complex drives the transcription of a wide variety of genes, including the αv integrins (Levy and Hill 2005; Margadant and Sonnenberg 2010).”
BackgroundInfluentialModulation of the Tumor Microenvironment for Cancer Treatment: A Biomaterials Approach
Adjei, I. M., & Sharma, B. (2015) · Journal of Functional Biomaterials · doi:10.3390/jfb6010081 · Cited by 112 · see citing works
“Within tumors, the cytotoxic activity of M1 macrophages is inhibited by IL-4, IL-6, TGF-b1 and myocardiac depression factor secreted by cancer cells.”
BackgroundInfluentialRole of caveolin-1 in fibrotic diseases
Gvaramia, D., Blaauboer, M. E., Hanemaaijer, R., & Everts, V. E. (2013) · Matrix Biology · doi:10.1016/j.matbio.2013.03.005 · Cited by 109 · see citing works
van der Horst, G., van den Hoogen, C., Buijs, J. T., Cheung, H., Bloys, H., Pelger, R. C. M., Lorenzon, G., Heckmann, B., Feyen, J. H. M., Pujuguet, P., et al. (2011) · Neoplasia · doi:10.1593/neo.11122 · Cited by 110 · see citing works
α11 integrin stimulates myofibroblast differentiation in diabetic cardiomyopathy
Talior‐Volodarsky, I., Connelly, K. A., Arora, P. D., Gullberg, D., & McCulloch, C. A. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs259 · Cited by 110 · see citing works
Enomoto, Y., Katsura, H., Fujimura, T., Ogata, A., Baba, S., Yamaoka, A., Kihara, M., Abe, T., Nishimura, O., Kadota, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40617-y · Cited by 110 · see citing works
Jiang, D., & Scharffetter‐Kochanek, K. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00697 · Cited by 107 · see citing works
“TGF-β signaling is the most important pathway that determines granulation tissue formation and wound healing outcome (Desmouliere et al., 1993; Margadant and Sonnenberg, 2010; Lichtman et al., 2016; Jiang and Rinkevich, 2020).”
BackgroundThe extracellular matrix of the dermis: flexible structures with dynamic functions
Krieg, T. M., & Aumailley, M. (2011) · Experimental Dermatology · doi:10.1111/j.1600-0625.2011.01313.x · Cited by 107 · see citing works
Epithelial polarity – Generating and integrating signals from the ECM with integrins
Manninen, A. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.01.003 · Cited by 103 · see citing works
TGF beta −1, −2 and −3 in the modulation of fibrosis in the cornea and other organs
Wilson, S. E. (2021) · Experimental Eye Research · doi:10.1016/j.exer.2021.108594 · Cited by 108 · see citing works
Nowrin, K., Sohal, S. S., Peterson, G. M., Patel, R. P., & Walters, E. H. (2014) · Expert Review of Respiratory Medicine · doi:10.1586/17476348.2014.948853 · Cited by 99 · see citing works
“ILK, perhaps in combination with TGFb, induces the de novo expression of several integrins, such as a5b1, avb3 and avb6, which enhance the migration and invasion of carcinoma cells, particularly in conjunction with MMPs and fibronectin [89].”
Background
- Authors
- Margadant, C., & Sonnenberg, A.
- Affiliations
- The Netherlands Cancer Institute (NL)
- Corresponding author
- Sonnenberg, Arnoud
- Venue
- The EMBO Reports
- Published
- 2010-01-15
- Volume
- 11
- Issue
- 2
- Pages
- 97-105
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC2828749
- OpenAlex
- W2112195516
- Cited by
- 653
- References
- 81
- Citations by year
- 2026: 28 · 2025: 50 · 2024: 32 · 2023: 41 · 2022: 30 · 2021: 38 · 2020: 41 · 2019: 34 · 2018: 45 · 2017: 38 · 2016: 45 · 2015: 43 · 2014: 49 · 2013: 36 · 2012: 51
- FWCI
- 3.90
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- EMBO Reports (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Molecular Biology Organization
- Dystrophic Epidermolysis Bullosa Research Association
- KWF Kankerbestrijding
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- TGF-beta signaling, integrins, Smad signaling, TGF-beta receptor, cell adhesion, cell migration, fibrosis, systemic sclerosis, idiopathic pulmonary fibrosis, chronic obstructive pulmonary disease, cancer, wound healing, therapeutic target
- MeSH terms
- Animals, Fibrosis, Humans, Models, Biological, Neoplasms, Wound Healing, Integrins, Transforming Growth Factor beta, Disease Progression, Receptor Cross-Talk
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