Integrin-Mediated TGFβ Activation Modulates the Tumour Microenvironment

Brown, Nicholas F.; Marshall, John F.

doi:10.3390/cancers11091221

Cited by 116TGF-β signaling in diseasesCell Adhesion Molecules ResearchCancer Immunotherapy and Biomarkers

Integrin-Mediated TGFβ Activation Modulates the Tumour Microenvironment

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Brown, Nicholas F., Marshall, John F.·2019·Cancers

DOI 10.3390/cancers11091221PMC PMC6769837

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Abstract

TGFβ (transforming growth factor-beta) is a pleotropic cytokine with contrasting effects in cancer. In normal tissue and early tumours, TGFβ acts as a tumour suppressor, limiting proliferation and inducing apoptosis. However, these effects are eventually abrogated by the loss or inactivation of downstream signalling within the TGFβ pathway, and in established tumours, TGFβ then acts as a tumour promotor through multiple mechanisms including inducing epithelial-to-mesenchymal transition (EMT), promoting formation of cancer-associated fibroblasts (CAFs) and increasing angiogenesis. TGFβ is secrereted as a large latent complex and is embedded in the extracellular matrix or held on the surface of cells and must be activated before mediating its multiple functions. Thus, whilst TGFβ is abundant in the tumour microenvironment (TME), its functionality is regulated by local activation. The αv-integrins are major activators of latent-TGFβ. The potential benefits of manipulating the immune TME have been highlighted by the clinical success of immune-checkpoint inhibitors in a number of solid tumour types. TGFβ is a potent suppressor of T-cell-mediated immune surveillance and a key cause of resistance to checkpoint inhibitors. Therefore, as certain integrins locally activate TGFβ, they are likely to have a role in the immunosuppressive TME, although this remains to be confirmed. In this review, we discussed the role of TGFβ in cancer, the role of integrins in activating TGFβ in the TME, and the potential benefits of targeting integrins to augment immunotherapies.

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Atf4 expression is enriched in hepatic Tregs from Western diet-induced obese mice, where it contributes to liver fibrosis by promoting TGF-β activation through integrin αvβ8.
“A recent report further demonstrated that Atf4 expression is enriched in hepatic Tregs from Western diet-induced obese mice, where it contributes to liver fibrosis by promoting TGF-β activation through integrin αvβ8.”
From The double-edged sword of regulatory T cells in MASLD: from inflammation control to fibrosis promotion (2026) · cites this paper as Brown and Marshall 2019
Section 5.5 (Immunomodulation; page unavailable) states that Tregs activate TGF-β through integrin αvβ8. The paper does not report Atf4 enrichment in hepatic Tregs from Western diet-induced obese mice or show that this pathway contributes to liver fibrosis; its fibrosis discussion in section 3.6 concerns hepatic stellate cells and a different experimental condition. (LLM, conf=0.86)
Experimental — accuracy not yet measured
αvβ1, αvβ6 and αvβ8 mediate TGF-β1 activation.
“Since αvβ1, αvβ6 and αvβ8 mediate TGF-β1 activation81”
From TGFβ biology in cancer progression and immunotherapy (2021) · cites this paper as [81]

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PD-1 and PD-L1 Immune Checkpoint Blockade to Treat Breast Cancer
Hartkopf, A. D., Taran, F., Wallwiener, M., Walter, C. B., Krämer, B., Grischke, E., & Brucker, S. Y. (2016) · Breast Care · doi:10.1159/000453569 · Cited by 30,989 · see citing works
Epithelial-Mesenchymal Transitions in Development and Disease
Thiery, J. P., Acloque, H., Huang, R. Y. J., & Nieto, M. A. (2009) · Cell · doi:10.1016/j.cell.2009.11.007 · Cited by 9,931 · see citing works
Untitled work
Hynes (2002) · doi:10.1016/s0092-8674(02)00971-6 · Cited by 8,606 · see citing works
Mechanisms of TGF-β Signaling from Cell Membrane to the Nucleus
Shi, Y., & Massagué, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00432-x · Cited by 5,860 · see citing works
TGFβ attenuates tumour response to PD-L1 blockade by contributing to exclusion of T cells
Mariathasan, S., Turley, S. J., Nickles, D., Castiglioni, A., Yuen, K., Wang, Y., Kadel III, E. E., Koeppen, H., Astarita, J. L., Cubas, R., et al. (2018) · Nature · doi:10.1038/nature25501 · Cited by 5,400 · see citing works
Smad-dependent and Smad-independent pathways in TGF-β family signalling
Derynck, R., & Zhang, Y. E. (2003) · Nature · doi:10.1038/nature02006 · Cited by 5,370 · see citing works
Predictive correlates of response to the anti-PD-L1 antibody MPDL3280A in cancer patients
Herbst, R. S., Soria, J.-C., Kowanetz, M., Fine, G. D., Hamid, O., Gordon, M. S., Sosman, J. A., McDermott, D. F., Powderly, J. D., Gettinger, S. N., et al. (2014) · Nature · doi:10.1038/nature14011 · Cited by 5,231 · see citing works
TGFβ in Cancer
Massagué, J. (2008) · Cell · doi:10.1016/j.cell.2008.07.001 · Cited by 3,907 · see citing works
Atezolizumab in patients with locally advanced and metastatic urothelial carcinoma who have progressed following treatment with platinum-based chemotherapy: a single-arm, multicentre, phase 2 trial
Rosenberg, J. E., Hoffman-Censits, J., Powles, T., van der Heijden, M. S., Balar, A. V., Necchi, A., Dawson, N., O'Donnell, P. H., Balmanoukian, A., Loriot, Y., et al. (2016) · The Lancet · doi:10.1016/s0140-6736(16)00561-4 · Cited by 3,669 · see citing works
Pembrolizumab as Second-Line Therapy for Advanced Urothelial Carcinoma
Bellmunt, J., de Wit, R., Vaughn, D. J., Fradet, Y., Lee, J.-L., Fong, L., Vogelzang, N. J., Climent, M. A., Petrylak, D. P., Choueiri, T. K., et al. (2017) · New England Journal of Medicine · doi:10.1056/nejmoa1613683 · Cited by 3,395 · see citing works
Polarization of Tumor-Associated Neutrophil Phenotype by TGF-β: “N1” versus “N2” TAN
Fridlender, Z. G., Sun, J., Kim, S., Kapoor, V., Cheng, G., Ling, L. E., Worthen, G. S., & Albelda, S. Μ. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.06.017 · Cited by 3,382 · see citing works
Transitions between epithelial and mesenchymal states: acquisition of malignant and stem cell traits
Polyak, K., & Weinberg, R. A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2620 · Cited by 3,302 · see citing works
The Transforming Growth Factor-Beta Family
Massagué, J. (1990) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.06.110190.003121 · Cited by 3,041 · see citing works
Targeted disruption of the mouse transforming growth factor-β1 gene results in multifocal inflammatory disease
Shull, M. M., Ormsby, I., Kier, A. B., Pawlowski, S., Diebold, R. J., Yin, M., Allen, R., Sidman, C., Proetzel, G., Calvin, D., et al. (1992) · Nature · doi:10.1038/359693a0 · Cited by 2,985 · see citing works
Depletion of Carcinoma-Associated Fibroblasts and Fibrosis Induces Immunosuppression and Accelerates Pancreas Cancer with Reduced Survival
Özdemir, B. C., Pentcheva-Hoang, T., Carstens, J. L., Zheng, X., Wu, C.-C., Simpson, T. R., Laklai, H., Sugimoto, H., Kahlert, C., Novitskiy, S. V., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.04.005 · Cited by 2,681 · see citing works
Distinct populations of inflammatory fibroblasts and myofibroblasts in pancreatic cancer
Öhlund, D., Handly-Santana, A., Biffi, G., Elyada, E., Almeida, A. S., Ponz-Sarvise, M., Corbo, V., Oni, T. E., Hearn, S. A., Lee, E. J., et al. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20162024 · Cited by 2,590 · see citing works
Role of Transforming Growth Factor β in Human Disease
Blobe, G. C., Schiemann, W. P., & Lodish, H. F. (2000) · New England Journal of Medicine · doi:10.1056/nejm200005043421807 · Cited by 2,430 · see citing works
Transforming Growth Factor-β Signaling in Immunity and Cancer
Batlle, E., & Massagué, J. (2019) · Immunity · doi:10.1016/j.immuni.2019.03.024 · Cited by 2,366 · see citing works
Mechanism of activation of the TGF-β receptor
Wrana, J. L., Attisano, L., Wieser, R., Ventura, F., & Massagué, J. (1994) · Nature · doi:10.1038/370341a0 · Cited by 2,340 · see citing works
Atezolizumab as first-line treatment in cisplatin-ineligible patients with locally advanced and metastatic urothelial carcinoma: a single-arm, multicentre, phase 2 trial
Balar, A. V., Galsky, M. D., Rosenberg, J. E., Powles, T., Petrylak, D. P., Bellmunt, J., Loriot, Y., Necchi, A., Hoffman-Censits, J., Perez-Gracia, J. L., et al. (2017) · The Lancet · doi:10.1016/s0140-6736(16)32455-2 · Cited by 2,199 · see citing works
Immune-related adverse events with immune checkpoint blockade: a comprehensive review
Michot, J. M., Bigenwald, C., Champiat, S., Collins, M., Carbonnel, F., Postel-Vinay, S., Berdelou, A., Varga, A., Bahleda, R., Hollebecque, A., et al. (2016) · European Journal of Cancer · doi:10.1016/j.ejca.2015.11.016 · Cited by 2,127 · see citing works
Stromal Elements Act to Restrain, Rather Than Support, Pancreatic Ductal Adenocarcinoma
Rhim, A. D., Oberstein, P. E., Thomas, D. H., Mirek, E. T., Palermo, C. F., Sastra, S. A., Dekleva, E. N., Saunders, T., Becerra, C. P., Tattersall, I. W., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.04.021 · Cited by 2,085 · see citing works
A Mechanism for Regulating Pulmonary Inflammation and Fibrosis: The Integrin αvβ6 Binds and Activates Latent TGF β1
Munger, J. S., Huang, X., Kawakatsu, H., Griffiths, M. J. D., Dalton, S. L., Wu, J., Pittet, J.-F., Kaminski, N., Garat, C., Matthay, M. A., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80545-0 · Cited by 2,076 · see citing works
Transforming growth factor beta 1 null mutation in mice causes excessive inflammatory response and early death.
Kulkarni, A. B., Huh, C. G., Becker, D., Geiser, A., Lyght, M., Flanders, K. C., Roberts, A. B., Sporn, M. B., Ward, J. M., & Karlsson, S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.2.770 · Cited by 1,967 · see citing works
EMT in cancer
Brabletz, T., Kalluri, R., Nieto, M. A., & Weinberg, R. A. (2018) · Nature Reviews Cancer · doi:10.1038/nrc.2017.118 · Cited by 1,961 · see citing works
Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis.
Yu, Q., & Stamenkovic, I. (2000) · PubMed · Cited by 1,952 · see citing works
How cells read TGF-β signals
Massagué, J. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35043051 · Cited by 1,882 · see citing works
TGFβ drives immune evasion in genetically reconstituted colon cancer metastasis
Tauriello, D. V. F., Palomo-Ponce, S., Stork, D., Berenguer-Llergo, A., Badia-Ramentol, J., Iglesias, M., Sevillano, M., Ibiza, S., Cañellas, A., Hernando-Momblona, X., et al. (2018) · Nature · doi:10.1038/nature25492 · Cited by 1,851 · see citing works
Molecular requirements for epithelial–mesenchymal transition during tumor progression
Huber, M. A., Kraut, N., & Beug, H. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.08.001 · Cited by 1,823 · see citing works
Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-β and promotes tumor invasion and angiogenesis
Yu, Q., & Stamenkovic, I. (2000) · Genes & Development · doi:10.1101/gad.14.2.163 · Cited by 1,754 · see citing works
Integrin ligands at a glance
Humphries, J. D., Byron, A., & Humphries, M. J. (2006) · Journal of Cell Science · doi:10.1242/jcs.03098 · Cited by 1,711 · see citing works
Structural Basis of Integrin Regulation and Signaling
Luo, B., Carman, C. V., & Springer, T. A. (2007) · Annual Review of Immunology · doi:10.1146/annurev.immunol.25.022106.141618 · Cited by 1,662 · see citing works
Cell Contact–Dependent Immunosuppression by Cd4+Cd25+Regulatory T Cells Is Mediated by Cell Surface–Bound Transforming Growth Factor β
Nakamura, K., Kitani, A., & Strober, W. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.194.5.629 · Cited by 1,596 · see citing works
Localization of Matrix Metalloproteinase MMP-2 to the Surface of Invasive Cells by Interaction with Integrin αvβ3
Brooks, P. C., Strömblad, S., Sanders, L. C., Schalscha, T. V., Aimes, R. T., Stetler‐Stevenson, W. G., Quigley, J. P., & Cheresh, D. A. (1996) · Cell · doi:10.1016/s0092-8674(00)81235-0 · Cited by 1,552 · see citing works
Every step of the way: integrins in cancer progression and metastasis
Hamidi, H., & Ivaska, J. (2018) · Nature Reviews Cancer · doi:10.1038/s41568-018-0038-z · Cited by 1,493 · see citing works
Angiogenesis in cancer
Nishida, N., Yano, H., Nishida, T., Kamura, T., & Kojiro, M. (2006) · Vascular Health and Risk Management · doi:10.2147/vhrm.2006.2.3.213 · Cited by 1,467 · see citing works
Myofibroblast contraction activates latent TGF-β1 from the extracellular matrix
Wipff, P.-J., Rifkin, D. B., Meister, J.-J., & Hinz, B. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704042 · Cited by 1,346 · see citing works
TGF-β and the TGF-β family: context-dependent roles in cell and tissue physiology
Morikawa, M., Derynck, R., & Miyazono, K. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021873 · Cited by 1,321 · see citing works
Immune checkpoint blockade therapy for cancer: An overview of FDA-approved immune checkpoint inhibitors
Hargadon, K. M., Johnson, C. E., & Williams, C. J. (2018) · International Immunopharmacology · doi:10.1016/j.intimp.2018.06.001 · Cited by 1,211 · see citing works
Integrin Structure, Activation, and InteractionsPreprint
Campbell, I. D., & Humphries, M. J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004994 · Cited by 1,192 · see citing works
Global Conformational Rearrangements in Integrin Extracellular Domains in Outside-In and Inside-Out Signaling
Takagi, J., Petre, B. M., Walz, T., & Springer, T. A. (2002) · Cell · doi:10.1016/s0092-8674(02)00935-2 · Cited by 1,168 · see citing works
Stromal gene expression defines poor-prognosis subtypes in colorectal cancer
Calon, A., Lonardo, E., Berenguer-Llergo, A., Espinet, E., Hernando-Momblona, X., Iglesias, M., Sevillano, M., Palomo-Ponce, S., Tauriello, D. V. F., Byrom, D., et al. (2015) · Nature Genetics · doi:10.1038/ng.3225 · Cited by 1,070 · see citing works
Non-Smad TGF-β signals
Moustakas, A., & Heldin, C. (2005) · Journal of Cell Science · doi:10.1242/jcs.02554 · Cited by 1,069 · see citing works
Cilengitide combined with standard treatment for patients with newly diagnosed glioblastoma with methylated MGMT promoter (CENTRIC EORTC 26071-22072 study): a multicentre, randomised, open-label, phase 3 trial
Stupp, R., Hegi, M. E., Gorlia, T., Erridge, S. C., Perry, J., Hong, Y.-K., Aldape, K. D., Lhermitte, B., Pietsch, T., Grujicic, D., et al. (2014) · The Lancet Oncology · doi:10.1016/s1470-2045(14)70379-1 · Cited by 1,052 · see citing works
Defective haematopoiesis and vasculogenesis in transforming growth factor-β1 knock out mice
Dickson, M. C., Martin, J. S., Cousins, F. M., Kulkarni, A. B., Karlsson, S., & Akhurst, R. J. (1995) · Development · doi:10.1242/dev.121.6.1845 · Cited by 1,029 · see citing works
TGF-β and immune cells: an important regulatory axis in the tumor microenvironment and progression
Yang, L., Pang, Y., & Moses, H. L. (2010) · Trends in Immunology · doi:10.1016/j.it.2010.04.002 · Cited by 1,023 · see citing works
Latent TGF-β structure and activation
Shi, M., Zhu, J., Wang, R., Chen, X., Mi, L., Walz, T., & Springer, T. A. (2011) · Nature · doi:10.1038/nature10152 · Cited by 1,013 · see citing works
The Where, the When, and the How of Immune Monitoring for Cancer Immunotherapies in the Era of Checkpoint Inhibition
Hegde, P. S., Karanikas, V., & Evers, S. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-1507 · Cited by 1,000 · see citing works
TGF-β signaling blockade inhibits PTHrP secretion by breast cancer cells and bone metastases development
Yin, J. J., Selander, K. S., Chirgwin, J. M., Dallas, M., Grubbs, B. G., Wieser, R., Massagué, J., Mundy, G. R., & Guise, T. A. (1999) · Journal of Clinical Investigation · doi:10.1172/jci3523 · Cited by 988 · see citing works
Prognostic value of tumor-infiltrating FoxP3+ regulatory T cells in cancers: a systematic review and meta-analysis
Shang, B., Liu, Y., Jiang, S.-J., & Liu, Y. (2015) · Scientific Reports · doi:10.1038/srep15179 · Cited by 985 · see citing works
CD4+CD25+ regulatory T cells inhibit natural killer cell functions in a transforming growth factor–β–dependent manner
Ghiringhelli, F., Menard, C., Terme, M., Flament, C., Taı̈eb, J., Chaput, N., Puig, P. E., Novault, S., Escudier, B. J., Vivier, É., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20051511 · Cited by 948 · see citing works
The polarization of immune cells in the tumour environment by TGFβ
Flavell, R. A., Sanjabi, S., Wrzesinski, S. H., & Licona-Limón, P. (2010) · Nature Reviews Immunology · doi:10.1038/nri2808 · Cited by 940 · see citing works
TGF-beta induced transdifferentiation of mammary epithelial cells to mesenchymal cells: involvement of type I receptors.
Miettinen, P. J., Ebner, R., Lopez, A. R., & Derynck, R. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.127.6.2021 · Cited by 939 · see citing works
The roles of TGFβ in the tumour microenvironment
Pickup, M. W., Novitskiy, S. V., & Moses, H. L. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3603 · Cited by 915 · see citing works
TGF-β: A Master of All T Cell Trades
Li, M. O., & Flavell, R. A. (2008) · Cell · doi:10.1016/j.cell.2008.07.025 · Cited by 888 · see citing works
Targeting of αv integrin identifies a core molecular pathway that regulates fibrosis in several organs
Henderson, N. C., Arnold, T. D., Katamura, Y., Giacomini, M. M., Rodriguez, J. D., McCarty, J. H., Pellicoro, A., Raschperger, E., Betsholtz, C., Ruminski, P. G., et al. (2013) · Nature Medicine · doi:10.1038/nm.3282 · Cited by 866 · see citing works
TGF-β Activation and Function in Immunity
Travis, M. A., & Sheppard, D. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032713-120257 · Cited by 856 · see citing works
Phenotypic Diversity and Plasticity in Circulating Neutrophil Subpopulations in Cancer
Sagiv, J. Y., Michaeli, J., Assi, S., Mishalian, I., Kisos, H., Levy, L., Damti, P., Lumbroso, D., Polyansky, L., Sionov, R. V., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2014.12.039 · Cited by 818 · see citing works
Smad3 and NFAT cooperate to induce Foxp3 expression through its enhancer
Tone, Y., Furuuchi, K., Kojima, Y., Tykocinski, M. L., Greene, M. I., & Tone, M. (2008) · Nature Immunology · doi:10.1038/ni1549 · Cited by 807 · see citing works
Immune-mediated eradication of tumors through the blockade of transforming growth factor-β signaling in T cells
Gorelik, L., & Flavell, R. A. (2001) · Nature Medicine · doi:10.1038/nm1001-1118 · Cited by 770 · see citing works
TGF-β Superfamily Signaling in Embryonic Development and Homeostasis
Wu, M., & Hill, C. S. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.02.012 · Cited by 743 · see citing works
The integrin αvβ8 mediates epithelial homeostasis through MT1-MMP–dependent activation of TGF-β1
Mu, D., Cambier, S., Fjellbirkeland, L., Baron, J. L., Munger, J. S., Kawakatsu, H., Sheppard, D., Broaddus, V. C., & Nishimura, S. L. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200109100 · Cited by 729 · see citing works
T Cell-Produced Transforming Growth Factor-β1 Controls T Cell Tolerance and Regulates Th1- and Th17-Cell Differentiation
Li, M. O., Wan, Y. Y., & Flavell, R. A. (2007) · Immunity · doi:10.1016/j.immuni.2007.03.014 · Cited by 728 · see citing works
Immune related adverse events associated with anti-CTLA-4 antibodies: systematic review and meta-analysis
Bertrand, A., Kostine, M., Barnetche, T., Truchetet, M.-E., & Schaeverbeke, T. (2015) · BMC Medicine · doi:10.1186/s12916-015-0455-8 · Cited by 704 · see citing works
Integrin–TGF‐β crosstalk in fibrosis, cancer and wound healing
Margadant, C., & Sonnenberg, A. (2010) · The EMBO Reports · doi:10.1038/embor.2009.276 · Cited by 653 · see citing works
Enhanced pathological angiogenesis in mice lacking β3 integrin or β3 and β5 integrins
Reynolds, L. E., Wyder, L., Lively, J. C., Taverna, D., Robinson, S. D., Huang, X., Sheppard, D., Hynes, R. O., & Hodivala‐Dilke, K. (2002) · Nature Medicine · doi:10.1038/nm0102-27 · Cited by 614 · see citing works
Targeting the TGFβ pathway for cancer therapy
Neuzillet, C., Tijeras‐Raballand, A., Cohen, R., Cros, J. F., Faivre, S. J., Raymond, É., & Gramont, A. D. E. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.11.001 · Cited by 610 · see citing works
Localized and reversible TGFβ signalling switches breast cancer cells from cohesive to single cell motility
Giampieri, S., Manning, C. S., Hooper, S., Jones, J. L., Hill, C. S., & Sahai, E. A. (2009) · Nature Cell Biology · doi:10.1038/ncb1973 · Cited by 602 · see citing works
LOX-Mediated Collagen Crosslinking Is Responsible for Fibrosis-Enhanced Metastasis
Cox, T. R., Bird, D., Baker, A.-M., Barker, H. E., Ho, M. W.-Y., Lang, G., & Erler, J. T. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-2233 · Cited by 571 · see citing works
Clinical development of galunisertib (LY2157299 monohydrate), a small molecule inhibitor of transforming growth factor-beta signaling pathway
Lahn, M. M. F., Herbertz, S., Sawyer, J. S., Stauber, A. J., Gueorguieva, I., Driscoll, K. E., Estrem, S. T., Cleverly, A., Desaiah, D., Guba, S. C., et al. (2015) · Drug Design Development and Therapy · doi:10.2147/dddt.s86621 · Cited by 558 · see citing works
Alterations in components of the TGF-β superfamily signaling pathways in human cancer
LEVY, L., & HILL, C. (2006) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2005.09.009 · Cited by 539 · see citing works
TGF-β-miR-34a-CCL22 Signaling-Induced Treg Cell Recruitment Promotes Venous Metastases of HBV-Positive Hepatocellular Carcinoma
Yang, P., Li, Q.-J., Feng, Y., Zhang, Y., Markowitz, G. J., Ning, S., Deng, Y., Zhao, J., Jiang, S., Yuan, Y., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.07.023 · Cited by 536 · see citing works
A high M1/M2 ratio of tumor-associated macrophages is associated with extended survival in ovarian cancer patients
Zhang, M., He, Y., Sun, X., Li, Q. Y., Wang, W., Zhao, A., & Di, W. J. (2014) · Journal of Ovarian Research · doi:10.1186/1757-2215-7-19 · Cited by 530 · see citing works
T cells that cannot respond to TGF-β escape control by CD4+CD25+ regulatory T cells
Fahlén, L., Read, S., Gorelik, L., Hurst, S. D., Coffman, R. L., Flavell, R. A., & Powrie, F. M. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20040685 · Cited by 516 · see citing works
Integrins and the activation of latent transforming growth factor β1 – An intimate relationship
Wipff, P., & Hinz, B. (2008) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2008.01.012 · Cited by 514 · see citing works
Loss of integrin αvβ8 on dendritic cells causes autoimmunity and colitis in mice
Travis, M. A., Reizis, B., Melton, A. C., Masteller, E., Tang, Q., Proctor, J. M., Wang, Y., Bernstein, X., Huang, X., Reichardt, L. F., et al. (2007) · Nature · doi:10.1038/nature06110 · Cited by 503 · see citing works
Integrin αVβ6-mediated activation of latent TGF-β requires the latent TGF-β binding protein-1
Annes, J. P., Chen, Y., Munger, J. S., & Rifkin, D. B. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200312172 · Cited by 500 · see citing works
Cellular Mechanisms of Fatal Early-Onset Autoimmunity in Mice with the T Cell-Specific Targeting of Transforming Growth Factor-β Receptor
Marie, J. C., Liggitt, D., & Rudensky, A. Y. (2006) · Immunity · doi:10.1016/j.immuni.2006.07.012 · Cited by 480 · see citing works
GARP (LRRC32) is essential for the surface expression of latent TGF-β on platelets and activated FOXP3 + regulatory T cells
Tran, D. Q., Andersson, J., Wang, R., Ramsey, H. E., Unutmaz, D., & Shevach, E. M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901944106 · Cited by 473 · see citing works
Integrin activation
Calderwood, D. (2004) · Journal of Cell Science · doi:10.1242/jcs.01014 · Cited by 428 · see citing works
TGFβ signaling plays a critical role in promoting alternative macrophage activation
Gong, D., Shi, W., Yi, S.-J., Chen, H., Groffen, J., & Heisterkamp, N. (2012) · BMC Immunology · doi:10.1186/1471-2172-13-31 · Cited by 424 · see citing works
Latent Transforming Growth Factor-β (TGF-β) Binding Proteins: Orchestrators of TGF-β Availability
Rifkin, D. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400029200 · Cited by 422 · see citing works
Nucleocytoplasmic Shuttling of Smads 2, 3, and 4 Permits Sensing of TGF-β Receptor Activity
Inman, G. J., Nicolás, F. J., & Hill, C. S. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00585-3 · Cited by 417 · see citing works
Global analysis of gene expression in pulmonary fibrosis reveals distinct programs regulating lung inflammation and fibrosis
Kaminski, N., Allard, J. D., Pittet, J., Zuo, F., Griffiths, M., Morris, D. G., Huang, X., Sheppard, D., & Heller, R. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.4.1778 · Cited by 416 · see citing works
Regulation of the Bioavailability of TGF-β and TGF-β-Related Proteins
Robertson, I. B., & Rifkin, D. B. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021907 · Cited by 403 · see citing works
Mutational inactivation of transforming growth factor beta receptor type II in microsatellite stable colon cancers.
Grady, W. M., Myeroff, L. L., Swinler, S. E., Rajput, A., Thiagalingam, S., Lutterbaugh, J., Neumann, A., Brattain, M. G., Chang, J., Kim, S., et al. (1999) · PubMed · Cited by 391 · see citing works
Integrin β1 Signaling Is Necessary for Transforming Growth Factor-β Activation of p38MAPK and Epithelial Plasticity
Bhowmick, N. A., Zent, R., Ghiassi, M., McDonnell, M. A., & Moses, H. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106176200 · Cited by 388 · see citing works
Differentiation plasticity regulated by TGF-β family proteins in development and disease
Derynck, R., & Akhurst, R. J. (2007) · Nature Cell Biology · doi:10.1038/ncb434 · Cited by 383 · see citing works
Transcriptional activation of integrin β6 during the epithelial-mesenchymal transition defines a novel prognostic indicator of aggressive colon carcinoma
Bates, R. C., Bellovin, D. I., Brown, C. L., Maynard, E., Wu, B., Kawakatsu, H., Sheppard, D., Oettgen, P., & Mercurio, A. M. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23183 · Cited by 380 · see citing works
Structural Biology and Evolution of the TGF-β FamilyPreprint
Hinck, A. P., Mueller, T. D., & Springer, T. A. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022103 · Cited by 364 · see citing works
The role of proteases in transforming growth factor-β activation
Jenkins, G. R. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.11.026 · Cited by 358 · see citing works
Latent TGF-β Binding Proteins: Extracellular Matrix Association and Roles in TGF-β Activation
Hyytiäinen, M. M., Penttinen, C., & Keski‐Oja, J. (2004) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360490460933 · Cited by 351 · see citing works
Complexities of TGF-β Targeted Cancer Therapy
Connolly, E. C., Freimuth, J., & Akhurst, R. J. (2012) · International Journal of Biological Sciences · doi:10.7150/ijbs.4564 · Cited by 344 · see citing works
Platelets subvert T cell immunity against cancer via GARP-TGFβ axis
Rachidi, S., Metelli, A., Riesenberg, B., Wu, B. X., Nelson, M. H., Wallace, C., Paulos, C. M., Rubinstein, M. P., Garrett-Mayer, E. S., Hennig, M., et al. (2017) · Science Immunology · doi:10.1126/sciimmunol.aai7911 · Cited by 338 · see citing works
Activated integrin αvβ3 cooperates with metalloproteinase MMP-9 in regulating migration of metastatic breast cancer cells
Rolli, M., Fransvea, E., Pilch, J., Saven, A., & Felding‐Habermann, B. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1633689100 · Cited by 333 · see citing works
Absence of integrin-mediated TGFβ1 activation in vivo recapitulates the phenotype of TGFβ1-null mice
Yang, Z., Mu, Z., Dabovic, B., Jurukovski, V., Yu, D., Sung, J. J., Xiong, X., & Munger, J. S. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611044 · Cited by 321 · see citing works
Recombinant latent transforming growth factor beta 1 has a longer plasma half-life in rats than active transforming growth factor beta 1, and a different tissue distribution.
Wakefield, L. M., Winokur, T. S., Hollands, R. S., Christopherson, K. S., Levinson, A. D., & Sporn, M. B. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114932 · Cited by 320 · see citing works
Smad4 signalling in T cells is required for suppression of gastrointestinal cancer
Kim, B., Li, C., Qiao, W., Mamura, M., Kasperczak, B., Anver, M. R., Wolfraim, L. A., Hong, S., Mushinski, E. B., Potter, M., et al. (2006) · Nature · doi:10.1038/nature04846 · Cited by 320 · see citing works
Expression of transforming growth factor beta type II receptor leads to reduced malignancy in human breast cancer MCF-7 cells
Sun, L., Wu, G., Willson, J. K. V., Zborowska, E., Yang, J., Rajkarunanayake, I., Wang, J., Gentry, L. E., Wang, X. F., & Brattain, M. G. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47215-8 · Cited by 319 · see citing works
Inactivation of the integrin beta 6 subunit gene reveals a role of epithelial integrins in regulating inflammation in the lung and skin.
Huang, X., Wu, J. F., Cass, D. L., Erle, D. J., Corry, D. B., Young, S. G., Farese, R. V., & Sheppard, D. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.133.4.921 · Cited by 316 · see citing works
v Integrins in Angiogenesis and CancerPreprint
Weis, S. M., & Cheresh, D. A. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006478 · Cited by 311 · see citing works
Inter‐ and intra‐tumoural heterogeneity in cancer‐associated fibroblasts of human pancreatic ductal adenocarcinoma
Neuzillet, C., Tijeras‐Raballand, A., Ragulan, C., Cros, J. F., Patil, Y., Martinet, M., Erkan, M., Kleeff, J. H., Wilson, J. S., Apte, M. V., et al. (2018) · The Journal of Pathology · doi:10.1002/path.5224 · Cited by 296 · see citing works
Identification of amino acid sequences in the integrin beta 1 cytoplasmic domain implicated in cytoskeletal association
Reszka, A. A., Hayashi, Y., & Horwitz, A. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.117.6.1321 · Cited by 281 · see citing works
Force interacts with macromolecular structure in activation of TGF-β
Dong, X., Zhao, B., Iacob, R. E., Zhu, J., Koksal, A. C., Lu, C., Engen, J. R., & Springer, T. A. (2017) · Nature · doi:10.1038/nature21035 · Cited by 273 · see citing works
Loss of TGFβ Signaling Destabilizes Homeostasis and Promotes Squamous Cell Carcinomas in Stratified Epithelia
Guasch, G., Schöber, M., Pasolli, H. A., Conn, E. B., Polak, L., & Fuchs, E. V. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.08.020 · Cited by 267 · see citing works
β8 integrins are required for vascular morphogenesis in mouse embryos
Zhu, J., Motejlek, K., Wang, D., Zang, K., Schmidt, A., & Reichardt, L. F. (2002) · Development · doi:10.1242/dev.129.12.2891 · Cited by 267 · see citing works
The Single-Molecule Mechanics of the Latent TGF-β1 Complex
Buscemi, L., Ramonet, D., Klingberg, F., Formey, A., Smith-Clerc, J., Meister, J.-J., & Hinz, B. (2011) · Current Biology · doi:10.1016/j.cub.2011.11.037 · Cited by 257 · see citing works
Integrins
Silva, R., D’Amico, G., Hodivala‐Dilke, K., & Reynolds, L. E. (2008) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.108.172015 · Cited by 254 · see citing works
Two cilengitide regimens in combination with standard treatment for patients with newly diagnosed glioblastoma and unmethylated MGMT gene promoter: results of the open-label, controlled, randomized phase II CORE study
Nabors, B., Fink, K., Mikkelsen, T., Grujičić, D., Tarnawski, R., Nam, D. H., Mazurkiewicz, M., Salacz, M. E., Ashby, L. S., Zagonel, V., et al. (2015) · Neuro-Oncology · doi:10.1093/neuonc/nou356 · Cited by 242 · see citing works
Interactions between Growth Factors and Integrins: Latent Forms of Transforming Growth Factor-β Are Ligands for the Integrin αvβ1
Munger, J. S., Harpel, J. G., Giancotti, F. G., & Rifkin, D. B. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.9.2627 · Cited by 239 · see citing works
Differentiation plasticity regulated by TGF-|[beta]| family proteins in development and disease
Derynck, R., & Akhurst, R. J. (2007) · Nature · doi:10.1038/ncb0907-1000 · Cited by 227 · see citing works
Mice that lack activity of αvβ6- and αvβ8-integrins reproduce the abnormalities of Tgfb1 - and Tgfb3 -null mice
Aluwihare, P., Mu, Z., Zhao, Z., Yu, D., Weinreb, P. H., Horan, G. S. B., Violette, S. M., & Munger, J. S. (2008) · Journal of Cell Science · doi:10.1242/jcs.035246 · Cited by 224 · 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
Complete integrin headpiece opening in eight steps
Zhu, J., Zhu, J., & Springer, T. A. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201212037 · Cited by 215 · see citing works
Targeting TGF-β signaling in cancer
Katz, L. H., Li, Y., Chen, J.-S., Muñoz, N. M., Majumdar, A., Chen, J., & Mishra, L. (2013) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.782287 · Cited by 212 · see citing works
The TGF-β Signaling Regulator PMEPA1 Suppresses Prostate Cancer Metastases to Bone
Fournier, P. G. J., Juárez, P., Jiang, G., Clines, G. A., Niewolna, M., Kim, H. S., Walton, H. W., Peng, X., Liu, Y., Mohammad, K. S., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2015.04.009 · Cited by 212 · see citing works
Extracellular Matrix-Associated Transforming Growth Factor-β: Role in Cancer Cell Growth and Invasion
Taipale, J., Saharinen, J., & Keski‐Oja, J. (1998) · Advances in cancer research · doi:10.1016/s0065-230x(08)60740-x · Cited by 209 · see citing works
Integrin αvβ8-Mediated TGF-β Activation by Effector Regulatory T Cells Is Essential for Suppression of T-Cell-Mediated Inflammation
Worthington, J. J., Kelly, A., Smedley, C., Bauché, D., Campbell, S. S., Marie, J. C., & Travis, M. A. (2015) · Immunity · doi:10.1016/j.immuni.2015.04.012 · Cited by 199 · see citing works
Switching TGFβ from a tumor suppressor to a tumor promoter
Inman, G. J. (2011) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2010.12.004 · Cited by 197 · see citing works
Disruption of the antiproliferative TGF-β signaling pathways in human pancreatic cancer cells
Villanueva, A., García, C., Paules, A. B., Vicente, M., Megías, M., Reyes, G., Villalonga, P., Agell, N., Lluı́s, F., Bachs, O., et al. (1998) · Oncogene · doi:10.1038/sj.onc.1202118 · Cited by 194 · see citing works
A randomized phase 2 study of etaracizumab, a monoclonal antibody against integrin αvβ3, ± dacarbazine in patients with stage IV metastatic melanoma
Hersey, P., Sosman, J. A., O'Day, S. J., Richards, J. M., Bedikian, A. Y., Gonzalez, R. C., Sharfman, W. H., Weber, R. W., Logan, T. F., Buzoianu, M., et al. (2010) · Cancer · doi:10.1002/cncr.24821 · Cited by 190 · see citing works
A Pilot Trial of Vitaxin, A Humanized Anti-Vitronectin Receptor (anti α v β 3 ) Antibody in Patients with Metastatic Cancer
Posey, J. A., Khazaeli, M. B., Delgrosso, A., Saleh, M. N., Lin, C., Huse, W. D., & LoBuglio, A. F. (2001) · Cancer Biotherapy and Radiopharmaceuticals · doi:10.1089/108497801300189218 · Cited by 189 · see citing works
A Peptide Selected by Biopanning Identifies the Integrin αvβ6 as a Prognostic Biomarker for Nonsmall Cell Lung Cancer
Elayadi, A. N., Samli, K. N., Prudkin, L., Liu, Y.-H., Bian, A., Xie, X., Wistuba, I. I., Roth, J. A., McGuire, M. J., & Brown, K. C. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0245 · Cited by 189 · see citing works
The transforming growth factor beta receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand.
Moustakas, A., Lin, H. Y.-F., Henis, Y. I., Plamondon, J., O'Connor‐McCourt, M. D., & Lodish, H. F. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41509-8 · Cited by 181 · see citing works
Fibronectin is required for integrin o:vβ6‐mediated activation of latent TGF‐β complexes containing LTBP‐1
Fontana, L., Chen, Y., Prijatelj, P., Sakai, T., Fässler, R., Sakai, L. Y., & Rifkin, D. B. (2005) · The FASEB Journal · doi:10.1096/fj.05-4134com · Cited by 181 · see citing works
GARP regulates the bioavailability and activation of TGFβ
Wang, R., Zhu, J., Dong, X., Shi, M., Lu, C., & Springer, T. A. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-12-1018 · Cited by 180 · see citing works
Overexpression of the αvβ6 integrin in cervical squamous cell carcinoma is a prognostic factor for decreased survival
Hazelbag, S., Kenter, G. G., Gorter, A., Dreef, E., Koopman, L., Violette, S., Weinreb, P. H., & Fleuren, G. J. (2007) · The Journal of Pathology · doi:10.1002/path.2168 · Cited by 178 · see citing works
Cloning and expression of a divergent integrin subunit beta 8.
Moyle, M., Napier, M. A., & McLean, J. W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55042-0 · Cited by 177 · see citing works
Increased Expression of Integrin αvβ5 Induces the Myofibroblastic Differentiation of Dermal Fibroblasts
Asano, Y., Ihn, H., Yamane, K., Jinnin, M., & Tamaki, K. (2006) · The American Journal of Pathology · doi:10.2353/ajpath.2006.041306 · Cited by 175 · see citing works
The integrin αVβ6 binds and activates latent TGFβ3
Annes, J. P., Rifkin, D. B., & Munger, J. S. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03280-x · Cited by 173 · see citing works
The αvβ6 Integrin Is Transferred Intercellularly via Exosomes
Fedele, C., Singh, A., Zerlanko, B. J., Iozzo, R. V., & Languino, L. R. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.c114.617662 · Cited by 167 · see citing works
Signal transduction by members of the transforming growth factor-β superfamily
Attisano, L., & Wrana, J. L. (1996) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(96)00042-1 · Cited by 159 · see citing works
Autocrine Transforming Growth Factor-β Signaling Mediates Smad-independent Motility in Human Cancer Cells
Dumont, N., Bakin, A. V., & Arteaga, C. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m204623200 · Cited by 159 · see citing works
Exosome-mediated Transfer of αvβ3 Integrin from Tumorigenic to Nontumorigenic Cells Promotes a Migratory Phenotype
Singh, A., Fedele, C., Lu, H., Nevalainen, M. T., Keen, J. H., & Languino, L. R. (2016) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-16-0058 · Cited by 157 · see citing works
Monoclonal antibodies against GARP/TGF-β1 complexes inhibit the immunosuppressive activity of human regulatory T cells in vivo
Cuende, J., Liénart, S., Dedobbeleer, O., van der Woning, B., De Boeck, G., Stockis, J., Huygens, C., Colau, D., Somja, J., Delvenne, P., et al. (2015) · Science Translational Medicine · doi:10.1126/scitranslmed.aaa1983 · Cited by 155 · see citing works
Structural basis of latent TGF-β1 presentation and activation by GARP on human regulatory T cells
Liénart, S., Merceron, R., Vanderaa, C., Lambert, F., Colau, D., Stockis, J., van der Woning, B., de Haard, H., Saunders, M. J., Coulie, P. G., et al. (2018) · Science · doi:10.1126/science.aau2909 · Cited by 153 · see citing works
Integrin αvβ5-Mediated TGF-β Activation by Airway Smooth Muscle Cells in Asthma
Tatler, A. L., John, A. E., Jolly, L., Habgood, A., Porte, J., Brightling, C. E., Knox, A. J., Pang, L., Sheppard, D., Huang, X., et al. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1003507 · Cited by 149 · see citing works
The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization.
Chacko, B. M., Qin, B. Y., Correia, J. J., Lam, S. S., de Caestecker, M. P., & Lin, K. F. (2001) · Nature Structural Biology · doi:10.1038/84995 · Cited by 146 · see citing works
Antibody-Mediated Blockade of Integrin αvβ6 Inhibits Tumor Progression <i>In vivo</i> by a Transforming Growth Factor-β–Regulated Mechanism
Koopman Van Aarsen, L. A., Leone, D. R., Ho, S., Dolinski, B. M., McCoon, P. E., LePage, D. J., Kelly, R., Heaney, G., Rayhorn, P., Reid, C., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-2307 · Cited by 146 · see citing works
Therapeutic Targeting of Integrin αvβ6 in Breast Cancer
Moore, K. M., Thomas, G. J., Duffy, S. W., Warwick, J., Gabe, R., Chou, P., Ellis, I. O., Green, A. R., Haider, S. A., Brouilette, K., et al. (2014) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/dju169 · Cited by 144 · see citing works
Self-citation
Blockade of surface-bound TGF-β on regulatory T cells abrogates suppression of effector T cell function in the tumor microenvironment
Budhu, S., Schaer, D., Li, Y., Toledo‐Crow, R., Panageas, K. S., Yang, X., Zhong, H., Houghton, A. N., Silverstein, S. C., Merghoub, T., et al. (2017) · Science Signaling · doi:10.1126/scisignal.aak9702 · Cited by 144 · see citing works
Structural determinants of integrin β-subunit specificity for latent TGF-β
Dong, X., Hudson, N. E., Lu, C., & Springer, T. A. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2905 · Cited by 141 · see citing works
Snail and Slug, key regulators of TGF-β-induced EMT, are sufficient for the induction of single-cell invasion
Naber, H. P. H., Drabsch, Y., Snaar-Jagalska, E. B., ten Dijke, P., & van Laar, T. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.04.037 · Cited by 135 · see citing works
TGF-β is responsible for NK cell immaturity during ontogeny and increased susceptibility to infection during mouse infancy
Marcoe, J. P., Lim, J., Schaubert, K. L., Fodil-Cornu, N., Matka, M., McCubbrey, A. L., Farr, A. R., Vidal, S. M., & Laouar, Y. (2012) · Nature Immunology · doi:10.1038/ni.2388 · Cited by 134 · see citing works
The integrin alphavbeta3 is a receptor for the latency-associated peptides of transforming growth factors beta1 and beta3
Ludbrook, S. B., Barry, S. T., Delves, C. J., & Horgan, C. M. T. (2003) · Biochemical Journal · doi:10.1042/bj20020809 · Cited by 126 · see citing works
Abituzumab combined with cetuximab plus irinotecan versus cetuximab plus irinotecan alone for patients with KRAS wild-type metastatic colorectal cancer: the randomised phase I/II POSEIDON trial
Élez, E., Kocáková, I., Höhler, T., Martens, U. M., Bokemeyer, C., Cutsem, E. V., Melichar, B., Šmakal, M., Csőszi, T., Топузов, Э. Э., et al. (2014) · Annals of Oncology · doi:10.1093/annonc/mdu474 · Cited by 124 · see citing works
Immunohistochemical screening for β6‐integrin subunit expression in adenocarcinomas using a novel monoclonal antibody reveals strong up‐regulation in pancreatic ductal adenocarcinomas in vivo and in vitro
Sipos, B., Hahn, D., Carceller, A., Piulats, J., Hedderich, J., Kalthoff, H., Goodman, S. L., Kosmahl, M., & Klöppel, G. (2004) · Histopathology · doi:10.1111/j.1365-2559.2004.01919.x · Cited by 124 · see citing works
Human monocytes and macrophages regulate immune tolerance via integrin αvβ8–mediated TGFβ activation
Kelly, A., Gunaltay, S., McEntee, C. P., Shuttleworth, E. E., Smedley, C., Houston, S. A., Fenton, T. M., Levison, S., Mann, E. R., & Travis, M. A. (2018) · Journal of Experimental Medicine · doi:10.1084/jem.20171491 · Cited by 124 · see citing works
Expression of αvβ8 integrin on dendritic cells regulates Th17 cell development and experimental autoimmune encephalomyelitis in mice
Melton, A. C., Bailey-Bucktrout, S. L., Travis, M. A., Fife, B. T., Bluestone, J. A., & Sheppard, D. (2010) · Journal of Clinical Investigation · doi:10.1172/jci43786 · Cited by 123 · see citing works
TGF-beta receptor 2 downregulation in tumour-associated stroma worsens prognosis and high-grade tumours show more tumour-associated macrophages and lower TGF-beta1 expression in colon carcinoma: a retrospective study
Bacman, D., Merkel, S., Croner, R. S., Papadopoulos, T., Brueckl, W. M., & Dimmler, A. W. (2007) · BMC Cancer · doi:10.1186/1471-2407-7-156 · Cited by 118 · see citing works
Transforming growth factor beta 1 suppresses genomic instability independent of a G1 arrest, p53, and Rb.
Glick, A. B., Weinberg, W. C., Wu, I. H., Quan, W., & Yuspa, S. H. (1996) · PubMed · Cited by 117 · see citing works
β 1 Integrin Inhibition Elicits a Prometastatic Switch Through the TGFβ–miR-200–ZEB Network in E-Cadherin–Positive Triple-Negative Breast Cancer
Truong, H. H., Xiong, J., Ghotra, V. P. S., Nirmala, E., Haazen, L. C. J. M., Dévédec, S. E. L., Balcioglu, H. E., He, S., Snaar-Jagalska, E. B., Vreugdenhil, E., et al. (2014) · Science Signaling · doi:10.1126/scisignal.2004751 · Cited by 115 · see citing works
The integrin αvβ6 drives pancreatic cancer through diverse mechanisms and represents an effective target for therapy
Reader, C. S., Vallath, S., Steele, C. W., Haider, S., Brentnall, A. R., Desai, A., Moore, K. M., Jamieson, N. B., Chang, D. K.-F., Bailey, P. J., et al. (2019) · The Journal of Pathology · doi:10.1002/path.5320 · Cited by 115 · see citing works
Self-citation
Blocking immunosuppression by human Tregs in vivo with antibodies targeting integrin αVβ8
Stockis, J., Liénart, S., Colau, D., Collignon, A., Nishimura, S. L., Sheppard, D., Coulie, P. G., & Lucas, S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1710680114 · Cited by 111 · see citing works
Biological Significance of Local TGF-β Activation in Liver Diseases
Hayashi, H., & Sakai, T. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00012 · Cited by 110 · see citing works
Release of Active TGF-β1 from the Latent TGF-β1/GARP Complex on T Regulatory Cells Is Mediated by Integrin β8
Edwards, J. P., Thornton, A. M., & Shevach, E. M. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1401102 · Cited by 99 · see citing works
TGF-β and αvβ6 Integrin Act in a Common Pathway to Suppress Pancreatic Cancer Progression
Hezel, A. F., Deshpande, V., Zimmerman, S. M., Contino, G., Alagesan, B., O’Dell, M. R., Rivera, L. B., Harper, J. W., Lonning, S. M., Brekken, R. A., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-0634 · Cited by 99 · see citing works
Three Key Residues Underlie the Differential Affinity of the TGFβ Isoforms for the TGFβ Type II Receptor
Crescenzo, G. D., Hinck, C. S., Shu, Z., Zúñiga, J. E., Yang, J., Tang, Y., Baardsnes, J., Mendoza, V., Sun, L., López‐Casillas, F., et al. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.10.022 · Cited by 90 · see citing works
Altered Microenvironment Promotes Progression of Preinvasive Breast Cancer: Myoepithelial Expression of αvβ6 Integrin in DCIS Identifies High-risk Patients and Predicts Recurrence
Allen, M. D., Thomas, G. J., Clark, S. J., Dawoud, M. M., Vallath, S., Payne, S. J., Gomm, J. J., Dreger, S. A., Dickinson, S., Edwards, D. R., et al. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-1504 · Cited by 90 · see citing works
Self-citation
A role for the integrin alphavbeta8 in the negative regulation of epithelial cell growth.
Cambier, S., Mu, D., O'Connell, D., Boylen, K., Travis, W. D., Liu, W. H., Broaddus, V. C., & Nishimura, S. L. (2000) · PubMed · Cited by 90 · see citing works
VEGF and inhibitors of TGFβ type-I receptor kinase synergistically promote blood-vessel formation by inducing α5-integrin expression
Liu, Z., Kobayashi, K., van Dinther, M., van Heiningen, S. H., Valdimarsdóttir, G., van Laar, T., Scharpfenecker, M., Löwik, C. W. G. M., Goumans, M., ten Dijke, P., et al. (2009) · Journal of Cell Science · doi:10.1242/jcs.048942 · Cited by 89 · see citing works
Cilengitide in newly diagnosed glioblastoma: biomarker expression and outcome
Weller, M., Nabors, B., Gorlia, T., Leske, H., Rushing, E. J., Bady, P., Hicking, C., Perry, J., Hong, Y.-K., Roth, P., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.7588 · Cited by 89 · see citing works
A human monoclonal antibody 264RAD targeting αvβ6 integrin reduces tumour growth and metastasis, and modulates key biomarkers in vivo
Eberlein, C. A., Kendrew, J., McDaid, K., Alfred, A., Kang, J., Jacobs, V. N., Ross, S. J., Rooney, C., Smith, N. R., Rinkenberger, J. L., et al. (2012) · Oncogene · doi:10.1038/onc.2012.460 · Cited by 87 · see citing works
Self-citation
Suprabasal α6β4 integrin expression in epidermis results in enhanced tumourigenesis and disruption of TGFβ signalling
Owens, D. M., Romero, M. R., Gardner, C., & Watt, F. M. (2003) · Journal of Cell Science · doi:10.1242/jcs.00725 · Cited by 87 · see citing works
Suppression of TGFβand Angiogenesis by Type VII Collagen in Cutaneous SCC
Martins, V., Caley, M. P., Moore, K. M., Szentpétery, Z., Marsh, S., Murrell, D. F., Kim, M. H., Avari, M., McGrath, J. A., Cerio, R., et al. (2015) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djv293 · Cited by 86 · see citing works
Self-citation
Intestinal epithelial cell-derived integrin αβ6 plays an important role in the induction of regulatory T cells and inhibits an antigen-specific Th2 response
Chen, X., Song, C., Feng, B.-S., Li, T., Li, P., Zheng, P.-Y., Chen, X., Xing, Z., & Yang, P.-C. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.1210696 · Cited by 83 · see citing works
αvβ6 Integrin Promotes the Invasion of Morphoeic Basal Cell Carcinoma through Stromal Modulation
Marsh, D. J., Dickinson, S., Neill, G. W., Marshall, J. F., Hart, I. R., & Thomas, G. J. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0174 · Cited by 81 · see citing works
Self-citation
Epithelial–Mesenchymal Interactions in Fibrosis and Repair. Transforming Growth Factor-β Activation by Epithelial Cells and Fibroblasts
Sheppard, D. (2015) · Annals of the American Thoracic Society · doi:10.1513/annalsats.201406-245mg · Cited by 81 · see citing works
Connexins and Integrins in Exosomes
Shimaoka, M., Kawamoto, E., Gaowa, A., Okamoto, T., & Park, E. J. (2019) · Cancers · doi:10.3390/cancers11010106 · Cited by 81 · see citing works
Activation of the Mitogen-Activated Protein Kinase Pathway by Transforming Growth Factor-β
Yue, J., & Mulder, K. M. (2003) · Humana Press eBooks · doi:10.1385/1-59259-053-5:125 · Cited by 77 · see citing works
The dual adverse effects of TGF-β secretion on tumor progression
Trapani, J. A. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.10.018 · Cited by 77 · see citing works
Exosome-mediated transfer from the tumor microenvironment increases TGFβ signaling in squamous cell carcinoma.
Languino, L. R., Singh, A., di Prisco, M., Inman, G. J., Luginbuhl, A., Curry, J., & South, A. P. (2016) · PubMed Central · Cited by 74 · see citing works
Role of TGF-β in breast cancer bone metastases
Chiechi, A., Waning, D. L., Stayrook, K. R., Buijs, J. T., Guise, T. A., & Mohammad, K. S. (2013) · Advances in Bioscience and Biotechnology · doi:10.4236/abb.2013.410a4003 · Cited by 73 · see citing works
Exosomal αvβ6 integrin is required for monocyte M2 polarization in prostate cancer
Lu, H., Bowler, N., Harshyne, L. A., Hooper, D. C., Krishn, S. R., Kurtoglu, S., Fedele, C., Liu, Q., Tang, H., Kossenkov, A. V., et al. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.03.009 · Cited by 73 · see citing works
MAP-kinase activity necessary for TGFβ1-stimulated mesangial cell type I collagen expression requires adhesion-dependent phosphorylation of FAK tyrosine 397
Hayashida, T., Wu, M.-H., Pierce, A. A., Poncelet, A.-C., Varga, J., & Schnaper, H. W. (2007) · Journal of Cell Science · doi:10.1242/jcs.03492 · Cited by 70 · see citing works
Exosomal regulation of lymphocyte homing to the gut
Park, E. J., Prajuabjinda, O., Soe, Z. Y., Darkwah, S. O., Appiah, M. G., Kawamoto, E., Momose, F., Shiku, H., & Shimaoka, M. (2018) · Blood Advances · doi:10.1182/bloodadvances.2018024877 · Cited by 69 · see citing works
Integrin αvβ6 Promotes an Osteolytic Program in Cancer Cells by Upregulating MMP2
Dutta, A., Li, J., Lu, H., Akech, J., Pratap, J., Wang, T., Zerlanko, B. J., FitzGerald, T. J., Jiang, Z., Birbe, R., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-1796 · Cited by 68 · see citing works
Tgfb1 expressed in the Tgfb3 locus partially rescues the cleft palate phenotype of Tgfb3 null mutants
Yang, L., & Kaartinen, V. (2007) · Developmental Biology · doi:10.1016/j.ydbio.2007.09.034 · Cited by 67 · see citing works
Hydrogel Micropillars with Integrin Selective Peptidomimetic Functionalized Nanopatterned Tops: A New Tool for the Measurement of Cell Traction Forces Transmitted through αvβ3‐ or α5β1‐Integrins
Rahmouni, S., Lindner, A., Rechenmacher, F., Neubauer, S., Sobahi, T. R., Kessler, H., Cavalcanti‐Adam, E. A., & Spatz, J. P. (2013) · Advanced Materials · doi:10.1002/adma.201301338 · Cited by 64 · see citing works
Binding Affinity of Transforming Growth Factor-β for Its Type II Receptor Is Determined by the C-terminal Region of the Molecule
Qian, S. W., Burmester, J. K., Tsang, M., Weatherbee, J. A., Hinck, A. P., Ohlsen, D. J., Sporn, M. B., & Roberts, A. B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.48.30656 · Cited by 63 · see citing works
E-Cadherin and EpCAM expression by NSCLC tumour cells associate with normal fibroblast activation through a pathway initiated by integrin αvβ6 and maintained through TGFβ signalling
Eberlein, C. A., Rooney, C., Ross, S. J., Farren, M. R., Weir, H. M., & Barry, S. T. (2014) · Oncogene · doi:10.1038/onc.2013.600 · Cited by 60 · see citing works
Characterization of integrin ?6 and thrombospondin-1 double-null mice
Ludlow, A., Yee, K. O., Lipman, R. D., Bronson, R. T., Weinreb, P. H., Huang, X., Sheppard, D., & Lawler, J. (2005) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2005.tb00367.x · Cited by 59 · see citing works
Role of GARP in the activation of latent TGF-β1
Stockis, J., Dedobbeleer, O., & Lucas, S. (2017) · Molecular BioSystems · doi:10.1039/c7mb00251c · Cited by 59 · see citing works
Dissecting the role of TGF-beta type I receptor/ALK5 in pancreatic ductal adenocarcinoma: Smad activation is crucial for both the tumor suppressive and prometastatic function
Schniewind, B., Groth, S., Müerköster, S. S., Sipos, B., Schäfer, H., Kalthoff, H., Fändrich, F., & Ungefroren, H. (2007) · Oncogene · doi:10.1038/sj.onc.1210272 · Cited by 58 · see citing works
Integrin α3β1 Potentiates TGFβ-Mediated Induction of MMP-9 in Immortalized Keratinocytes
Lamar, J. M., Iyer, V., & DiPersio, C. M. (2007) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5701042 · Cited by 48 · see citing works
Integrin signaling potentiates transforming growth factor-beta 1 (TGF-β1) dependent down-regulation of E-Cadherin expression – Important implications for epithelial to mesenchymal transition (EMT) in renal cell carcinoma
Feldkoren, B., Hutchinson, R., Rapoport, Y., Mahajan, A., & Margulis, V. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.03.051 · Cited by 46 · see citing works
A mosaic mouse model of astrocytoma identifies αvβ8 integrin as a negative regulator of tumor angiogenesis
Tchaicha, J. H., Mobley, A. K., Hossain, M. G., Aldape, K., & McCarty, J. H. (2010) · Oncogene · doi:10.1038/onc.2010.199 · Cited by 40 · see citing works
Activation of the mitogen-activated protein kinase pathway by transforming growth factor-beta.
Yue, J., & Mulder, K. (2000) · The HKU Scholars Hub (University of Hong Kong) · Cited by 29 · see citing works
αvβ6 integrin is required for TGFβ1-mediated matrix metalloproteinase2 expression
Dutta, A., Li, J., Fedele, C., Sayeed, A., Singh, A., Violette, S. M., Manes, T. D., & Languino, L. R. (2015) · Biochemical Journal · doi:10.1042/bj20140698 · Cited by 28 · see citing works
Glycoprotein A repetitions predominant (GARP) positively regulates transforming growth factor (TGF) β3 and is essential for mouse palatogenesis
Wu, B. X., Li, A., Lei, L., Kaneko, S., Wallace, C. H., Li, X., & Li, Z. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.797613 · Cited by 24 · see citing works

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TGFβ biology in cancer progression and immunotherapy
Derynck, R., Turley, S. J., & Akhurst, R. J. (2021) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-020-0403-1 · Cited by 944 · see citing works
Emerging 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
TGF-β1 – A truly transforming growth factor in fibrosis and immunity
Lodyga, M., & Hinz, B. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.12.010 · Cited by 462 · see citing works
Targeting TGFβ signal transduction for cancer therapy
Liu, S., Ren, J., & ten Dijke, P. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00436-9 · Cited by 413 · see citing works
“Previous studies showed that genetically and pharmacologically inhibition of αvβ integrin can inhibit TGFβ signaling and suppress metastasis.(201,203) For example, the cyclic RGD pentapeptide cilengitide (EMD121974) is a potent and selective inhibitor of integrin αvβ3/5 that showed a reduction of TGFβ1 and TGFβ2 messe…”
Background
Overcoming TGFβ-mediated immune evasion in cancer
Tauriello, D. V. F., Sancho, E., & Batlle, E. (2022) · Nature Reviews Cancer · doi:10.1038/s41568-021-00413-6 · Cited by 377 · see citing works
TGF ‐β as a driver of fibrosis: physiological roles and therapeutic opportunities
Budi, E. H., Schaub, J. R., Decaris, M. L., Turner, S., & Derynck, R. (2021) · The Journal of Pathology · doi:10.1002/path.5680 · Cited by 300 · see citing works
Roles of cancer-associated fibroblasts (CAFs) in anti- PD-1/PD-L1 immunotherapy for solid cancers
Pei, L., Liu, Y., Liu, L., Gao, S., Gao, X., Feng, Y., Sun, Z., Zhang, Y., & Wang, C. (2023) · Molecular Cancer · doi:10.1186/s12943-023-01731-z · Cited by 265 · see citing works
The Pathogenesis of Cardiac Fibrosis: A Review of Recent Progress
Maruyama, K., & Imanaka‐Yoshida, K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052617 · Cited by 216 · see citing works
TGF-beta signal transduction: biology, function and therapy for diseases
Tie, Y., Tang, F., Peng, D., Zhang, Y., & Shi, H. (2022) · Molecular Biomedicine · doi:10.1186/s43556-022-00109-9 · Cited by 178 · see citing works
The transformation of cancer-associated fibroblasts: Current perspectives on the role of TGF-β in CAF mediated tumor progression and therapeutic resistance
Jena, B. C., Sarkar, S., Rout, L., & Mandal, M. (2021) · Cancer Letters · doi:10.1016/j.canlet.2021.08.002 · Cited by 137 · see citing works
Spatially exploring RNA biology in archival formalin-fixed paraffin-embedded tissues
Bai, Z., Zhang, D., Gao, Y. P., Tao, B., Zhang, D., Bao, S., Enninful, A., Wang, Y., Li, H., Su, G., et al. (2024) · Cell · doi:10.1016/j.cell.2024.09.001 · Cited by 118 · see citing works
PET/CT imaging of head-and-neck and pancreatic cancer in humans by targeting the “Cancer Integrin” αvβ6 with Ga-68-Trivehexin
Quigley, N. G., Steiger, K., Hoberück, S., Czech, N., Zierke, M. A., Kossatz, S., Pretze, M., Richter, F., Weichert, W., Pox, C. P., et al. (2021) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-021-05559-x · Cited by 87 · see citing works
Adhesion, metastasis, and inhibition of cancer cells: a comprehensive review
Yayan, J., Franke, K.-J., Berger, M. P., Windisch, W., & Rasche, K. (2024) · Molecular Biology Reports · doi:10.1007/s11033-023-08920-5 · Cited by 85 · see citing works
Transforming growth factor-β receptors: versatile mechanisms of ligand activation
Chia, Z. J., Cao, Y.-N., Little, P. J., & Kamato, D. (2024) · Acta Pharmacologica Sinica · doi:10.1038/s41401-024-01235-6 · Cited by 92 · see citing works
Integrin-αV-mediated activation of TGF-β regulates anti-tumour CD8 T cell immunity and response to PD-1 blockade
Malenica, I., Adam, J., Corgnac, S., Mezquita, L., Auclin, É., Damei, I., Grynszpan, L., Gros, G., de Montpréville, V., Planchard, D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25322-y · Cited by 72 · see citing works
Integrin Crosstalk Contributes to the Complexity of Signalling and Unpredictable Cancer Cell Fates
Samaržija, I., Dekanić, A., Humphries, J. D., Paradžik, M., Stojanović, N., Humphries, M. J., & Ambriović‐Ristov, A. (2020) · Cancers · doi:10.3390/cancers12071910 · Cited by 64 · see citing works
Can’t handle the stress? Mechanobiology and disease
Zuela-Sopilniak, N., & Lammerding, J. (2022) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2022.05.010 · Cited by 59 · see citing works
Inhibition of integrin αvβ6 sparks T-cell antitumor response and enhances immune checkpoint blockade therapy in colorectal cancer
Busenhart, P., Montalban‐Arques, A., Katkeviciutė, E., Morsy, Y., Passen, C. V., Hering, L., Atrott, K., Lang, S., Garzon, J. F. G., Naschberger, E., et al. (2022) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2021-003465 · Cited by 58 · see citing works
Transforming Growth Factor-β: An Agent of Change in the Tumor Microenvironment
Stuelten, C. H., & Zhang, Y. E. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.764727 · Cited by 57 · see citing works
Mechanosensitive Regulation of Fibrosis
Yang, S., & Plotnikov, S. V. (2021) · Cells · doi:10.3390/cells10050994 · Cited by 56 · see citing works
The Bright and the Dark Side of TGF-β Signaling in Hepatocellular Carcinoma: Mechanisms, Dysregulation, and Therapeutic Implications
Gungor, M. Z., Uysal, M., & Şentürk, Ş. (2022) · Cancers · doi:10.3390/cancers14040940 · Cited by 51 · see citing works
Integrin alpha V (ITGAV) expression in esophageal adenocarcinoma is associated with shortened overall-survival
Loeser, H., Scholz, M., Fuchs, H. F., Essakly, A., Damanakis, A. I., Zander, T., Büttner, R., Schröder, W., Bruns, C. J., Quaas, A., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-75085-7 · Cited by 49 · see citing works
Prostate cancer bone metastases biology and clinical management (Review)
Goode, E. A., Wang, N., & Munkley, J. (2023) · Oncology Letters · doi:10.3892/ol.2023.13749 · Cited by 49 · see citing works
There is a world beyond αvβ3-integrin: Multimeric ligands for imaging of the integrin subtypes αvβ6, αvβ8, αvβ3, and α5β1 by positron emission tomography
Steiger, K., Quigley, N. G., Groll, T., Richter, F., Zierke, M. A., Beer, A. J., Weichert, W., Schwaiger, M., Kossatz, S., & Notni, J. (2021) · EJNMMI Research · doi:10.1186/s13550-021-00842-2 · Cited by 46 · see citing works
Hyaluronan, Transforming Growth Factor β, and Extra Domain A-Fibronectin: A Fibrotic Triad
McKeown‐Longo, P. J., & Higgins, P. J. (2020) · Advances in Wound Care · doi:10.1089/wound.2020.1192 · Cited by 42 · see citing works
Osteosarcoma Cells Secrete CXCL14 That Activates Integrin α11β1 on Fibroblasts to Form a Lung Metastatic Niche
Xu, Y., Deng, C., Chen, H., Song, Y., Xu, H., Song, G., Wang, X., Luo, T., Chen, W., Ma, J., et al. (2024) · Cancer Research · doi:10.1158/0008-5472.can-23-1307 · Cited by 41 · see citing works
Click‐Chemistry (CuAAC) Trimerization of an αvβ6 Integrin Targeting Ga‐68‐Peptide: Enhanced Contrast for in‐Vivo PET Imaging of Human Lung Adenocarcinoma Xenografts
Quigley, N. G., Tomassi, S., Leva, F. S. D., Maro, S. D., Richter, F., Steiger, K., Kossatz, S., Marinelli, L., & Notni, J. (2020) · ChemBioChem · doi:10.1002/cbic.202000200 · Cited by 38 · see citing works
Overexpression of TGF-β1 induces renal fibrosis and accelerates the decline in kidney function in polycystic kidney disease
Zhang, Y., Dai, Y., Raman, A., Daniel, E. A., Metcalf, J., Reif, G. A., Pierucci‐Alves, F., & Wallace, D. P. (2020) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00366.2020 · Cited by 37 · see citing works
Mesenchymal cells in the Lung: Evolving concepts and their role in fibrosis
Ligresti, G., Raslan, A., Hong, J., Caporarello, N., Confalonieri, M., & Huang, S. K. (2023) · Gene · doi:10.1016/j.gene.2022.147142 · Cited by 34 · see citing works
Mechanotransduction and the extracellular matrix: Key drivers of lung pathologies and drug responsiveness
Burgess, J. K., & Gosens, R. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116255 · Cited by 34 · see citing works
Alkaline activation of endogenous latent TGFβ1 by an injectable hydrogel directs cell homing for in situ complex tissue regeneration
Wang, S., Niu, Y., Jia, P., Liao, Z.-T., Guo, W., Chaves, R. C., Tran‐Ba, K., He, L., Bai, H., Sia, S., et al. (2021) · Bioactive Materials · doi:10.1016/j.bioactmat.2021.12.015 · Cited by 32 · see citing works
FAM83H overexpression predicts worse prognosis and correlates with less CD8+ T cells infiltration and Ras-PI3K-Akt-mTOR signaling pathway in pancreatic cancer
Zhuang, H., Zhang, C., & Hou, B. (2020) · Clinical & Translational Oncology · doi:10.1007/s12094-020-02365-z · Cited by 31 · see citing works
Role of αVβ3 in Prostate Cancer: Metastasis Initiator and Important Therapeutic Target
Tang, L., Xu, M. Q., Zhang, L., Qu, L., & Liu, X. (2020) · OncoTargets and Therapy · doi:10.2147/ott.s258252 · Cited by 31 · see citing works
It’s Time to Shift the Paradigm: Translation and Clinical Application of Non-αvβ3 Integrin Targeting Radiopharmaceuticals
Kossatz, S., Beer, A. J., & Notni, J. (2021) · Cancers · doi:10.3390/cancers13235958 · Cited by 27 · see citing works
In silico transcriptomic mapping of integrins and immune activation in Basal-like and HER2+ breast cancer
Rojas, K., Baliu‐Piqué, M., Manzano, A., Sáiz-Ladera, C., García‐Barberán, V., Cimas, F. J., Pérez‐Segura, P., Pandiella, A., Győrffy, B., & Ocaña, A. (2021) · Cellular Oncology · doi:10.1007/s13402-020-00583-9 · Cited by 26 · see citing works
Advances in Immunotherapy and the TGF-β Resistance Pathway in Metastatic Bladder Cancer
Benjamin, D. J., & Lyou, Y. (2021) · Cancers · doi:10.3390/cancers13225724 · Cited by 26 · see citing works
Wnt5A and TGFβ1 Converges through YAP1 Activity and Integrin Alpha v Up-Regulation Promoting Epithelial to Mesenchymal Transition in Ovarian Cancer Cells and Mesothelial Cell Activation
Dehghani‐Ghobadi, Z., Hasani, S. S., Arefian, E., & Hossein, G. (2022) · Cells · doi:10.3390/cells11020237 · Cited by 25 · see citing works
Focusing on Mechanoregulation Axis in Fibrosis: Sensing, Transduction and Effecting
Wen, D., Gao, Y., Ho, C., Li, Y., Zhang, Y., Lyu, G., Hu, D., Li, Q., & Zhang, Y. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.804680 · Cited by 22 · see citing works
A ternary composite hydrogel based on sodium alginate, carboxymethyl cellulose and copper-doped 58S bioactive glass promotes cutaneous wound healing in vitro and in vivo
Kohoolat, G., Alizadeh, P., Zarandi, F. M., & Rezaeipour, Y. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.129260 · Cited by 22 · see citing works
Integrin αvβ8 serves as a Novel Marker of Poor Prognosis in Colon Carcinoma and Regulates Cell Invasiveness through the Activation of TGF-β1
Zhou, M., Niu, J., Wang, J., Gao, H., Shahbaz, M., Niu, Z., Li, Z., Zou, X., & Liang, B. (2020) · Journal of Cancer · doi:10.7150/jca.43826 · Cited by 21 · see citing works
Tracking a TGF-β activator in vivo: sensitive PET imaging of αvβ8-integrin with the Ga-68-labeled cyclic RGD octapeptide trimer Ga-68-Triveoctin
Quigley, N. G., Steiger, K., Richter, F., Weichert, W., Hoberück, S., Kotzerke, J., & Notni, J. (2020) · EJNMMI Research · doi:10.1186/s13550-020-00706-1 · Cited by 21 · see citing works
The crosstalk between circular RNAs and the tumor microenvironment in cancer metastasis
Shao, Y., & Lü, B. (2020) · Cancer Cell International · doi:10.1186/s12935-020-01532-0 · Cited by 20 · see citing works
Exosomal ITGB6 from dormant lung adenocarcinoma cells activates cancer-associated fibroblasts by KLF10 positive feedback loop and the TGF-β pathway
Xiang, F., Liu, X., Xiang, J., Xu, J., Yin, N., Wang, L., Liu, C., Liu, Y., Zhao, T., Zhao, Z., et al. (2023) · Translational Lung Cancer Research · doi:10.21037/tlcr-23-707 · Cited by 19 · see citing works
Integrins and integrin-driven secretory pathways as multi-dimensional regulators of tumor-associated macrophage recruitment and reprogramming in tumor microenvironment
Dalpati, N., Rai, S. K., Sharma, P., & Sarangi, P. P. (2024) · Matrix Biology · doi:10.1016/j.matbio.2024.12.003 · Cited by 17 · see citing works
Exosomal regulation of cellular reprogramming and polarization in the tumor microenvironment
Bayat, M., Shahabi, P., Rezaei, T., & Nahand, J. S. (2025) · Cancer Cell International · doi:10.1186/s12935-025-04105-1 · Cited by 17 · see citing works
Prognostic and Predictive Value of Cadherin 11 for Patients with Gastric Cancer and Its Correlation with Tumor Microenvironment: Results from Microarray Analysis
Feng, Z., Li, X., Ren, Z., Feng, J., He, X., & You, C. (2020) · BioMed Research International · doi:10.1155/2020/8107478 · Cited by 17 · see citing works
Integrin α2β1 Represents a Prognostic and Predictive Biomarker in Primary Ovarian Cancer
Dötzer, K., Schlüter, F., von Koch, F. E., Brambs, C., Anthuber, S., Frangini, S., Czogalla, B., Burges, A., Werner, J., Mahner, S., et al. (2021) · Biomedicines · doi:10.3390/biomedicines9030289 · Cited by 15 · see citing works
Activated fibroblasts in cardiac and cancer fibrosis: An overview of analogies and new potential therapeutic options
Nicolini, G., Balzan, S., & Forini, F. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121575 · Cited by 18 · see citing works
CSK-mediated signalling by integrins in cancer
Maldonado, H., & Leyton, L. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1214787 · Cited by 13 · see citing works
Development of a low-seroprevalence, αvβ6 integrin-selective virotherapy based on human adenovirus type 10
Bates, E. A., Davies, J. A., Váňová, J., Nestić, D., Méniel, V. S., Koushyar, S., Cunliffe, T. G., Mundy, R. M., Moses, E., Uusi-Kerttula, H. K., et al. (2022) · Molecular Therapy — Oncolytics · doi:10.1016/j.omto.2022.03.007 · Cited by 13 · see citing works
Integrins in cancer stem cells
Gou, S., Wu, A., & Luo, Z. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1434378 · Cited by 12 · see citing works
Integrin signaling in tumor biology: mechanisms of intercellular crosstalk and emerging targeted therapies
Li, Y., Peng, S., Xu, J., Liu, W., & Luo, Q. (2025) · PeerJ · doi:10.7717/peerj.19328 · Cited by 12 · see citing works
Interstitial lung disease following coronavirus disease 2019
Vasarmidi, E., Ghanem, M., & Crestani, B. (2022) · Current Opinion in Pulmonary Medicine · doi:10.1097/mcp.0000000000000900 · Cited by 12 · see citing works
GTF2IRD1 overexpression promotes tumor progression and correlates with less CD8+ T cells infiltration in pancreatic cancer
Zhuang, H., Zhang, C., & Hou, B. (2020) · Bioscience Reports · doi:10.1042/bsr20202150 · Cited by 12 · see citing works
Machine learning with imaging features to predict the expression of ITGAV, which is a poor prognostic factor derived from transcriptome analysis in pancreatic cancer
Iwatate, Y., Yokota, H., Hoshino, I., Ishige, F., Kuwayama, N., Itami, M., Mori, Y., Chiba, S., Arimitsu, H., Yanagibashi, H., et al. (2022) · International Journal of Oncology · doi:10.3892/ijo.2022.5350 · Cited by 11 · see citing works
Integrative Models for TGF-β Signaling and Extracellular Matrix
Théret, N., Ferêt, J., Hodgkinson, A., Boutillier, P., Vignet, P., & Radulescu, O. (2020) · Biology of extracellular matrix · doi:10.1007/978-3-030-58330-9_10 · Cited by 11 · see citing works
Integrin ανβ6 Protein Expression and Prognosis in Solid Tumors: A Meta-Analysis
Desnoyers, A., González, C., Pérez‐Segura, P., Pandiella, A., Amir, E., & Ocaña, A. (2020) · Molecular Diagnosis & Therapy · doi:10.1007/s40291-020-00450-1 · Cited by 11 · see citing works
Lipopolysaccharide acting via toll-like receptor 4 transactivates the TGF-β receptor in vascular smooth muscle cells
Afroz, R., Kumarapperuma, H., Nguyen, Q. V. N., Mohamed, R., Little, P. J., & Kamato, D. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04159-8 · Cited by 11 · see citing works
Nintedanib-Containing Dual Conjugates Targeting αVβ6 Integrin and Tyrosine Kinase Receptors as Potential Antifibrotic Agents
Bugatti, K., Andreucci, E., Monaco, N., Battistini, L., Peppicelli, S., Ruzzolini, J., Curti, C., Zanardi, F., Bianchini, F., & Sartori, A. M. (2022) · ACS Omega · doi:10.1021/acsomega.2c00535 · Cited by 10 · see citing works
Cell type-specific transforming growth factor-β (TGF-β) signaling in the regulation of salivary gland fibrosis and regeneration
Forti, K. M., Weisman, G. A., & Jasmer, K. J. (2024) · Journal of Oral Biology and Craniofacial Research · doi:10.1016/j.jobcr.2024.03.005 · Cited by 9 · see citing works
High beta integrin expression is differentially associated with worsened pancreatic ductal adenocarcinoma outcomes.
Benesch, M. G. K., Wu, R., Menon, G., & Takabe, K. (2022) · PubMed Central · Cited by 9 · see citing works
Altered biopterin-related cofactor metabolism in the aqueous humor of glaucoma patients
Zemītis, A., Caikovska, L., Vanags, J., Fan, J., Klavins, K., & Laganovska, G. (2025) · Experimental Eye Research · doi:10.1016/j.exer.2025.110778 · Cited by 8 · see citing works
Multifaceted Role of the Transforming Growth Factor β on Effector T Cells and the Implication for CAR-T Cell Therapy
de Folmont, A. D. T., Bourhis, J.-H., Chouaı̈b, S., & Terry, S. (2021) · Immuno · doi:10.3390/immuno1030010 · Cited by 8 · see citing works
Identification, molecular evolution, and expression analysis of the transcription factor Smad gene family in lamprey
Zhong, Z., Wu, T., Zhu, T., Pang, Y., Li, Q., & Su, P. (2021) · Molecular Immunology · doi:10.1016/j.molimm.2021.06.004 · Cited by 8 · see citing works
Overcoming Immune Checkpoint Inhibitor Resistance with Potent, Selective Dual αvβ6/8 Inhibitors Based on Engineered Lasso Peptides
Lechner, A., Jordan, P. A., da Cruz, G. C. M., Lamson, J. S., Gordon, J., Okada, B. K., Anderson, K., Chaudhari, R. R., Rosario, C. J., Mikesell, J., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c06142 · Cited by 9 · see citing works
ALDH1A3–Linc00284 Axis Mediates the Invasion of Colorectal Cancer by Targeting TGFβ Signaling via Sponging miR-361-5p
Ke, C., Shen, M., Wang, P., Chen, Z., Lin, S., & Dong, F. (2022) · International Journal of Genomics · doi:10.1155/2022/6561047 · Cited by 7 · see citing works
Mycobacterium tuberculosis-induced monocyte transcriptional responses associated with resistance to tuberculin skin test/interferon-γ release assay conversion in people with HIV
Hong, H., Dill‐McFarland, K. A., Benson, B., Simmons, J. D., Peterson, G. J., Benchek, P. H., Stein, C. M., Boom, W. H., Mayanja‐Kizza, H., & Hawn, T. R. (2023) · AIDS · doi:10.1097/qad.0000000000003716 · Cited by 7 · see citing works
Shared mechanisms for metastasis and drug resistance in prostate cancer
Chen, Y., Chen, L., Xu, Y., Cheng, H., & Zhou, J. (2025) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2025.189358 · Cited by 6 · see citing works
The Role of αvβ3 Integrin in Lamina Cribrosa Cell Mechanotransduction in Glaucoma
Irnaten, M., Gaynor, E., & O'Brien, C. J. (2024) · Cells · doi:10.3390/cells13171487 · Cited by 6 · see citing works
What Is the Fuss about Integrins and the Tumor Microenvironment?
Eble, J. A., & Gullberg, D. (2019) · Cancers · doi:10.3390/cancers11091296 · Cited by 6 · see citing works
The immunoregulatory role of integrins in pulmonary diseases
Xu, Q., Yang, C., Li, W., Qian, W., Chen, S., & Yang, L. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1716118 · Cited by 5 · see citing works
Selective blockade of latent TGF-β1 activation suppresses tissue fibrosis with good safety
Kanamori, M., Sato, I., Koo, C. X., Sun, Y., Kawauchi, H., Nakagawa, K., Murai, A., Asanuma, K., Gan, S. W., Pang, C. L., et al. (2026) · Communications Medicine · doi:10.1038/s43856-026-01408-w · Cited by 5 · see citing works
RGD Density on Tadpole Nanostructures Regulates Cancer Stem Cell Proliferation and Stemness
Zhang, D., Sun, B. F., Wang, J., Chen, S. R., Bobrin, V. A., Gu, Y., Ng, C. K., Gu, W., & Monteiro, M. J. (2024) · Biomacromolecules · doi:10.1021/acs.biomac.4c00645 · Cited by 4 · see citing works
Pan-cancer characterization of cellular senescence reveals its inter-tumor heterogeneity associated with the tumor microenvironment and prognosis
Li, K., Guo, C., Li, R., Yao, Y., Qiang, M., Chen, Y., Tu, K., & Xu, Y. (2024) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2024.109196 · Cited by 4 · see citing works
The Combination of Oncolytic Virus and Antibody Blockade of TGF-β Enhances the Efficacy of αvβ6-Targeting CAR T Cells Against Pancreatic Cancer in an Immunocompetent Model
Zhao, Z., Cutmore, L. C., Baleeiro, R. B., Hartlebury, J., Brown, N. F., Chard, L. S., Lemoine, N. R., Wang, Y., & Marshall, J. F. (2025) · Cancers · doi:10.3390/cancers17091534 · Cited by 6 · see citing works
Self-citation
Macrophage regulation of tumor cell dormancy and the dormant niche: an overview in solid tumors
Zhang, H., Ding, Y., Gu, L., Guo, A., Duan, W., Wang, X., & Zhang, B. (2025) · Cancer and Metastasis Reviews · doi:10.1007/s10555-025-10280-4 · Cited by 4 · see citing works
Fully-automated production of [68Ga]Ga-Trivehexin for clinical application and its biodistribution in healthy volunteers
Wang, B., Jiang, Y., Zhu, J., Wu, H., Wu, J., Li, L., Huang, J., Xiao, Z., & He, Y. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1445415 · Cited by 4 · see citing works
Development and bioevaluation of 18F-labeled bivalent cyclic peptides for PET imaging of αvβ6 integrin overexpression
Ye, S., Shi, D., Li, X., Yang, Y., Pan, X., Wang, L., & Wu, H. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.108362 · Cited by 4 · see citing works
Magnesium Supplementation: Effect on the Expression of Inflammation Genes in Erlich's Tumor
Draghi, P. F., Fernandes, J. C. B., Petri, G., da Silva, E. B., Perez, M. M., da Veiga, G. L., Alves, B. D. C. A., & Fonseca, F. L. A. (2021) · Journal of Dietary Supplements · doi:10.1080/19390211.2021.1897056 · Cited by 4 · see citing works
Collagen-disrupting attIL12 TIL therapy boosts deep T cell infiltration via dual signaling activation and CCKAR reduction in sarcomas
Hu, J., Singh, H., Jin, Y., Zhang, W., Wang, J., Xia, X., Somaiah, N., Gorlick, R. G., & Li, S. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2507542122 · Cited by 4 · see citing works
PET/CT imaging of esophageal cancer targeting tumor cell specific αvβ6-integrin expression
Bendová, K. D., Groll, T., Neužilová, B., Krasulová, K., Nový, Z., Reissig, F., Steiger, K., Boxberg, M., Eppard, E., Wuestemann, J., et al. (2025) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-025-07408-7 · Cited by 4 · see citing works
Transforming Growth Factor‐Beta Signaling in Cancer: Therapeutic Implications, Challenges, and Pathways to Progress
Alabi, F. A., Okpalanwaka, I. F., Oyegbesan, A., Okoyeocha, E. O. M., Oladejo, M., & Imodoye, S. O. (2025) · MedComm – Oncology · doi:10.1002/mog2.70027 · Cited by 3 · see citing works
Functional Peptides in Targeted Cancer Therapy: Mechanisms, Delivery Strategies, and Clinical Perspectives
Wu, Y. F., Maki, M. A. A., Mani, V., Rajagopal, M. S., & Kumar, P. V. (2025) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-025-10748-5 · Cited by 3 · see citing works
Effect of lathyrol derivatives on non-small cell lung cancer and the possible mechanism.
Yan, Y., Zhou, W., Guo, Q., Zhang, H., Ji, H., Yang, L., & Zhang, J. (2022) · PubMed Central · doi:10.11817/j.issn.1672-7347.2022.210104 · Cited by 3 · see citing works
αvβ3 Integrin as a Link between the Development of Fibrosis and Thyroid Hormones in Systemic Sclerosis
Kohon, M. Y., Levy, M. Z., Hornik‐Lurie, T., Shalom, A., Berl, A., Drucker, L., Levy, Y. M., & Matalon, S. T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24108927 · Cited by 3 · see citing works
Targeting αvβ8 Integrin with mAb MEDI8367 Prevents Fibrosis in Preclinical Models of CKD
Marin, E. L., Seth, A., Liang, L., Baker, D., Conway, J., McCarthy, M., Lapointe, J., Stebbings, R., Hebeis, B. J., Hess, S. Y., et al. (2025) · Kidney360 · doi:10.34067/kid.0000001006 · Cited by 2 · see citing works
ICAM-1⁺CD51⁺ CAFs drive immunosuppression in colorectal cancer via OPN-triggered chemokine secretion
Liu, J., Xue, S., Xu, Y., Wu, S., Zhao, W., Li, X. G., Hu, N., 孙晋敏, & Ren, J. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-08642-9 · Cited by 2 · see citing works
Integrins in Cancer: Refocusing on the Tumor Microenvironment
Zeltz, C., Lü, N., Heljäsvaara, R., & Gullberg, D. (2022) · Biology of extracellular matrix · doi:10.1007/978-3-030-99708-3_11 · Cited by 2 · see citing works
The prognostic significance and potential mechanism of DBF4 zinc finger in hepatocellular carcinoma
Wu, Z., Zhang, L., Li, X., Liu, L., Kuang, T., Qiu, Z., Deng, W., & Wang, W. (2024) · Scientific Reports · doi:10.1038/s41598-024-60342-w · Cited by 2 · see citing works
Adhesion, Metastasis, and Inhibitor for Cancer CellsPreprint
Yayan, J., Franke, K.-J., Berger, M. P., Windisch, W., & Rasche, K. (2023) · Preprints.org · doi:10.20944/preprints202308.0651.v1 · Cited by 1 · see citing works
The double-edged sword of regulatory T cells in MASLD: from inflammation control to fibrosis promotion
Lee, S. E., Jo, M. G., Park, S. W., Kim, H. J., Yun, S. P., & Kim, J.-W. (2026) · Animal Cells and Systems · doi:10.1080/19768354.2026.2630463 · Cited by 2 · see citing works
“Therefore, blockade of integrin αvβ8 decreased active TGF-β levels in the livers of mice and attenuated fibrosis, underscoring the role of the ATF4–integrin αvβ8 axis in Treg-mediated fibrogenesis (Brown and Marshall 2019; Wang et al. 2025).”
TGF-β1 and its signal molecules: are they correlated with the elasticity characteristics of breast lesions?
Zhang, M. K., Wang, B., Li, S. Y., Liu, G., & Wang, Z. (2021) · BMC Cancer · doi:10.1186/s12885-021-09036-4 · Cited by 1 · see citing works
Transcriptome analysis of chicken fibroblast following transforming growth factor β1-mediated activation
Hou, T., Zhang, L., Zhao, L., Gao, F., & Xing, T. (2025) · Poultry Science · doi:10.1016/j.psj.2025.105576 · Cited by 2 · see citing works
Transforming growth factor-β and integrins: key players in EMT and breast cancer progression
Ramalingam, P. S., Afzal, M., Mirle, R. M., Sahoo, S., Pandey, S. N., Maji, C., Goyal, K., Ali, H., Singh, S. K., Gupta, G., et al. (2026) · Cancer Cell International · doi:10.1186/s12935-026-04196-4 · Cited by 1 · see citing works
Enhanced antitumor efficacy of combined targeting of adenosine A2B receptor and PD-1 is mediated via multiple effects on different cell populations within tumor microenvironment
Guan, S., Wang, C., Amann, J. M., Cho, J. H., Ma, Q., & Carbone, D. P. (2026) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-026-04330-1 · Cited by 1 · see citing works
A structural bioinformatics framework for prioritizing pH-sensitive proteins from 3D structural features
Arsanjani, A. A., Malekshahi, Z. V., Mosayyebi, B., Negahdari, B., Amirlou, M., Khavari, F., & Faradonbeh, D. R. (2026) · BMC Bioinformatics · doi:10.1186/s12859-026-06415-1 · Cited by 1 · see citing works
Collagen remodeling in breast cancer progression: from molecular mechanisms to diagnostic and therapeutic opportunities
Mohammad-Rezaei, M., Shafaghat, Z., Noroozbeygi, M., Velu, P., Safaee, M., Heiranizadeh, N., & Safari, E. (2026) · Clinical & Translational Oncology · doi:10.1007/s12094-026-04450-1 · Cited by 1 · see citing works
Unveiling the therapeutic potential: KBU2046 halts triple-negative breast cancer cell migration by constricting TGF-β1 activation in vitro
CHEN, J., Dai, S., Zhang, G., WEI, S., ZHAO, X., Yang, Z., WANG, Y., WANG, X., LIU, Y., & ZHAO, L. (2024) · Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics · doi:10.32604/or.2024.049348 · Cited by 1 · see citing works
Integrin β5-positive cancer-associated fibroblasts promoting lung adenocarcinoma invasion leading to poor prognosis
Shibata, S., Inoue, C., Miki, Y., Notsuda, H., Niikawa, H., Okada, Y., & SUZUKI, T. A. (2025) · Pathology - Research and Practice · doi:10.1016/j.prp.2025.156215 · Cited by 1 · see citing works
Signaling pathways in cardiac fibrosis; A review and future therapeutic options
Elsayed, M. O. K., Moustafa, Y. M., Mehanna, E. T., El-Sayed, N. M., & Hazem, R. M. (2023) · Records of Pharmaceutical and Biomedical Sciences/Records of Pharmaceutical & Biomedical Sciences · doi:10.21608/rpbs.2023.238923.1244 · Cited by 1 · see citing works

αv Integrin-Dependent TGFβ Activation in Cancer: A Brief Update
Marshall, J. F., Protopapa, P., & Allen, N. E. (2023) · Biology of extracellular matrix · doi:10.1007/978-3-031-23781-2_6
Self-citation
The 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
Self-citation
647 Selective targeting of integrins a v b 8 and a v b 1 improves anti-tumor responses mediated by immune checkpoint inhibition
Rajabian, N., Fousek, K., Angstadt, S. M., Horn, L. A., Qin, H., Medina-Enríquez, M. M., Hsiao-Sanchez, N., Kelly, M. D., Finkelstein, D. S., Machajewski, T. D., et al. (2025) · Regular and Young Investigator Award Abstracts · doi:10.1136/jitc-2025-sitc2025.0647
TGFβ biology in cancer progression and immunotherapy
Derynck, R., Turley, S. J., & Akhurst, R. J. (2021) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-020-0403-1 · Cited by 944 · see citing works
Overcoming TGFβ-mediated immune evasion in cancer
Tauriello, D. V. F., Sancho, E., & Batlle, E. (2022) · Nature Reviews Cancer · doi:10.1038/s41568-021-00413-6 · Cited by 377 · see citing works

Authors: Brown, N. F., & Marshall, J. F.
Affiliations: Queen Mary University of London (GB)
Corresponding author: Marshall, John F.
ORCID: Brown, Nicholas F.
Marshall, John F.
Venue: Cancers
Publisher: MDPI AG
Published: 2019-08-21
Volume: 11
Issue: 9
Pages: 1221
ISSN: 2072-6694 (ISSN-L)
DOI: 10.3390/cancers11091221
PMC: PMC6769837
OpenAlex: W2969253527
Cited by: 116
References: 192
Citations by year: 2026: 13 · 2025: 17 · 2024: 18 · 2023: 11 · 2022: 16 · 2021: 23 · 2020: 16 · 2019: 2
FWCI: 1.26
Type: journal article
Language: en
Open access: gold
dx.doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Cancers (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Queen Mary Research Online (Queen Mary University of London) (submittedVersion, cc-by)
Funders: Cancer Research UK (S_3565)
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
Health Sciences › Medicine › Oncology › Cancer Immunotherapy and Biomarkers
Keywords: integrins, ITGAV, tumor microenvironment, TGF-beta signaling, immunosuppression, immune checkpoint inhibitors, cancer-associated fibroblasts, epithelial-mesenchymal transition, angiogenesis

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Integrin-Mediated TGFβ Activation Modulates the Tumour Microenvironment

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