The DOI matches its Crossref record; 221 of the 221 references it cites were found in a registry or an index.
TGF‐β as a driver of fibrosis: physiological roles and therapeutic opportunities
Abstract
Many chronic diseases are marked by fibrosis, which is defined by an abundance of activated fibroblasts and excessive deposition of extracellular matrix, resulting in loss of normal function of the affected organs. The initiation and progression of fibrosis are elaborated by pro‐fibrotic cytokines, the most critical of which is transforming growth factor‐β1 (TGF‐β1). This review focuses on the fibrogenic roles of increased TGF‐β activities and underlying signaling mechanisms in the activated fibroblast population and other cell types that contribute to progression of fibrosis. Insight into these roles and mechanisms of TGF‐β as a universal driver of fibrosis has stimulated the development of therapeutic interventions to attenuate fibrosis progression, based on interference with TGF‐β signaling. Their promise in preclinical and clinical settings will be discussed. © 2021 The Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.
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Items 201–221 of 221
Inhibition of the p38 MAPK pathway ameliorates renal fibrosis in an NPHP2 mouse model
Sugiyama, N., Kohno, M., & Yokoyama, T. (2011) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfr550 · Cited by 62
Role of Receptor Tyrosine Kinase Signaling in Renal Fibrosis
Liu, F., & Zhuang, S. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17060972 · Cited by 58
Greco, R., Qu, H., Qu, H., Theilhaber, J., Shapiro, G., Gregory, R. C., Winter, C. G., Malkova, N. V., Sun, F. F., Jaworski, J. A., et al. (2020) · OncoImmunology · doi:10.1080/2162402x.2020.1811605 · Cited by 58
Inhibition of p38 MAPK attenuates renal atrophy and fibrosis in a murine renal artery stenosis model
Wang, D., Warner, G. M., Yin, P., et al. (2013) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00706.2012 · Cited by 55
Origin of Myofibroblasts in Lung Fibrosis
Hung, C. (2020) · Current Tissue Microenvironment Reports · doi:10.1007/s43152-020-00022-9 · Cited by 55
Han, Q., Lin, L., Zhao, B., Wang, N., & Liu, X. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.04.148 · Cited by 44
Bedinger, D., Lao, L., Khan, S., Lee, S., Takeuchi, T., & Mirza, A. M. (2016) · mAbs · doi:10.1080/19420862.2015.1115166 · Cited by 42 · cited 1×
“Among these, fresolimumab (1D11) [171] and SAR439459 [172] neutralize all three TGF-β homodimers, whereas NIS793 neutralizes TGF-β 1 and TGF-β 2 but not TGF-β 3 [173].”
BackgroundEW‐7197 prevents ulcerative colitis‐associated fibrosis and inflammation
Binabaj, M. M., Asgharzadeh, F., Avan, A., Rahmani, F., Soleimani, A., Parizadeh, M. R., Ferns, G. A., Ryzhikov, M., Khazaei, M., & Hassanian, S. M. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27823 · Cited by 42
Liver Fibrosis and Inflammation under the Control of ERK2
Jeng, K., Lu, S.-J., Wang, C.-H., & Chang, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113796 · Cited by 39
Rictor/mammalian target of rapamycin complex 2 promotes macrophage activation and kidney fibrosis
Ren, J., Li, J., Ye, F., Shu, B., Gui, Y., Wei, W., He, W., Yang, J., & Dai, C. (2017) · The Journal of Pathology · doi:10.1002/path.4921 · Cited by 36
Roubin, R., Pizette, S., Ollendorff, V., Planche, J., Birnbaum, D., & deLapeyrière, O. (1996) · The International Journal of Developmental Biology · doi:10.1387/ijdb.8840187 · Cited by 33
Ma, W., Qin, Y., Chapuy, B., & Lu, C. (2019) · PLoS ONE · doi:10.1371/journal.pone.0213482 · Cited by 30
Evidence for Activation of the TGF-β1 Promoter by C/EBPβ and Its Modulation by Smads
Abraham, S., Sweet, T., Khalili, K., Sawaya, B., & Amini, S. (2009) · Journal of Interferon and Cytokine Research · doi:10.1089/jir.2008.0036 · Cited by 27
Liang, X., Schnaper, H. W., Matsusaka, T., Pastan, I. H., Ledbetter, S., & Hayashida, T. (2016) · PLoS ONE · doi:10.1371/journal.pone.0155534 · Cited by 26
Inhibition of TGFβ1 and TGFβ3 promotes hematopoiesis in Fanconi anemia
Rodríguez, A., Yang, C., Furutani, E., Teresa, B. G., Velázquez, M., Filiatrault, J., Sambel, L. A., Phan, T., Flores-Guzmán, P., Sánchez, S., et al. (2020) · Experimental Hematology · doi:10.1016/j.exphem.2020.11.002 · Cited by 26
Huang, X., Cai, H., Ammar, R., Zhang, Y., Wang, Y., Ravi, K., Thompson, J. R., & Járai, G. (2018) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00281.2018 · Cited by 25
P. Hinck, A., & D. O'Connor-McCourt, M. (2011) · Current Pharmaceutical Biotechnology · doi:10.2174/138920111798808383 · Cited by 21 · cited 1×
“These comprise dimers of TβRII ectodomains (Fc-stabilized) that are designed to sequester TGF-β1 and TGF-β3, but not TGF-β2, and thus prevent them binding to receptors [174,175].”
BackgroundEngineering and Therapeutic Application of Single-Chain Bivalent TGF-β Family Traps
Zwaagstra, J. C., Sulea, T., Baardsnes, J., Lenferink, A. E. G., Collins, C., Cantin, C., Paul-Roc, B., Grothe, S., Hossain, S., Richer, L.-P., et al. (2012) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-12-0060 · Cited by 20
Myh11+ microvascular mural cells and derived mesenchymal stem cells promote retinal fibrosis
Ray, H. C., Corliss, B. A., Bruce, A. C., Kesting, S., Dey, P., Mansour, J., Seaman, S. A., Smolko, C. M., Mathews, C., Dey, B. K., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-72875-x · Cited by 14
Jung, S. Y., Park, J.-H., Baek, M., Kim, G.-H., Kim, J., Zheng, H.-M., Kim, J., Kang, I.-M., Kim, D., & Lee, J. I. (2020) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2020.119103 · Cited by 9
Phase 2B dose selection of BG00011 for the treatment of idiopathic pulmonary fibrosis (IPF)
Arefayene, M., Mouded, M., Stebbins, C., Zhao, G., Song, G., Christmann, R., Violette, S. M., & Gallagher, D. C. (2018) · European Respiratory Journal · doi:10.1183/13993003.congress-2018.pa596 · Cited by 5
Cited by
Immune cell dysregulation as a mediator of fibrosis in systemic sclerosis
Fang, D., Chen, B., Lescoat, A., Khanna, D., & Mu, R. (2022) · Nature Reviews Rheumatology · doi:10.1038/s41584-022-00864-7 · Cited by 84
Reininger, D., Fundel‐Clemens, K., Mayr, C. H., Wollin, L., Laemmle, B., Quast, K., Nickolaus, P., & Herrmann, F. E. (2024) · British Journal of Pharmacology · doi:10.1111/bph.17303 · Cited by 48
“Its increased signalling not only affects the activated fibroblast population but also influences other cell types that actively contribute to the progression of IPF (Budi et al., 2021).”
Inhibition of TGFβ1 activation prevents radiation-induced lung fibrosis
Yi, M., Yuan, Y., Ma, L., Li, L., Qin, W., Wu, B., Zheng, B., Liao, X., Hu, G., & Liu, B. (2024) · Clinical and Translational Medicine · doi:10.1002/ctm2.1546 · Cited by 33
Control of fibrosis with enhanced safety via asymmetric inhibition of prolyl‐tRNA synthetase 1
Yoon, I., Kim, S., Cho, M., You, K. A., Son, J., Lee, C., Suh, J. H., Bae, D., Kim, J. M., Oh, S., et al. (2023) · EMBO Molecular Medicine · doi:10.15252/emmm.202216940 · Cited by 22
Haga, M., Iida, K., & Okada, M. (2024) · iScience · doi:10.1016/j.isci.2024.109708 · Cited by 19
Metadata
- Authors
- Budi, E. H., Schaub, J. R., Decaris, M., Turner, S., & Derynck, R.
- Venue
- The Journal of Pathology
- Publisher
- Wiley
- Published
- 2021-05-19
- Volume
- 254
- Issue
- 4
- Pages
- 358-373
- ISSN
- 0022-3417 (ISSN-L)
- 1096-9896
- OpenAlex
- W3149662796
- Cited by
- 292
- References
- 221
- FWCI
- 10.87
- Type
- journal article
- Language
- en
- Open access
- closed
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