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Regulation of the Bioavailability of TGF-β and TGF-β-Related Proteins
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The bioavailability of members of the transforming growth factor β (TGF-β) family is controlled by a number of mechanisms. Bona fide TGF-β is sequestered into the matrix in a latent state and must be activated before it can bind to its receptors. Here, we review the molecules and mechanisms that regulate the bioavailability of TGF-β and compare these mechanisms with those used to regulate other TGF-β family members. We also assess the physiological significance of various latent TGF-β activators, as well as other extracellular modulators of TGF-β family signaling, by examining the available in vivo data from knockout mouse models and other biological systems.
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“CAFs support tumor growth and progression through secreted or membrane-associated signals that benefit the carcinoma cells, and deposition of extracellular matrix (ECM) proteins, which confer instructive signals, and retain and thus store secreted chemokines and cytokines, including TGF-β40,43.”
From TGFβ biology in cancer progression and immunotherapy (2021) · cites this paper as [43]
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“Latent complexes of the TGF-β1 homodimer, often have one of the dimeric pro-segments covalently linked to a fibrillin-like latent TGF-β binding protein 1 (LTBP1) that enables their deposition in the ECM43 (Figure 2B). Secretion of such complexes does not result in release of soluble active TGF-β, but in localized deposition of inactive complexes in proximity to TGF-β expressing cells. As a con”
From TGFβ biology in cancer progression and immunotherapy (2021) · cites this paper as [43]
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1 retracted
Attur, M. G., Palmer, G. D., Al-Mussawir, H., Dave, M. N., Teixeira, C. C., Rifkin, D. B., Appleton, C. T., Beier, F., & Abramson, S. B. (2008) · The FASEB Journal · doi:10.1096/fj.08-114363 · Cited by 61
Self-citationRetractedRegulation of skeletal muscle mass in mice by a new TGF-p superfamily member
McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1997) · Nature · doi:10.1038/387083a0 · Cited by 4,013
Bone Resorption by Osteoclasts
Teitelbaum, S. L. (2000) · Science · doi:10.1126/science.289.5484.1504 · Cited by 3,962
TGF-β signaling and the fibrotic response
Leask, A., & Abraham, D. J. (2004) · The FASEB Journal · doi:10.1096/fj.03-1273rev · Cited by 2,319
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
Self-citationKulkarni, 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
Yu, Q., & Stamenkovic, I. (2000) · PubMed · Cited by 1,952
Losartan, an AT1 Antagonist, Prevents Aortic Aneurysm in a Mouse Model of Marfan Syndrome
Habashi, J. P., Judge, D. P., Holm, T. M., Cohn, R. D., Loeys, B. L., Cooper, T. K., Myers, L., Klein, E. C., Liu, G., Calvi, C., et al. (2006) · Science · doi:10.1126/science.1124287 · Cited by 1,794
Self-citationYu, Q., & Stamenkovic, I. (2000) · Genes & Development · doi:10.1101/gad.14.2.163 · Cited by 1,754
Making sense of latent TGFβ activation
Annes, J. P., Munger, J. S., & Rifkin, D. B. (2002) · Journal of Cell Science · doi:10.1242/jcs.00229 · Cited by 1,624
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Sato, R., Imamura, K., Semba, T., Tomita, Y., Saeki, S., Ikeda, K., Komohara, Y., Suzuki, M., Sakagami, T., Saya, H., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-3941 · Cited by 59
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Li, J., Chen, F., Peng, Y., Lv, Z., Lin, X., Chen, Z., & Wang, H. (2020) · Cells · doi:10.3390/cells9020296 · Cited by 59
Miller, S. M., Cybulski, V., Whitacre, M., Bess, L. S., Livesay, M. T., Walsh, L. M., Burkhart, D. J., Bazin, H. G., & Evans, J. T. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00406 · Cited by 58
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The role of TGF-β2 in cartilage development and diseases
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Zi, Z. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.05.022 · Cited by 55
Akasaka, E., Kleiser, S., Sengle, G., Bruckner‐Tuderman, L., & Nyström, A. (2020) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2020.10.024 · Cited by 56
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Melchionna, R., Trono, P., Tocci, A., & Nisticò, P. (2021) · Biomolecules · doi:10.3390/biom11020336 · Cited by 60
André, P., Joshi, S. R., Briscoe, S. D., Alexander, M. J., Li, G., & Kumar, R. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2021.814222 · Cited by 53
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Shihan, M. H., Kanwar, M., Wang, Y., Jackson, E., Faranda, A. P., & Duncan, M. K. (2020) · Matrix Biology · doi:10.1016/j.matbio.2020.02.004 · Cited by 54
Metadata
- Authors
- Robertson, I. B., & Rifkin, D. B.
- Affiliations
- New York University (US)
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2016-06
- Volume
- 8
- Issue
- 6
- Pages
- a021907
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC4888822
- OpenAlex
- W2414680576
- Cited by
- 403
- References
- 212
- Citations by year
- 2026: 33 · 2025: 33 · 2024: 35 · 2023: 46 · 2022: 71 · 2021: 55 · 2020: 48 · 2019: 30 · 2018: 30 · 2017: 20 · 2016: 2
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (AR49698)
- National Cancer Institute (R01CA034282)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (P01AR049698)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Health Sciences › Medicine › Hepatology › Liver physiology and pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- TGF-beta, TGF-beta superfamily, latent TGF-beta, extracellular matrix, knockout mouse models, TGF-beta receptor
- MeSH terms
- Fibrillins, Protein Domains, Animals, Biological Availability, Carrier Proteins, Extracellular Matrix, Glycosylation, Humans, Phylogeny, Signal Transduction, Transforming Growth Factor beta, Mice, Knockout, Mice, Latent TGF-beta Binding Proteins, Protein Multimerization
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