The DOI matches its Crossref record; 213 of the 213 references it cites were found in a registry or an index.
Regulation of the Bioavailability of TGF-β and TGF-β-Related Proteins
Open accessAbstract
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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“Mice lacking the αvβ6 integrin are protected in mouse models of lung, kidney and biliary fibrosis90,98–102”
From Fibrosis: from mechanisms to medicines (2020) · cites this paper as [101]
In the citing paper
“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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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
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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
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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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