Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-beta.
Open accessAbstract
Transforming growth factors beta 1 and beta 2 bind with high affinity to the core protein of a 250-350-kD cell surface proteoglycan. This proteoglycan (formerly referred to as the type III TGF-beta receptor) coexists in many cells with the receptor implicated in TGF-beta signal transduction (type I TGF-beta receptor), but its function is not known. We report here that soluble TGF-beta-binding proteoglycans are released by several cell types into the culture media, and can be found in serum and extracellular matrices. As has been shown for the membrane-bound form, the soluble proteoglycans have a heterogeneous core protein of 100-120 kD that carries chondroitin sulfate and/or heparan sulfate glycosaminoglycan chains and a small amount of N-linked carbohydrate. The membrane-bound form of this proteoglycan is hydrophobic and associates with liposomes, whereas the soluble forms lack a membrane anchor and do not associate with liposomes. Differences in the electrophoretic migration of the soluble and membrane forms of this proteoglycan suggest additional structural differences in their core proteins and glycosaminoglycan chains. These soluble and membrane-bound proteoglycans, for which we propose the name "betaglycans," might play distinct roles in pericellular retention, delivery, or clearance of activated TGF-beta.
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TGFβR3 may act as a reservoir for TGFβ ligand, establishing a signaling environment for later in development.
“here TGFβR3 may act as a reservoir for TGFβ ligand, establishing a signaling environment for later in development”
From Single-Cell Transcriptomics Reveals Early Emergence of Liver Parenchymal and Non-parenchymal Cell Lineages (2020) · cites this paper as Andres et al., 1989
The paper proposes that betaglycan might help retain and deliver activated TGFβ locally (opening summary, p. 3137; discussion). That supports the hedged reservoir idea, but the paper does not connect this role to establishing a signaling environment for later in development. (LLM, conf=0.85)
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- Authors
- Andres, J. L., Stanley, K., Cheifetz, S., & Massagué, J.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- ORCID
- Massagué, J
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1989-12-01
- Volume
- 109
- Issue
- 6
- Pages
- 3137-3145
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2115961
- OpenAlex
- W2117901334
- Cited by
- 354
- References
- 35
- Citations by year
- 2026: 1 · 2024: 13 · 2023: 6 · 2022: 4 · 2021: 6 · 2020: 2 · 2019: 2 · 2018: 3 · 2017: 6 · 2016: 1 · 2015: 2 · 2014: 6 · 2013: 4 · 2012: 2
- FWCI
- 14.39
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (CA34610)
- National Cancer Institute (CA34610)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- betaglycan, TGF-beta type I receptor, chondroitin sulfate, heparan sulfate, glycosaminoglycan chains, extracellular matrix
- MeSH terms
- Animals, Cell Line, Cell Membrane, Cells, Cultured, Chromatography, Affinity, Chromatography, Ion Exchange, Cytosol, Humans, Kinetics, Liposomes, Molecular Weight, Protein Binding, Proteoglycans, Transforming Growth Factors
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