Cited by 354Proteoglycans and glycosaminoglycans researchTGF-β signaling in diseasesProtease and Inhibitor Mechanisms

Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-beta.

Open access
Andres, J L, Stanley, K, Cheifetz, S, Massagué, J·1989·The Journal of cell biology

Abstract

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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Crossref · 10.1083/jcb.109.6.3137

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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)
Venue
The Journal of cell biology
Published
1989-12-01
Volume
109
Issue
6
Pages
3137-3145
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
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
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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