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

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

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

DOI 10.1083/jcb.109.6.3137PMC PMC2115961

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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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Additional file 7 of Glycosaminoglycan modifications of betaglycan regulate ectodomain shedding to fine-tune TGF-β signaling responses in ovarian cancer
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Additional file 8 of Glycosaminoglycan modifications of betaglycan regulate ectodomain shedding to fine-tune TGF-β signaling responses in ovarian cancer
Choi, A. S., Jenkins, L. M., Barton, W., Kumari, A., Lancaster, C. L., Raulerson, C., Ji, H., Altomare, D., Starr, M. D., Whitaker, R., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26681170
Additional file 1 of Glycosaminoglycan modifications of betaglycan regulate ectodomain shedding to fine-tune TGF-β signaling responses in ovarian cancer
Choi, A. S., Jenkins, L. M., Barton, W., Kumari, A., Lancaster, C. L., Raulerson, C., Ji, H., Altomare, D., Starr, M. D., Whitaker, R., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25231271
Additional file 2 of Glycosaminoglycan modifications of betaglycan regulate ectodomain shedding to fine-tune TGF-β signaling responses in ovarian cancer
Choi, A. S., Jenkins, L. M., Barton, W., Kumari, A., Lancaster, C. L., Raulerson, C., Ji, H., Altomare, D., Starr, M. D., Whitaker, R., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25231346
Additional file 3 of Glycosaminoglycan modifications of betaglycan regulate ectodomain shedding to fine-tune TGF-β signaling responses in ovarian cancer
Choi, A. S., Jenkins, L. M., Barton, W., Kumari, A., Lancaster, C. L., Raulerson, C., Ji, H., Altomare, D., Starr, M. D., Whitaker, R., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26681155
Additional file 5 of Glycosaminoglycan modifications of betaglycan regulate ectodomain shedding to fine-tune TGF-β signaling responses in ovarian cancer
Choi, A. S., Jenkins, L. M., Barton, W., Kumari, A., Lancaster, C. L., Raulerson, C., Ji, H., Altomare, D., Starr, M. D., Whitaker, R., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26681161
Additional file 6 of Glycosaminoglycan modifications of betaglycan regulate ectodomain shedding to fine-tune TGF-β signaling responses in ovarian cancer
Choi, A. S., Jenkins, L. M., Barton, W., Kumari, A., Lancaster, C. L., Raulerson, C., Ji, H., Altomare, D., Starr, M. D., Whitaker, R., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26681164
Additional file 4 of Glycosaminoglycan modifications of betaglycan regulate ectodomain shedding to fine-tune TGF-β signaling responses in ovarian cancer
Choi, A. S., Jenkins, L. M., Barton, W., Kumari, A., Lancaster, C. L., Raulerson, C., Ji, H., Altomare, D., Starr, M. D., Whitaker, R., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26681158
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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
DOI: 10.1083/jcb.109.6.3137
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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Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-beta.

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