ArticleThe Journal of cell biology1993
A 60-kD protein mediates the binding of transforming growth factor-beta to cell surface and extracellular matrix proteoglycans.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 39 citations in OpenAlex.
- Article
- Collagen type IV and Perlecan exhibit dynamic localization in the Allantoic Core Domain, a putative stem cell niche in the murine allantois.Developmental dynamics : an official publication of the American Association of Anatomists · 2009Article
- Transforming growth factor beta depletion is the primary determinant of Smad signaling kinetics.Molecular and cellular biology · 2009Article
- Rapid up-regulation of alpha4 integrin-mediated leukocyte adhesion by transforming growth factor-beta1.Molecular biology of the cell · 2003Article
- Extracellular matrix and growth factors during heart growth.Heart failure reviews · 2000Review
- Basal lamina and other extracellular matrix produced by bovine granulosa cells in anchorage-independent culture.Cell and tissue research · 1995Article
- Localisation of extracellular matrix components in the embryonic human notochord and axial mesenchyme.Journal of anatomy · 1995Article
- Characterization of a human hepatoma cell line with acquired resistance to growth inhibition by transforming growth factor beta 1 (TGF-beta 1).In vitro cellular & developmental biology. Animal · 1995Article
- Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta.The Biochemical journal · 1994Article
- Plasmin cleaves betaglycan and releases a 60 kDa transforming growth factor-beta complex from the cell surface.The Biochemical journal · 1994Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The biological activity of many cytokines is regulated by binding proteins present at the cell surface, in extracellular matrices or in soluble phase. We describe here a TGF-beta binding protein that is both an extracellular matrix and a cell surface protein. When intact extracellular matrices of HEP-G2 cells were affinity cross-linked with 125I-TGF-beta 1, two major binding components were seen: a 250-kD, proteoglycan-like molecule, presumed to be betaglycan, and a 60-kD protein. The 60-kD TGF-beta-binding protein was also present at the cell surface. It could be released from the cell surface by treating cells with high salt, heparin, chondroitin sulfate, heparitinase, or chondroitinase, indicating that it is bound to heparan sulfate and chondroitin sulfate proteoglycans. The 60-kD protein bound TGF-beta 1 with an apparent dissociation constant of 1.6 nM, and there were 30,000 binding sites per cell at the cell surface. In addition to the HEP-G2 cells and another hepatoma cell line, the 60-kD protein was also found in a human colon carcinoma (HT-29) cell line but not in rat kidney (NRK-49F) or human fibroblast (HUT-12) cell lines. The 60-kD protein could be extracted from cells containing it and transferred to the surface of previously negative cells. The 60-kD protein may serve to regulate the binding of TGF-beta to its signal transducing receptors by targeting TGF-beta to appropriate locations in the microenvironment of cells.
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Registered trials
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