Evidence map›Paper›PMID 8093006›Full record

ArticleThe Biochemical journal1994

Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta.

A Hildebrand, M Romarís, L M Rasmussen, D Heinegård, D R Twardzik, W A Border, E Ruoslahti

Abstract read
In one paragraph

Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 358 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
358citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

358 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  13. Sex Differences in Response to Diet Enriched With Glutathione Precursors in the Aging Heart.The journals of gerontology. Series A, Biological sciences and medical sciences · 2025
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  14. Review
  15. An Update on Molecular Mechanisms of Scarring-A Narrative Review.International journal of molecular sciences · 2024
    Review
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298 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

A HildebrandCancer Research Center, La Jolla Cancer Research Foundation, CA 92037.
M Romarís
L M Rasmussen
D Heinegård
D R Twardzik
W A Border
E Ruoslahti

Funding

Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Michael Jackson · 1985 to 2026
$107.2M
REGULATION OF EXTRACELLULAR MATRIX IN KIDNEY DISEASER37DK043609 · NIDDK · UNIVERSITY OF UTAH · PI BORDER, WAYNE A. · 1999 to 2008
$4.2M
REGULATION OF EXTRACELLULAR MATRIX IN KIDNEY DISEASER01DK043609 · NIDDK · UNIVERSITY OF UTAH · PI BORDER, WAYNE A. · 1990 to 1998
–
MOLECULAR MECHANISMS OF CELL ADHESIONR35CA042507 · NCI · BURNHAM INSTITUTE FOR MEDICAL RESEARCH · PI RUOSLAHTI, ERKKI I · 1986 to 1992
–
NCI NIH HHS NCI CA30199NCI NIH HHS NCI CA42507NIDDK NIH HHS NIDDK DK43609
6 · The paper itself

Abstract

We have analysed the interactions of three proteoglycans of the decorin family, decorin, biglycan and fibromodulin, with transforming growth factor beta (TGF-beta). The proteoglycan core proteins, expressed from human cDNAs as fusion proteins with Escherichia coli maltose-binding protein, each bound TGF-beta 1. They showed only negligible binding to several other growth factors. Intact decorin, biglycan and fibromodulin isolated from bovine tissues competed with the fusion proteins for the TGF-beta binding. Affinity measurements suggest a two-site binding model with Kd values ranging from 1 to 20 nM for a high-affinity binding site and 50 to 200 nM for the lower-affinity binding site. The stoichiometry indicated that the high-affinity binding site was present in one of ten proteoglycan core molecules and that each molecule contained a low-affinity binding site. Tissue-derived biglycan and decorin were less effective competitors for TGF-beta binding than fibromodulin or the non-glycosylated fusion proteins; removal of the chondroitin/dermatan sulphate chains of decorin and biglycan (fibromodulin is a keratan sulphate proteoglycan) increased the activities of decorin and biglycan, suggesting that the glycosaminoglycan chains may hinder the interaction of the core proteins with TGF-beta. The fusion proteins competed for the binding of radiolabelled TGF-beta to Mv 1 Lu cells and endothelial cells. Affinity labelling showed that the binding of TGF-beta to betaglycan and the type-I receptors in Mv 1 Lu cells and to endoglin in endothelial cells was reduced, but the binding to the type-II receptors was unaffected. TGF-beta 2 and 3 also bound to all three fusion proteins. Latent recombinant TGF-beta 1 precursor bound slightly to fibromodulin and not at all to decorin and biglycan. The results show that the three decorin-type proteoglycans each bind TGF-beta isoforms and that slight differences exist in their binding properties. They may regulate TGF-beta activities by sequestering TGF-beta into extracellular matrix.

Indexed as

Extracellular Matrix ProteinsBiglycanCarrier ProteinsCloning, MolecularCross-Linking ReagentsDecorinDNA, ComplementaryElectrophoresis, Polyacrylamide GelEscherichia coliFibromodulinHumansProtein BindingProteoglycansRecombinant Fusion ProteinsTransforming Growth Factor betaBGN protein, humanBiglycanCarrier ProteinsCross-Linking ReagentsDCN protein, humanDecorinDNA, ComplementaryExtracellular Matrix ProteinsFibromodulinFMOD protein, humanProteoglycansRecombinant Fusion ProteinsTransforming Growth Factor beta

Identifiers

PMID8093006
PMCPMC1137259

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.