Evidence map›Paper›PMID 1379245›Full record

ArticleThe Journal of cell biology1992

Repression of myogenic differentiation by aFGF, bFGF, and K-FGF is dependent on cellular heparan sulfate.

B B Olwin, A Rapraeger

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed, 1 pooled it
8.3field-weighted citation impact, top 2% of its field
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

58 citing papers in PubMed, 1 synthesis or guideline pooled it, 237 citations in OpenAlex.

  1. Pooled it
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  4. Review
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  7. Review
  8. Article
  9. Heparan Sulfate Proteoglycans: Key Mediators of Stem Cell Function.Frontiers in cell and developmental biology · 2020
    Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
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  20. Review
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

2 authors at 1 institution in 1 country.

B B OlwinDepartment of Biochemistry, School of Medicine, University of Wisconsin, Madison 53706.
A Rapraeger
University of Wisconsin–Madison · US

Funding

MYOGENIC GRWOTH AND DIFFERENTIATIONR01AR039467 · NIAMS · UNIVERSITY OF COLORADO AT BOULDER · PI OLWIN, BRADLEY B · 1994 to 2008
$2.8M
PROTEOGLYCANS OF THE PLASMA MEMBRANER01HD021881 · NICHD · UNIVERSITY OF WISCONSIN MADISON · PI RAPRAEGER, ALAN C · 1986 to 2003
$899k
PROTEOGLYCANS OF THE PLASMA MEMBRANER23HD021881 · NICHD · UNIVERSITY OF WISCONSIN MADISON · PI RAPRAEGER, ALAN C · 1985 to 1985
–
ANALYSIS OF MYOGENIC GROWTH AND DIFFERENTIATIONR29AR039467 · NIAMS · UNIVERSITY OF WISCONSIN MADISON · PI OLWIN, BRADLEY B · 1988 to 1992
–
NIAMS NIH HHS AR39467NICHD NIH HHS HD21881
6 · The paper itself

Abstract

We have proposed a model in which fibroblast growth factor (FGF) signalling requires the interaction of FGF with at least two FGF receptors, a heparan sulfate proteoglycan (HSPG) and a tyrosine kinase. Since FGF may be a key mediator of skeletal muscle differentiation, we examined the synthesis of glycosaminoglycans in MM14 skeletal muscle myoblasts and their participation in FGF signalling. Proliferating and differentiated MM14 cells exhibit similar levels of HSPG, while differentiated cells exhibit reduced levels of chondroitin sulfate proteoglycans and heparan sulfate chains. HSPGs, including syndecan, present in proliferating cells bind bFGF, while the majority of chondroitin sulfate and heparan sulfate chains do not. Treatment of skeletal muscle cells with chlorate, a reversible inhibitor of glycosaminoglycan sulfation, was used to examine the requirement of sulfated proteoglycans for FGF signalling. Chlorate treatment reduced glycosaminoglycan sulfation by 90% and binding of FGF to high affinity sites by 80%. Chlorate treatment of MM14 myoblasts abrogated the biological activity of acidic, basic, and Kaposi's sarcoma FGFs resulting in terminal differentiation. Chlorate inhibition of FGF signalling was reversed by the simultaneous addition of sodium sulfate or heparin. Further support for a direct role of heparan sulfate proteoglycans in fibroblast growth factor signal transduction was demonstrated by the ability of heparitinase to inhibit basic FGF binding and biological activity. These results suggest that activation of FGF receptors by acidic, basic or Kaposi's sarcoma FGF requires simultaneous binding to a HSPG and the tyrosine kinase receptor. Skeletal muscle differentiation in vivo may be dependent on FGFs, FGF tyrosine kinase receptors, and HSPGs. The regulation of these molecules may then be expected to have important implications for skeletal muscle development and regeneration.

Indexed as

Fibroblast Growth FactorsAnimalsCattleCell DifferentiationCell LineChloratesFibroblast Growth Factor 1Fibroblast Growth Factor 2Fibroblast Growth Factor 4GlycosaminoglycansHeparan SulfateHeparinHumansMusclesPolysaccharide-LyasesProtein BindingChloratesFGF4 protein, humanFibroblast Growth Factor 1Fibroblast Growth Factor 2Fibroblast Growth Factor 4Fibroblast Growth FactorsGlycosaminoglycansHeparan SulfateHeparinheparitinsulfate lyasePolysaccharide-LyasesProto-Oncogene ProteinsSulfates

Identifiers

PMID1379245
PMCPMC2289538
OpenAlexW2104239648

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.