Evidence map›Paper›PMID 10684260›Full record

ArticleThe Journal of cell biology2000

The small leucine-rich repeat proteoglycan biglycan binds to alpha-dystroglycan and is upregulated in dystrophic muscle.

M A Bowe, D B Mendis, J R Fallon

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 149 citations in OpenAlex.

  1. Review
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  8. Skeletal muscle: A review of molecular structure and function, in health and disease.Wiley interdisciplinary reviews. Systems biology and medicine · 2020
    Review
  9. Non-Glycanated Biglycan and LTBP4: Leveraging the extracellular matrix for Duchenne Muscular Dystrophy therapeutics.Matrix biology : journal of the International Society for Matrix Biology · 2018
    Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Soluble biglycan as a biomarker of inflammatory renal diseases.The international journal of biochemistry & cell biology · 2014
    Review
  17. De novo expression of circulating biglycan evokes an innate inflammatory tissue response via MyD88/TRIF pathways.Matrix biology : journal of the International Society for Matrix Biology · 2014
    Article
  18. Review
  19. Article
  20. Article
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

3 authors at 1 institution in 1 country.

M A BoweDepartment of Neuroscience, Brown University, Providence, Rhode Island 02912, USA.
D B Mendis
J R Fallon
Brown University · US

Funding

NERVE-MUSCLE SYNAPSE-ORGANIZING MOLECULES IN DEVELOPMENTR01HD023924 · NICHD · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI FALLON, JUSTIN R · 1988 to 2005
$1.8M
NICHD NIH HHS HD23924NICHD NIH HHS R01 HD023924
6 · The paper itself

Abstract

The dystrophin-associated protein complex (DAPC) is necessary for maintaining the integrity of the muscle cell plasma membrane and may also play a role in coordinating signaling events at the cell surface. The alpha-/beta-dystroglycan subcomplex of the DAPC forms a critical link between the cytoskeleton and the extracellular matrix. A ligand blot overlay assay was used to search for novel dystroglycan binding partners in postsynaptic membranes from Torpedo electric organ. An approximately 125-kD dystroglycan-binding polypeptide was purified and shown by peptide microsequencing to be the Torpedo ortholog of the small leucine-rich repeat chondroitin sulfate proteoglycan biglycan. Biglycan binding to alpha-dystroglycan was confirmed by coimmunoprecipitation with both native and recombinant alpha-dystroglycan. The biglycan binding site was mapped to the COOH-terminal third of alpha-dystroglycan. Glycosylation of alpha-dystroglycan is not necessary for this interaction, but binding is dependent upon the chondroitin sulfate side chains of biglycan. In muscle, biglycan is detected at both synaptic and nonsynaptic regions. Finally, biglycan expression is elevated in muscle from the dystrophic mdx mouse. These findings reveal a novel binding partner for alpha-dystroglycan and demonstrate a novel avenue for interaction of the DAPC and the extracellular matrix. These results also raise the possibility of a role for biglycan in the pathogenesis, and perhaps the treatment, of muscular dystrophy.

Indexed as

Up-RegulationAmino Acid SequenceAnimalsBiglycanBinding SitesChondroitin SulfatesCytoskeletal ProteinsDystroglycansDystrophinExtracellular Matrix ProteinsGlycosylationHumansLeucineMembrane GlycoproteinsMiceMice, Mutant StrainsBGN protein, humanBgn protein, mouseBiglycanChondroitin SulfatesCytoskeletal ProteinsDAG1 protein, humanDystroglycansDystrophinExtracellular Matrix ProteinsLeucineMembrane GlycoproteinsProteoglycans

Identifiers

PMID10684260
PMCPMC2169361
OpenAlexW2160038542

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.