Evidence map›Paper›PMID 20843788›Full record

ArticleThe Journal of biological chemistry2010

Activin A binds to perlecan through its pro-region that has heparin/heparan sulfate binding activity.

Shaoliang Li, Chisei Shimono, Naoko Norioka, Itsuko Nakano, Tetsuo Okubo, Yoshiko Yagi, Maria Hayashi, Yuya Sato, Hitomi Fujisaki, Shunji Hattori and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

34 citing papers in PubMed, 64 citations in OpenAlex.

  1. Yet another twist to the regulation of the TGF-β family ligands.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Matrix metalloproteinase-9 deficiency confers resilience in fibrodysplasia ossificans progressiva in a man and mice.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2024
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  18. The Corneal Basement Membranes and Stromal Fibrosis.Investigative ophthalmology & visual science · 2018
    Review
  19. Review
  20. Structural Biology and Evolution of the TGF-β Family.Cold Spring Harbor perspectives in biology · 2016
    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

13 authors at 4 institutions in 1 country.

Shaoliang LiLaboratory of Extracellular Matrix Biochemistry, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Chisei Shimono
Naoko Norioka
Itsuko Nakano
Tetsuo Okubo
Yoshiko Yagi
Maria Hayashi
Yuya Sato
Hitomi Fujisaki
Shunji Hattori
Nobuo Sugiura
Koji Kimata
Kiyotoshi Sekiguchi
Osaka University · JPJapan Institute of Leather Research · JPAichi Medical University · JPInstitute for Molecular Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activin A, a member of the transforming growth factor-β family, plays important roles in hormonal homeostasis and embryogenesis. In this study, we produced recombinant human activin A and examined its abilities to bind to extracellular matrix proteins. Recombinant activin A expressed in 293-F cells was purified as complexes of mature dimeric activin A with its pro-region. Among a panel of extracellular matrix proteins tested, recombinant activin A bound to perlecan and agrin, but not to laminins, nidogens, collagens I and IV, fibronectin, and nephronectin. The binding of recombinant activin A to perlecan was inhibited by heparin and high concentrations of NaCl and abolished by heparitinase treatment of perlecan, suggesting that activin A binds to the heparan sulfate chains of perlecan. In support of this possibility, recombinant activin A was capable of directly binding to heparin and heparan sulfate chains. Site-directed mutagenesis of recombinant activin A revealed that clusters of basic amino acid residues, Lys(259)-Lys(263) and Lys(270)-Lys(272), in the pro-region were required for binding to perlecan. Interestingly, deletion of the peptide segment Lys(259)-Gly(277) containing both basic amino acid clusters from the pro-region did not impair the activity of activin A to stimulate Smad-dependent gene expressions, although it completely ablated the perlecan-binding activity. The binding of activin A to basement membrane heparan sulfate proteoglycans through the basic residues in the pro-region was further confirmed by in situ activin A overlay assays using frozen tissue sections. Taken together, the present results indicate that activin A binds to heparan sulfate proteoglycans through its pro-region and thereby regulates its localization within tissues.

Indexed as

ActivinsAmino Acid SequenceAnimalsBlotting, WesternEmbryo, MammalianExtracellular Matrix ProteinsHeparan SulfateHeparan Sulfate ProteoglycansHeparinHumansImmunoenzyme TechniquesLamininLuciferasesMembrane GlycoproteinsMiceMolecular Sequence Dataactivin AActivinsExtracellular Matrix ProteinsHeparan SulfateHeparan Sulfate ProteoglycansHeparinLamininLuciferasesMembrane GlycoproteinsnephronectinnidogenperlecanRecombinant Proteins

Identifiers

PMID20843788
PMCPMC2978593
OpenAlexW2014449218

What OpenQuestion holds

Textmetadata
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.