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Related Experiment Video

Updated: Jun 12, 2026

Visualization and Quantification of TGFβ/BMP/SMAD Signaling under Different Fluid Shear Stress Conditions using Proximity-Ligation-Assay
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Agrin binds BMP2, BMP4 and TGFbeta1.

László Bányai1, Peter Sonderegger, László Patthy

  • 1Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary.

Plos One
|May 28, 2010
PubMed
Summary

Agrin

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Agrin's C-terminal fragment clusters acetylcholine receptors.
  • Functions of other agrin isoforms and the N-terminal region remain largely unknown.
  • Agrin's N-terminus contains follistatin-like domains, suggesting potential interactions with TGF-beta family members.

Purpose of the Study:

  • To investigate the interaction between the N-terminal part of rat agrin (Agrin-Nterm) and TGF-beta family members.
  • To elucidate the functional consequences of these interactions.

Main Methods:

  • Surface Plasmon Resonance (SPR) spectroscopy to quantify binding affinity.
  • Reporter assays to assess functional activity modulation.

Main Results:

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Last Updated: Jun 12, 2026

Visualization and Quantification of TGFβ/BMP/SMAD Signaling under Different Fluid Shear Stress Conditions using Proximity-Ligation-Assay
11:38

Visualization and Quantification of TGFβ/BMP/SMAD Signaling under Different Fluid Shear Stress Conditions using Proximity-Ligation-Assay

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Published on: July 21, 2021

  • Agrin-Nterm binds BMP2, BMP4, and TGF-beta1 with high affinity (K(D) in the 10(-8) M–10(-7) M range).
  • Agrin-Nterm inhibits BMP2 and BMP4 activity.
  • Agrin-Nterm slightly enhances TGF-beta1 activity.

Conclusions:

  • Agrin interacts with TGF-beta family members, impacting synaptogenesis.
  • Agrin may act as a reservoir for growth factors and modulate their activity.
  • The growth factor binding function of agrin appears evolutionarily older than its role in acetylcholine receptor clustering.