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Related Experiment Videos

Sulfation is required for bone morphogenetic protein 2-dependent Id1 induction.

Nelson Osses1, Jaime Gutierrez, Teresa Lopez-Rovira

  • 1Unitat de Bioquímica, Departament de Ciències Fisiològiques II, Campus de Bellvitge, Universitat de Barcelona, L'Hospitalet de Llobregat, Barcelona, Spain.

Biochemical and Biophysical Research Communications
|May 2, 2006
PubMed
Summary

Sulfation is crucial for early bone morphogenetic protein-2 (BMP-2) signaling, specifically for the induction of Id1. This effect appears to be intracellular, as extracellular components do not rescue the inhibition.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Signaling

Background:

  • Bone morphogenetic protein (BMP) activity is reportedly linked to sulfated glycosaminoglycan (GAG) chains in proteoglycans.
  • The necessity of sulfated molecules in early BMP-2 signaling pathways remains unconfirmed.

Purpose of the Study:

  • To investigate the role of sulfation in early BMP-2 signaling responses.
  • To determine if sulfated molecules are required intracellularly for BMP-2-induced Id1 expression.

Main Methods:

  • Utilized C2C12 cells treated with sodium chlorate to inhibit sulfation.
  • Analyzed the induction of Id1 gene expression following BMP-2 stimulation.
  • Assessed the impact of extracellular GAGs, extracellular matrix (ECM), and GAG lyases on Id1 induction.

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Main Results:

  • Inhibition of sulfation significantly reduced the transcriptional induction of Id1 by BMP-2.
  • Adding extracellular GAGs or ECM did not restore Id1 induction.
  • Inhibition of GAG incorporation or removal of GAGs did not replicate the effect of sulfation inhibition.
  • Sulfation inhibition also repressed Id1 induction by an active BMP receptor, indicating an intracellular requirement.

Conclusions:

  • Sulfated molecules are essential for the early transcriptional induction of Id1 by BMP-2.
  • The requirement for sulfated molecules in BMP-2 signaling appears to be intracellular.
  • Extracellular modifications involving GAGs are not the primary mechanism mediating this sulfation-dependent effect.