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Related Experiment Videos

Extracellular RGD-binding proteins modulate cell adhesion.

A Ciarrocchi1, M S Rieber, M Rieber

  • 1I.V.I.C., Caracas, Venezuela.

Biochemical and Biophysical Research Communications
|March 16, 1992
PubMed
Summary
This summary is machine-generated.

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Extracellular RGD-binding proteins in blood prevent cell adhesion. Tumor development may cause partial degradation of these proteins, altering cell adhesive interactions.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Medicine

Background:

  • Cell adhesion to extracellular matrices, like fibronectin, is crucial and often mediated by integrin receptors recognizing RGD domains.
  • Soluble fibronectin is present in significant levels within the blood.

Purpose of the Study:

  • To investigate the presence and function of extracellular RGD-binding proteins in blood.
  • To explore their potential role in modulating blood-borne cell adhesive interactions.
  • To examine alterations in these proteins associated with tumor development.

Main Methods:

  • Attachment assays were used to assess cell adhesion.
  • Electrophoretic analysis was performed to characterize the RGD-binding proteins.
  • Plasma samples from tumor-bearing and normal mice were compared.

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Main Results:

  • Extracellular RGD-binding proteins were found to inhibit cell adhesion.
  • These proteins exhibit electrophoretic properties suggesting intrachain disulfide bonds, distinct from integrins.
  • Their electrophoretic profile is influenced by protease inhibitors.
  • Plasma from tumor-bearing mice showed increased fast-migrating RGD-binding species under reducing conditions.

Conclusions:

  • Extracellular RGD-binding proteins act as inhibitors of cell adhesion, representing potential modulators of blood-borne cell interactions.
  • Tumor development is associated with the partial degradation of these extracellular RGD-binding proteins.