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Related Experiment Videos

Integrin-associated protein (CD47) and its ligands.

E J Brown1, W A Frazier

  • 1Program in Host-Pathogen Interactions, University of California San Francisco, San Francisco, CA 94143, USA.

Trends in Cell Biology
|April 18, 2001
PubMed
Summary

Integrin-associated protein (CD47) binds thrombospondin peptides, activating Gi protein signaling. This enhances integrin functions, modulating cell motility, adhesion, and phagocytosis.

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Area of Science:

  • Cell biology
  • Molecular signaling
  • Immunology

Background:

  • Integrin-associated protein (CD47) interacts with thrombospondin family members.
  • CD47 is a ligand for SIRP alpha and part of a complex with integrins, G proteins, and cholesterol.
  • Thrombospondin peptides with a VVM motif activate CD47.

Purpose of the Study:

  • To elucidate the signaling pathway initiated by thrombospondin-activated CD47.
  • To understand how CD47 signaling influences integrin function and cell activities.

Main Methods:

  • Investigated the interaction between CD47 and thrombospondin peptides.
  • Analyzed the downstream signaling events, including Gi protein activation.
  • Assessed the impact on integrin function and various cell activities.

Main Results:

  • Thrombospondin VVM motif peptides act as agonists for CD47.
  • CD47 activation initiates heterotrimeric Gi protein signaling.
  • This signaling pathway augments the functions of beta 1, beta 2, and beta 3 integrins.

Conclusions:

  • CD47 plays a crucial role in modulating cell functions through Gi protein signaling.
  • The findings reveal a mechanism by which CD47 influences integrin-mediated cellular processes.
  • This pathway impacts platelet activation, cell motility, adhesion, and leukocyte functions.

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