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Structural insight into CD93 recognition by IGFBP7.

Yueming Xu1, Yi Sun2, Yuwen Zhu2

  • 1Shanghai Frontiers Science Center of Genome Editing and Cell Therapy, Shanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai 200241, China.

Structure (London, England : 1993)
|January 13, 2024
PubMed
Summary
This summary is machine-generated.

The CD93/IGFBP7 axis is crucial for endothelial cell (EC) angiogenesis. Blocking this interaction may improve cancer therapies by modulating the tumor microenvironment.

Keywords:
CD93EC angiogenesisIGFBP7crystal structuretumor therapy

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Cancer Research

Background:

  • The CD93/IGFBP7 axis in endothelial cells (EC) regulates angiogenesis and migration.
  • Upregulation of these proteins contributes to abnormal tumor vasculature.
  • Targeting this axis offers potential therapeutic strategies.

Purpose of the Study:

  • To elucidate the interaction between CD93 and IGFBP7.
  • To determine the structural basis of the CD93-IGFBP7 complex.
  • To assess the physiological relevance of this interaction in EC angiogenesis and tumor models.

Main Methods:

  • Partial structural determination of the human CD93-IGFBP7 complex.
  • Mutagenesis studies to confirm interaction specificity.
  • In vitro cellular assays and in vivo mouse tumor studies.

Main Results:

  • A partial structure of the CD93-IGFBP7 complex (CD93 EGF1 and IGFBP7 IB domains) was determined.
  • Mutagenesis confirmed specific interactions between these domains.
  • The CD93-IGFBP7 interaction was shown to be physiologically relevant in EC angiogenesis within tumor models.
  • Analysis of CD93 architecture provided insights into its cell surface presentation and ligand binding capabilities.

Conclusions:

  • The CD93-IGFBP7 interaction is a key mediator of EC angiogenesis.
  • Understanding this interaction provides a basis for developing targeted therapies against tumor angiogenesis.
  • Further structural insights into CD93 aid in understanding its role as a signaling platform.