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Quantitation of Endothelial Cell Adhesiveness In Vitro
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Structure/function studies on vascular cell adhesion molecule-1

B Pepinsky1, C Hession, L L Chen

  • 1Biogen, Inc., Cambridge, Massachusetts 02142.

The Journal of Biological Chemistry
|September 5, 1992
PubMed

Insights

Vascular cell adhesion molecule-1 (VCAM1) interaction with very late antigen-4 (VLA4) is crucial for immune responses. Domains 1-3 of VCAM1 are sufficient for adhesion and T cell activation, despite proteolytic cleavage sites in domains 4 and 5.

Area of Science:

  • Immunology
  • Molecular Biology
  • Cellular Biology

Background:

  • Vascular cell adhesion molecule-1 (VCAM1), an Ig superfamily member, interacts with integrin VLA4.
  • This VCAM1/VLA4 interaction is vital for inflammatory and immune responses in vivo.
  • Human VCAM1 typically has seven extracellular Ig-like domains; domain 1 is N-terminal.

Purpose of the Study:

  • To investigate the structure-function relationship of human VCAM1.
  • To identify functional domains and antibody binding sites within VCAM1.

Main Methods:

  • Utilized domain truncation mutants of VCAM1.
  • Employed proteolytic fragmentation of recombinant soluble VCAM1.
  • Characterized antibody epitope mapping.

Main Results:

  • Identified two VCAM1 regions (domains 4 and 5) sensitive to proteolytic cleavage.
  • Localized the epitope for the blocking antibody 4B9 to domain 1.
  • Determined that VCAM1 domains 1-3 mediate adhesion and initiate T cell activation.

Conclusions:

  • VCAM1 domains 1-3 are critical for adhesive function and T cell activation.
  • Specific domains are involved in proteolytic susceptibility and antibody binding.
  • Understanding VCAM1 domain function aids in modulating immune responses.

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