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Higher-affinity oligosaccharide ligands for E-selectin

R M Nelson1, S Dolich, A Aruffo

  • 1Howard Hughes Medical Institute, University of California, San Diego, La Jolla 92093-0669.

The Journal of Clinical Investigation
|March 1, 1993
PubMed
Summary
This summary is machine-generated.

Synthetic oligosaccharides targeting selectin interactions were studied. Modified sialyl Lewis a (sLea) derivatives showed significantly enhanced binding inhibition for E-selectin, highlighting potential therapeutic strategies.

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Area of Science:

  • Carbohydrate chemistry
  • Immunology
  • Biochemistry

Background:

  • Selectins are cell adhesion molecules crucial for immune responses.
  • Sialyl Lewis x (sLex) and sialyl Lewis a (sLea) are key carbohydrate ligands for selectins.
  • Understanding selectin-ligand interactions is vital for developing anti-inflammatory therapies.

Purpose of the Study:

  • To synthesize and evaluate a series of oligosaccharides based on sLex and sLea.
  • To investigate their binding interactions with E-selectin and P-selectin.
  • To identify structural modifications that enhance inhibitory activity against selectin binding.

Main Methods:

  • Synthesis of various sLex and sLea oligosaccharide analogs.
  • Binding assays using E-selectin-immunoglobulin (E-selectin-Ig) and P-selectin-Ig fusion proteins.
  • Competitive inhibition studies to determine IC50 values.
  • Evaluation of Ca(2+)-dependent binding.

Main Results:

  • E-selectin-Ig binding to sLex and sLea was Ca(2+)-dependent.
  • sLea was a more potent inhibitor than sLex.
  • Aglycone attachment and N-acetyl group modification (amino or azido) significantly increased inhibitory activity.
  • Amino-substituted sLea was the most potent inhibitor (IC50 = 21 microM).
  • P-selectin-Ig binding inhibition was modest and showed less variation among analogs.

Conclusions:

  • Structural modifications of sLex and sLea, particularly amino substitution, can dramatically enhance their inhibitory potency against E-selectin.
  • These findings provide a basis for designing novel selectin inhibitors for therapeutic applications.
  • IC50 values from competitive binding assays correlate with blocking of leukocyte adhesion.