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PMN binding to P-selectin is inhibited by sulfatide
G Todderud1, J Alford, K A Millsap
1Bristol-Myers Squibb Pharmaceutical Research Institute, Buffalo, NY 14213.
Journal of Leukocyte Biology
|July 1, 1992
Summary
P-selectin mediates leukocyte adhesion by binding to specific ligands. This study shows sulfatide inhibits P-selectin binding to polymorphonuclear leukocytes (PMNs), revealing its role in cell adhesion.
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- P-selectin is an endothelial adhesion protein crucial for leukocyte trafficking.
- Leukocyte adhesion involves interactions between cell surface proteins and their ligands.
Purpose of the Study:
- To characterize the binding interaction between P-selectin and polymorphonuclear leukocytes (PMNs).
- To investigate the role of sulfatide as a ligand in P-selectin-mediated PMN adhesion.
Main Methods:
- Utilized a soluble chimeric P-selectin-Fc fusion protein (receptor globulin, Rg) in an in vitro binding assay.
- Assessed binding saturation, concentration dependence, specificity, and cation dependence.
- Investigated the effect of sulfatide on P-selectin-PMN binding.
Main Results:
- PMN binding to immobilized Rg was saturable, concentration-dependent, and specific.
- Binding required divalent cations.
- PMNs expressed ligands for P-selectin and E-selectin, but not L-selectin.
- Sulfatide inhibited P-selectin-PMN binding in a dose-dependent manner.
Conclusions:
- Sulfatide acts as a functional ligand for P-selectin binding to PMNs.
- This interaction is important for understanding leukocyte adhesion mechanisms.