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Lectin and epidermal growth factor domains of P-selectin at physiologic
density are the recognition unit for leukocyte binding
RM Gibson, GS Kansas, TF Tedder, B Furie and BC Furie
Center for Hemostasis and Thrombosis, New England Medical Center, Boston,
MA 02111.
P-selectin is an integral membrane glycoprotein on stimulated platelets and
endothelial cells that serves as a receptor for leukocytes. To estimate the
density of P-selectin in membranes necessary to support adhesion, we
incorporated purified P-selectin at varying concentrations into
phospholipid bilayers that encapsulated glass microspheres. Maximal binding
of these lipospheres to HL60 cells, a P-selectin ligand- expressing cell
line, was approached at a P-selectin density of about 100 molecules per
microns 2; half-maximal binding was observed at about 50 to 60 molecules
per microns 2. Compatible results were obtained with P-selectin expressed
on Chinese hamster ovary cells. The P-selectin density on stimulated
platelets was estimated to be 150 to 200 molecules/microns 2. To identify
the domains of P-selectin required for HL60 cell binding, chimeras of
P-selectin and L-selectin were stably expressed in Chinese hamster ovary
cells and clones that expressed the chimeras at the estimated physiologic
density were selected. Chimeras containing the P-selectin lectin and
epidermal growth factor (EGF) domains or the lectin, EGF, and short
consensus repeats bound HL60 cells equivalently, but a chimera containing
the P-selectin lectin domain alone bound HL60 cells much less well. These
results indicate that at a physiologically relevant P-selectin density on
membrane surfaces, the lectin, and EGF domains of P-selectin are together
required for optimal leukocyte binding.
Volume 85,
Issue 1,
pp. 151-158,
01/01/1995
Copyright © 1995 by The American Society of Hematology
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