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Blood, 1 November 2000, Vol. 96, No. 9, pp. 3070-3077
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Dimerization of P-selectin in platelets and endothelial
cells
Fern J. Barkalow,
Kurt L. Barkalow, and
Tanya N. Mayadas
From the Department of Pathology and the Department of
Medicine, Brigham and Women's Hospital and Harvard Medical School,
Boston, MA.
P-selectin is a leukocyte adhesion receptor stored in platelets and
endothelial cells and is translocated to the surface upon cell
activation. Purified P-selectin is oligomeric and has increased avidity
for its ligand relative to the monomeric form, but whether P-selectin
self-associates in the membrane of intact cells is not known. A
chemical cross-linking approach was used to show that P-selectin is
present as noncovalent dimers in resting platelets, human umbilical
vein endothelial cells, and heterologous RIN5F cells expressing
P-selectin. The results of 2-dimensional isoelectric focusing are
consistent in showing P-selectin dimers as homodimers, but they are
composed of a more basic subset of P-selectin than the monomers. This
suggests that the dimers are a biochemically distinct subset of
P-selectin. P-selectin dimers form in the endoplasmic reticulum and
Golgi compartments of human umbilical vein endothelial cells only after
synthesis of the mature P-selectin subunit, and are not preferentially
stored in Weibel-Palade bodies as compared with the monomeric form.
Platelet activation with thrombin receptor-activating peptide leads to
the presence of P-selectin monomers and homodimers on the cell surface
as well as P-selectin heterodimers, which are composed of P-selectin
and an unidentified protein of approximately 81 kd molecular weight. In
summary, these studies demonstrate that P-selectin is homodimeric in
situ and that platelet activation leads to the formation of an
additional activation-specific heterodimeric species. In addition, the
homodimer has unique biochemical characteristics compared with the
monomeric form, and dimerization occurs in the endoplasmic reticulum
and Golgi compartments of endothelial cells.
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