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Blood, Vol. 95 No. 7 (April 1), 2000:
pp. 2420-2425
Lysophosphatidic acid opens a Ca++ channel in human
erythrocytes
Lu Yang,
Dina A. Andrews, and
Philip S. Low
From the Departments of Chemistry and Veterinary Pathobiology,
Purdue University, West Lafayette, IN.
Lysophosphatidic acid (LPA) is a lipid-derived second messenger that
mobilizes many cells of the circulatory and vascular systems to assist
in thrombus development and wound healing. LPA, however, has not been
tested on human erythrocytes, largely because erythrocytes are
considered to be both biologically inert and inactive in intercellular
communication. To test this presumption, we have examined the impact of
LPA on signaling reactions within the human red blood cell (RBC). Using
both 45Ca++ and a
Ca++-sensitive fluorescent probe (Fluo-3), we
demonstrated that LPA, but not phosphatidic acid or the closely related
sphingosine-1-phosphate, stimulates the influx of micromolar
quantities of extracellular Ca++ into fresh RBCs. This
Ca++ influx was shown to be channel mediated rather
than leak promoted because the influx was observed at LPA
concentrations too low to perturb membrane integrity, it was inhibited
by P-type but not L-type Ca++ channel blockers, it was
inhibited by broad-specificity protein kinase inhibitors, and it was
not induced by inactive analogues of LPA. Further characterization
reveals that only approximately 25% of the RBCs participate in
LPA-induced Ca++ entry and that within this active
population, Ca++ gating occurs in an all-or-nothing
manner. Because the stimulation of Ca++ uptake occurs
at LPA concentrations (1-5 µmol/L) known to occur near a
developing thrombus and because the internalized Ca++
can potentially promote prothrombic properties in the stimulated RBCs,
we conclude that RBCs are not insensitive to signals released from
other cells.
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