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J. Biol. Chem., Vol. 267, Issue 4, 2318-2324, Feb, 1992
N Demaurex, DP Lew and KH Krause
The filling state of intracellular Ca2+ stores has been proposed to
regulate Ca2+ influx across the plasma membrane in a variety of tissues. To
test this hypothesis, we have used three structurally unrelated inhibitors
of the Ca(2+)-ATPase of intracellular Ca2+ stores and investigated their
effect on Ca2+ homeostasis in HL-60 cells. Without increasing cellular
inositol (1,4,5)trisphosphate levels, all three inhibitors (cyclopiazonic
acid, thapsigargin, and 2,5-Di-tert- butylhydroquinone) released Ca2+ from
intracellular stores, resulting in total depletion of agonist-sensitive
Ca2+ stores. The Ca2+ release was relatively slow with a lag time of 5 s
and a time to peak of 60 s. After a lag time of approximately 15 s, all
three Ca(2+)-ATPase inhibitors activated a pathway for divalent cation
influx across the plasma membrane. At a given concentration of an
inhibitor, the plasma membrane permeability for divalent cations closely
correlated with the extent of depletion of Ca2+ stores. The influx pathway
activated by Ca(2+)-ATPase inhibitors conducted Ca2+, Mn2+, Co2+, Zn2+, and
Ba2+ and was blocked, at similar concentrations, by La3+, Ni2+, Cd2+, as
well as by the imidazole derivate SK&F 96365. The divalent cation
influx in response to the chemotactic peptide fMLP had the same
characteristics, suggesting a common pathway for Ca2+ entry. Our results
support the idea that the filling state of intracellular Ca2+ stores
regulates Ca2+ influx in HL-60 cells.
Cyclopiazonic acid depletes intracellular Ca2+ stores and activates an influx pathway for divalent cations in HL-60 cells
Infectious Diseases Division, University Hospital, Geneva, Switzerland.
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