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J. Biol. Chem., Vol. 266, Issue 21, 13503-13506, Jul, 1991
Y Sagara and G Inesi
ATP-dependent calcium uptake by isolated sarcoplasmic reticulum vesicles is
inhibited by concentrations of free thapsigargin as low as 10(-10) M. This
effect is due to primary inhibition of the Ca(2+)- dependent ATPase which
is coupled to active transport. When binding of calcium to the activating
sites of the enzyme is measured under equilibrium conditions in the absence
of ATP, addition of thapsigargin produces strong inhibition. On the other
hand, if [tau-32P]ATP is added to ATPase preincubated with Ca2+ under
favorable conditions, significant levels of 32P-phosphorylated intermediate
are still formed transiently, even in the presence of thapsigargin. The
phosphoenzyme, however, decays rapidly as the calcium-enzyme complex is
destabilized as a consequence of ATP utilization, and formation of the
thapsigargin- enzyme complex is favored. Formation of the
thapsigargin-enzyme complex is also favored by Ca2+ chelation with EGTA,
with consequent inhibition of the enzyme reactivity to Pi (i.e. reverse of
the ATPase hydrolytic reaction). Neither the Ca(2+)- and ATP-induced Ca2+
release from junctional sarcoplasmic reticulum nor the Ca(2+)- and
calmodulin- dependent ATPase of plasma membranes (erythrocyte ghosts) were
found to be altered by thapsigargin at such low concentrations.
Inhibition of the sarcoplasmic reticulum Ca2+ transport ATPase by thapsigargin at subnanomolar concentrations
Department of Biological Chemistry, University of Maryland School of Medicine, Baltimore 21201.
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