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J. Biol. Chem., Vol. 259, Issue 3, 1382-1385, Feb, 1984
V Prpic, KC Green, PF Blackmore and JH Exton
A rapid method for isolating highly purified rat liver plasma membrane
vesicles using isotonic medium and Percoll self-forming gradient
centrifugation is described. The vesicles were characterized by enzyme
markers and electron microscopy. The method also yielded a fraction rich in
nuclei. The vesicles transported Ca2+ in an ATP-dependent manner and this
was enhanced by oxalate. The Vmax for Ca2+ uptake was 0.65 +/- 0.08 nmol/mg
X min, which was approximately 18-fold higher than for other liver plasma
membrane preparations, and the Km for Ca2+ was 5.2 +/- 0.4 nM. Calcium
uptake was inhibited by 40-50% in vesicles isolated from rat livers
perfused for 3 min with 10(-7)M vasopressin. The half-maximally effective
concentration of vasopressin was 5 X 10(- 10)M which correlates with that
for raising cytosolic Ca2+ and phosphorylase a. Inhibition was not
significant in vesicles from livers perfused with vasopressin for only 1
min, indicating that inhibition of the Ca2+ pump may not be involved in the
rise in cytosolic Ca2+ observed at 1-2 s with this hormone. Epinephrine
(10(-5)M) and angiotensin II (10(-7)M) inhibited Ca2+ uptake by 31 +/- 10
and 26 +/- 5%, respectively, at 3 min. Glucagon (10(-7)M) had no effect. It
is proposed that the inhibitory action of the Ca2+-dependent hormones on
the plasma membrane Ca2+ pump plays an important role in the actions of
these hormones by prolonging the elevation in cytosolic Ca2+.
Vasopressin-, angiotensin II-, and alpha 1-adrenergic-induced inhibition of Ca2+ transport by rat liver plasma membrane vesicles
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