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J Biol Chem, Vol. 273, Issue 16, 9857-9863, April 17, 1998
From the Department of Physiology, Boston University School of
Medicine, Boston, Massachusetts 02118
ERcalcistorin/protein-disulfide isomerase
(ECaSt/PDI), a high capacity low affinity
Ca2+-binding protein in the endoplasmic reticulum of
sea urchin eggs (Lebeche, D., and Kaminer, B. (1992) Biochem.
J. 287, 741-747), shares 55% sequence identity with mammalian
PDI and has PDI activity (Lucero, H., Lebeche, D., and Kaminer, B. (1994) J. Biol. Chem. 269, 23112-23119). We report on
ECaSt/PDI functioning as a Ca2+ storage protein in the
endoplasmic reticulum (ER) of a living cell and compare it with
calsequestrin and calreticulin, high capacity low affinity
Ca2+-binding proteins in the sarcoplasmic reticulum and ER,
respectively. Stably transfected Chinese hamster ovary cell clones
expressed these proteins, which were localized in the ER of the cell.
Microsomes from cells expressing ECaSt/PDI, calreticulin, and
calsequestrin accumulated 17.2 ± 0.27, 20.0 ± 0.82, and
38.0 ± 0.28 nmol of Ca2+/mg of protein, respectively;
control microsomes accumulated from 2.6 ± 0.17 to 2.9 ± 0.14 nmol of Ca2+/mg of protein. The initial rate of
Ca2+ uptake was similar in microsomes from transfected and
control cells. Microsomes containing an ECaSt/PDI mutant in which 45% of the acidic residue pairs in the C terminus were truncated had a
reduced Ca2+ storage capacity. This supports our previous
hypothesis that the degree of low affinity Ca2+ binding is
dependent on the number of pairs of carboxyl groups in the molecule.
The maximal Ca2+ accumulation by microsomes containing the
expressed ECaSt/PDI, C-terminally truncated ECaSt/PDI, calreticulin, or
calsequestrin correlates approximately with the Ca2+
binding capacity of the respective proteins.
ERcalcistorin/Protein-disulfide Isomerase Acts as a Calcium
Storage Protein in the Endoplasmic Reticulum of a Living Cell
COMPARISON WITH CALRETICULIN AND CALSEQUESTRIN
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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