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Vol. 9, Issue 6, 1513-1522, June 1998
Department of Biomedical Sciences, National Research Center for
Biomembranes, University of Padova, I-35121 Padova, Italy
Calreticulin (CRT) is a high-capacity, low-affinity
Ca2+-binding protein located in the lumen of the
endoplasmic reticulum (ER) of all eukaryotic cells investigated so far.
Its high level of conservation among different species suggests that it
serves functions fundamental to cell survival. The role originally
proposed for CRT, i.e., the main Ca2+ buffer of the ER, has
been obscured or even casted by its implication in processes as diverse
as gene expression, protein folding, and cell adhesion. In this work we
seek the role of CRT in Ca2+ storing and signaling by
evaluating its effects on the kinetics and amplitude of the
store-operated Ca2+ current
(ICRAC). We show that, in the rat basophilic
leukemia cell line RBL-1, overexpression of CRT, but not of its mutant lacking the high-capacity Ca2+-binding domain, markedly
retards the ICRAC development, however, only
when store depletion is slower than the rate of current activation. On
the contrary, when store depletion is rapid and complete,
overexpression of CRT has no effect. The present results are compatible
with a major Ca2+-buffering role of CRT within the ER but
exclude a direct, or indirect, role of this protein on the mechanism of
ICRAC activation.
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