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J. Biol. Chem., Vol. 276, Issue 19, 15945-15952, May 11, 2001
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From the Laboratory of Signal Transduction, NIEHS, National
Institutes of Health, Research Triangle Park, North Carolina 27709 and
the § Department of Molecular Genetics, Institute for Liver
Research, Kansai Medical University, Moriguchi 570-8506, Japan
We investigated the putative roles of
phospholipase C, polyphosphoinositides, and inositol
1,4,5-trisphosphate (IP3) in capacitative calcium
entry and calcium release-activated calcium current
(Icrac) in lacrimal acinar cells, rat
basophilic leukemia cells, and DT40 B-lymphocytes. Inhibition of
phospholipase C with U73122 blocked calcium entry and
Icrac activation whether in response to a
phospholipase C-coupled agonist or to calcium store depletion with
thapsigargin. Run-down of cellular polyphosphoinositides by
concentrations of wortmannin that block phosphatidylinositol 4-kinase
completely blocked calcium entry and Icrac. The
membrane-permeant IP3 receptor inhibitor,
2-aminoethoxydiphenyl borane, blocked both capacitative calcium
entry and Icrac. However, it is likely that
2-aminoethoxydiphenyl borane does not inhibit through an action on the
IP3 receptor because the drug was equally effective in
wild-type DT40 B-cells and in DT40 B-cells whose genes for all three
IP3 receptors had been disrupted. Intracellular application
of another potent IP3 receptor antagonist, heparin, failed
to inhibit activation of Icrac. Finally, the
inhibition of Icrac activation by U73122 or
wortmannin was not reversed or prevented by direct intracellular application of IP3. These findings indicate a requirement
for phospholipase C and for polyphosphoinositides for activation of capacitative calcium entry. However, the results call into question the
previously suggested roles of IP3 and IP3
receptor in this mechanism, at least in these particular cell types.
Role of the Phospholipase C-Inositol 1,4,5-Trisphosphate Pathway
in Calcium Release-activated Calcium Current and Capacitative
Calcium Entry*
,
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Eli Lilly and Company, Ltd., Lilly Research
Centre, Erl Wood Manor, Sunninghill Road, Windlesham, Surrey GU20 6PH,
United Kingdom.
¶
To whom correspondence should be addressed. E-mail:
putney@niehs.nih.gov; Fax: 919-541-7879.
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