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Vol. 273, Issue 1, 133-142, January 2, 1998
,
From the Ca2+ release from its internal
stores as a result of activation of phospholipase C is accompanied by
Ca2+ influx from the extracellular space. Ca2+
influx channels may be formed of proteins homologous to
Drosophila Trp. At least six non-allelic Trp
genes are present in the mouse genome. Full-length human, bovine,
mouse, and rat cDNAs for Trp1, 3, 4, 6 have been
cloned. Expression of these genes in various mammalian cells has
provided evidence that Trp proteins form plasma membrane
Ca2+-permeant channels that can be activated by an agonist
that activates phospholipase C, by inositol 1,4,5-trisphosphate, and/or
store depletion. We have stably expressed human Trp3 (hTrp3) in human embryonic kidney (HEK)293 cells. Measurement of intracellular Ca2+ concentrations in Fura2-loaded cells showed that cell
lines expressing hTrp3 have significantly higher basal and
agonist-stimulated influxes of Ca2+, Mn2+,
Ba2+, and Sr2+ than control cells. The increase
in Ca2+ entry attributable to the expression of hTrp3
obtained upon store depletion by thapsigargin was much lower than that
obtained by stimulation with agonists acting via a
Gq-coupled receptor. Addition of agonists to
thapsigargin-treated Trp3 cells resulted in a further increase in the
entry of divalent cations. The increased cation entry in Trp3 cells was
blocked by high concentrations of SKF 96365, verapamil,
La3+, Ni2+, and Gd3+. The
Trp3-mediated Ca2+ influx activated by agonists was
inhibited by a phospholipase C inhibitor, U73122. We propose that
expression of hTrp3 in these cells forms a non-selective cation channel
that opens after the activation of phospholipase C but not after store
depletion. In addition, a subpopulation of the expressed hTrp3 may form
heteromultimeric channels with endogenous proteins that are sensitive
to store depletion.
Department of Pharmacology and
Neurobiotechnology Center, Ohio State University, Columbus, Ohio
43210 and Departments of ¶ Anesthesiology and
Biological Chemistry, Molecular Biology and Brain Research Institutes, UCLA,
Los Angeles, California 90095
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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