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Feedback regulation of Ca
Volume 270,
Number 24,
Issue of June 16, pp. 14445-14451, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
STORE-DEPENDENT AND -INDEPENDENT MECHANISMS
release-activated
Ca
(CRAC) channels was studied in Jurkat leukemic T
lymphocytes using whole cell recording and
[Ca
]
measurement
techniques. CRAC channels were activated by passively depleting
intracellular Ca
stores in the absence of
extracellular Ca
. Under conditions of moderate
intracellular Ca
buffering, elevating
[Ca
]
to 22 mM initiated an inward current through CRAC channels that declined
slowly with a half-time of
30 s. This slow inactivation was evoked
by a rise in [Ca
]
, as
it was effectively suppressed by an elevated level of EGTA in the
recording pipette that prevented increases in
[Ca
]
. Blockade of
Ca
uptake into stores by thapsigargin with or without
intracellular inositol 1,4,5-trisphosphate reduced the extent of slow
inactivation by
50%, indicating that store refilling normally
contributes significantly to this process. The store-independent
(thapsigargin-insensitive) portion of slow inactivation was largely
prevented by the protein phosphatase inhibitor, okadaic acid, and by a
structurally related compound, 1-norokadaone, but not by calyculin A
nor by cyclosporin A and FK506 at concentrations that fully inhibit
calcineurin (protein phosphatase 2B) in T cells. These results argue
against the involvement of protein phosphatases 1, 2A, 2B, or 3 in
store-independent inactivation. We conclude that calcium acts through
at least two slow negative feedback pathways to inhibit CRAC channels.
Slow feedback inhibition of CRAC current is likely to play important
roles in controlling the duration and dynamic behavior of
receptor-generated Ca
signals.
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