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J Biol Chem, Vol. 274, Issue 39, 27536-27544, September 24, 1999
From the Department of Biological Sciences, Stanford University,
Stanford, California 94305-5020
Gating of the cystic fibrosis
Cl
channel requires hydrolysis of ATP by its
nucleotide binding folds, but how this process controls the kinetics of
channel gating is poorly understood. In the present work we show that
the kinetics of channel gating and presumably the rate of ATP
hydrolysis depends on the species of divalent cation present and the
oxidation state of the protein. With Ca2+ as the dominant
divalent cation instead of Mg2+, the open burst duration of
the channel is increased approximately 20-fold, and this change is
reversible upon washout of Ca2+. In contrast, "soft"
divalent cations such as Cd2+ interact covalently with
cystic fibrosis transmembrane conductance regulator (CFTR). These
metals decrease both opening and closing rates of the channel, and the
effects are not reversed by washout. Oxidation of CFTR channels with a
variety of oxidants resulted in a similar slowing of channel gating. In
contrast, reducing agents had the opposite effect, increasing both
opening and closing rates of the channel. In cell-attached patches,
CFTR channels exhibit both oxidized and reduced types of gating,
raising the possibility that regulation of the redox state of the
channel may be a physiological mode of control of CFTR channel activity.
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