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- W2084967013 abstract "We describe ATP-dependent inhibition of the 75–105-pS (in 250 mM Cl−) anion channel (SCl) from the sarcoplasmic reticulum (SR) of rabbit skeletal muscle. In addition to activation by Ca2+ and voltage, inhibition by ATP provides a further mechanism for regulating SCl channel activity in vivo. Inhibition by the nonhydrolyzable ATP analog 5′-adenylylimidodiphosphate (AMP-PNP) ruled out a phosphorylation mechanism. Cytoplasmic ATP (∼1 mM) inhibited only when Cl− flowed from cytoplasm to lumen, regardless of membrane voltage. Flux in the opposite direction was not inhibited by 9 mM ATP. Thus ATP causes true, current rectification in SCl channels. Inhibition by cytoplasmic ATP was also voltage dependent, having a KI of 0.4–1 mM at −40 mV (Hill coefficient ∼2), which increased at more negative potentials. Luminal ATP inhibited with a KI of ∼2 mM at +40 mV, and showed no block at negative voltages. Hidden Markov model analysis revealed that ATP inhibition 1) reduced mean open times without altering the maximum channel amplitude, 2) was mediated by a novel, single, voltage-independent closed state (∼1 ms), and 3) was much less potent on lower conductance substates than the higher conductance states. Therefore, the SCl channel is unlikely to pass Cl− from cytoplasm to SR lumen in vivo, and balance electrogenic Ca2+ uptake as previously suggested. Possible roles for the SCl channel in the transport of other anions are discussed." @default.
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- W2084967013 date "1998-05-01" @default.
- W2084967013 modified "2023-10-18" @default.
- W2084967013 title "ATP Inhibition and Rectification of a Ca2+-Activated Anion Channel in Sarcoplasmic Reticulum of Skeletal Muscle" @default.
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- W2084967013 doi "https://doi.org/10.1016/s0006-3495(98)77943-3" @default.
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