TY - JOUR
T1 - Temperature dependence of human muscle CIC-1 chloride channel
AU - Bennetts, B.
AU - Roberts, M. L.
AU - Bretag, A. H.
AU - Rychkov, G. Y.
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 2001/8/15
Y1 - 2001/8/15
N2 - 1. In the present work we investigated the dependence on temperature of the ionic conductance and gating of human muscle ClC-1 chloride channels, transiently expressed in human embryonic kidney (HEK 293) cells. 2. At normal pH, ClC-1 currents deactivated at negative potentials with a double-exponential time course. The time constants of the exponential components, corresponding to the relaxations of the fast and slow gates, were temperature dependent with Q10 values of ∼3 and ∼4, respectively. Current amplitude increased with increasing temperature with a Q10 of ∼1.6. 3. The voltage dependence of the two gating processes was shifted towards more positive potentials with increasing temperature. The half-saturation voltage (V1/2) of the steady-state open probability (Po) was shifted by ∼23 and ∼34 m V per 10°C increase in temperature, for the fast and slow gate, respectively. 4. At low pH, the voltage dependence of ClC-1 was reversed and currents were activated by hyperpolarisation with a single-exponential time course. This type of gating in ClC-1 resembled the slow gating of the Torpedo ClC-0 homologue, but differed with respect to its kinetics and temperature dependence, with a Q10 of gating relaxations at negative potentials of ∼5. The Arrhenius plot of ClC-1 conductance at low pH had a clear break point at ∼25°C, with higher Q10 values at lower temperatures. 5. The temperature sensitivity of relaxation and open probability of the slow gate, which in both ClC-0 and ClC-1 controls two pores simultaneously, implies that the slow gating of ClC-1 is mechanistically different from that of ClC-0.
AB - 1. In the present work we investigated the dependence on temperature of the ionic conductance and gating of human muscle ClC-1 chloride channels, transiently expressed in human embryonic kidney (HEK 293) cells. 2. At normal pH, ClC-1 currents deactivated at negative potentials with a double-exponential time course. The time constants of the exponential components, corresponding to the relaxations of the fast and slow gates, were temperature dependent with Q10 values of ∼3 and ∼4, respectively. Current amplitude increased with increasing temperature with a Q10 of ∼1.6. 3. The voltage dependence of the two gating processes was shifted towards more positive potentials with increasing temperature. The half-saturation voltage (V1/2) of the steady-state open probability (Po) was shifted by ∼23 and ∼34 m V per 10°C increase in temperature, for the fast and slow gate, respectively. 4. At low pH, the voltage dependence of ClC-1 was reversed and currents were activated by hyperpolarisation with a single-exponential time course. This type of gating in ClC-1 resembled the slow gating of the Torpedo ClC-0 homologue, but differed with respect to its kinetics and temperature dependence, with a Q10 of gating relaxations at negative potentials of ∼5. The Arrhenius plot of ClC-1 conductance at low pH had a clear break point at ∼25°C, with higher Q10 values at lower temperatures. 5. The temperature sensitivity of relaxation and open probability of the slow gate, which in both ClC-0 and ClC-1 controls two pores simultaneously, implies that the slow gating of ClC-1 is mechanistically different from that of ClC-0.
UR - http://www.scopus.com/inward/record.url?scp=0035880975&partnerID=8YFLogxK
U2 - 10.1111/j.1469-7793.2001.t01-1-00083.x
DO - 10.1111/j.1469-7793.2001.t01-1-00083.x
M3 - Article
C2 - 11507159
AN - SCOPUS:0035880975
SN - 0022-3751
VL - 535
SP - 83
EP - 93
JO - Journal of Physiology
JF - Journal of Physiology
IS - 1
ER -