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|Title:||Temperature dependence of human muscle ClC-1 chloride channel|
|Citation:||Journal of Physiology-London, 2001; 535(1):83-93|
|Publisher:||Blackwell Publishing Ltd|
|B. Bennetts, M. L. Roberts, A. H. Bretag and G. Y. Rychkov|
|Abstract:||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 mV 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.|
|Description:||The definitive version is available at www.blackwell-synergy.com|
|Appears in Collections:||Physiology publications|
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