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Papers In Press, published online ahead of print May 6, 2002
J. Biol. Chem, 10.1074/jbc.C200215200
Submitted on April 5, 2002
Revised on April 19, 2002
Accepted on May 3, 2002
subunit can interact with and modulate the functional properties of a calcium activated chloride channel CLCA1
Department of Physiology, University of Nevada, Reno, NV 89557
Corresponding Author: burt{at}physio.unr.edu
We have recently compared the biophysical and pharmacological properties of native Ca2+ -activated Cl- currents in murine portal vein with mCLCA1 channels cloned from murine portal vein myocytes (Britton, F. C., Ohya, S., Horowitz, B., and Greenwood, I. A. (2002) Journal of Physiology, 539, 107-117). These channels shared a similar relative permeability to various anions but the expressed channel current lacked the marked time-dependence of the native current. In addition, the expressed channel showed a lower Ca2+ sensitivity than the native channel. As non-pore forming regulatory b-subunits alter the kinetics and increase the Ca2+ sensitivity of Ca2+ -dependent K+ channels (BK channels) we investigated whether coexpression of b-subunits with CLCA1 would alter the kinetics / Ca2+ sensitivity of mCLCA1. Internal dialysis of HEK cells stably expressing CLCA1 with 500 nM Ca2+ evoked a significantly larger current when the b-subunit KCNMB1 was coexpressed. In a small number of co-transfected cells marked time dependence to the activation kinetics was observed. Interaction studies using the mammalian two-hybrid technique demonstrated a physical association between CLCA1 and KCNMB1 when coexpressed in HEK cells. These data suggest that activation of CLCA1 can be modified by accessory subunits.
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