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J Biol Chem, Vol. 275, Issue 6, 3963-3969, February 11, 2000
From the The recently cloned epithelial
Ca2+ channel (ECaC) constitutes the Ca2+
influx pathway in 1,25-dihydroxyvitamin D3-responsive
epithelia. We have combined patch-clamp analysis and fura-2
fluorescence microscopy to functionally characterize ECaC
heterologously expressed in HEK293 cells. The intracellular
Ca2+ concentration in ECaC-expressing cells was closely
correlated with the applied electrochemical Ca2+ gradient,
demonstrating the distinctive Ca2+ permeability and
constitutive activation of ECaC. Cells dialyzed with 10 mM
1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid displayed large inward currents through ECaC in response to
voltage ramps. The corresponding current-voltage relationship showed
pronounced inward rectification. Currents evoked by voltage steps to
potentials below
Permeation and Gating Properties of the Novel Epithelial
Ca2+ Channel*
,,,
, and Department of Physiology, Campus
Gasthuisberg, Katholieke Universiteit Leuven,
Leuven B-3000, Belgium and the Departments of § Cell
Physiology and ¶ Biochemistry, Institute of Cellular Signalling,
University of Nijmegen, Nijmegen 6500 HB, The Netherlands
40 mV partially inactivated with a biexponential
time course. This inactivation was less pronounced if Ba2+
or Sr2+ replaced Ca2+ and was absent in
Ca2+-free solutions. ECaC showed an anomalous mole fraction
behavior. The permeability ratio
PCa:PNa calculated from
the reversal potential at 30 mM
[Ca2+]o was larger than 100. The divalent cation
selectivity profile is Ca2+ > Mn2+ > Ba2+ ~ Sr2+. Repetitive stimulation of
ECaC-expressing cells induced a decay of the current response, which
was greatly reduced if Ca2+ was replaced by
Ba2+ and was virtually abolished if
[Ca2+]o was lowered to 1 nM. In
conclusion, ECaC is a Ca2+ selective channel, exhibiting
Ca2+-dependent autoregulatory mechanisms,
including fast inactivation and slow down-regulation.
*
This work was supported by Federal Belgian State Grant IUAP
Nr.3P4/23; Flemish Government Grants Levenslijn 7.0021.98, FWO G.0118.00, GOA-7/1999, and FWO G.0136.00; European Commission Grant
BMH4-CT96-0602; and Dutch Organization of Scientific Research NWO-ALW
Grant 805-09.042.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Laboratorium voor
Fysiologie, Campus Gasthuisberg, KU Leuven, Herestraat 49,
B-3000 Leuven, Belgium. Tel.: 0032-16-34-5726; Fax: 0032-16-34-5991; E-mail: bernd.nilius@med.kuleuven.ac.be.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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B. Nilius, R. Vennekens, J. Prenen, J. G. J. Hoenderop, G. Droogmans, and R. J. M. Bindels The Single Pore Residue Asp542 Determines Ca2+ Permeation and Mg2+ Block of the Epithelial Ca2+ Channel J. Biol. Chem., January 5, 2001; 276(2): 1020 - 1025. [Abstract] [Full Text] [PDF]
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U. Wissenbach, B. A. Niemeyer, T. Fixemer, A. Schneidewind, C. Trost, A. Cavalie, K. Reus, E. Meese, H. Bonkhoff, and V. Flockerzi Expression of CaT-like, a Novel Calcium-selective Channel, Correlates with the Malignancy of Prostate Cancer J. Biol. Chem., May 25, 2001; 276(22): 19461 - 19468. [Abstract] [Full Text] [PDF]
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