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Phenotype of a recombinant store-operated channel: highly selective permeation of Ca²⁺

Jan Warnat, Stephan Philipp, Stephanie Zimmer, Veit Flockerzi and Adolfo Cavalié

Genes related to trp (transient receptor potential) are proposed to encode store-operated channels. We examined the ionic permeation of recombinant channels formed by stable and transient expression of the TRP homologue bCCE1 in Chinese hamster ovary (CHO) cells (CHO(CCE1)) and rat basophilic leukaemia (RBL) cells, respectively.

Store-operated currents were activated in CHO(CCE1) cells by internal dialysis of IP₃ under strong buffering of intracellular Ca²⁺. The action of IP₃ was mimicked by thapsigargin but not by IP₄.

With extracellular Ca²⁺, Na⁺ and Mg²⁺, the store-operated currents of CHO(CCE1) rectified inwardly in the presence of internal Cs⁺. Outward currents were not detected below +80 mV. Identical currents were recorded with external Ba²⁺ and also with no external Na⁺ and Mg²⁺. In the absence of external Mg²⁺, the inward currents showed an anomalous mole fraction behaviour between Ca²⁺ and Na⁺. Half-maximal inhibition of Na⁺ currents was observed with ~100 nM and full block with 2-5 µM external Ca²⁺.

In the parental CHO(-) cells, IP₃ dialysis evoked inward currents that also displayed anomalous mole fraction behaviour between Ca²⁺ and Na⁺. However, half-maximal block of Na⁺ currents required 5 times higher Ca²⁺ concentrations in CHO(-) cells. Additionally, the density of Ca²⁺ and Na⁺ currents at -80 mV was 5 and 2 times larger in CHO(CCE1) cells, respectively.

In RBL cells, dialysis of IP₃ evoked store-operated currents that showed 1·4-fold larger densities at -80 mV in cells expressing bCCE1.

The enhanced density of store-operated currents in CHO(CCE1) cells and in bCCE1-transfected RBL cells probably reflects the phenotype of CCE1. These results suggest a highly selective permeation of Ca²⁺ through recombinant channels formed by CCE1 either alone or in combination with endogenous channel proteins.

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