Co-expression of mCysLT1 receptors and IK channels in Xenopus laevis oocytes elicits LTD4-stimulated IK current, independent of an increase in [Ca2+]i.

TY - JOUR

T1 - Co-expression of mCysLT1 receptors and IK channels in Xenopus laevis oocytes elicits LTD4-stimulated IK current, independent of an increase in [Ca2+]i.

AU - Wulff, Tune

AU - Hougaard, Charlotte

AU - Klaerke, Dan A

AU - Hoffmann, Else K

N1 - Keywords: Animals; Calcium; Cations, Divalent; Cell Line; Cytokines; Egtazic Acid; Humans; Hydrogen-Ion Concentration; Large-Conductance Calcium-Activated Potassium Channels; Leukotriene D4; Membrane Proteins; Oocytes; Potassium Channels; Potassium Channels, Calcium-Activated; Potassium Channels, Tandem Pore Domain; RNA, Complementary; Receptors, Leukotriene; Transfection; Xenopus laevis

PY - 2004

Y1 - 2004

N2 - Addition of LTD4 (10 nM) to Xenopus laevis oocytes expressing the mCysLT1 receptor together with hBK or hIK channels resulted in the activation of both channels secondary to an LTD4-induced increase in [Ca2+]i. In addition, the hIK channel is activated by low concentrations of LTD4 (<0.1 nM), which did not result in any increase in [Ca2+]i. Even though activation of hIK by low concentrations of LTD4 was independent of an increase in [Ca2+]i, a certain "permissive" level of [Ca2+]i was required for its activation, since buffering of intracellular Ca2+ by EGTA completely abolished the response to LTD4. Neither hTBAK1 nor hTASK2 was activated following stimulations with LTD4 (0.1 and 100 nM).

AB - Addition of LTD4 (10 nM) to Xenopus laevis oocytes expressing the mCysLT1 receptor together with hBK or hIK channels resulted in the activation of both channels secondary to an LTD4-induced increase in [Ca2+]i. In addition, the hIK channel is activated by low concentrations of LTD4 (<0.1 nM), which did not result in any increase in [Ca2+]i. Even though activation of hIK by low concentrations of LTD4 was independent of an increase in [Ca2+]i, a certain "permissive" level of [Ca2+]i was required for its activation, since buffering of intracellular Ca2+ by EGTA completely abolished the response to LTD4. Neither hTBAK1 nor hTASK2 was activated following stimulations with LTD4 (0.1 and 100 nM).

U2 - 10.1016/j.bbamem.2003.11.001

DO - 10.1016/j.bbamem.2003.11.001

M3 - Journal article

C2 - 14757222

SN - 0304-4165

VL - 1660

SP - 75

EP - 79

JO - B B A - General Subjects

JF - B B A - General Subjects

IS - 1-2

ER -