High impact information on Kcnh1

• Calcium inhibited r-eag channel activity with a mean IC50 of 67 nM [1].
• Activation of muscarinic receptors, generating calcium oscillations in the transfected cells, induced a synchronous inhibition of r-eag mediated outward currents [1].
• We have studied the properties of r-eag voltage-activated potassium channels in a stably transfected human embryonic kidney cell line [1].
• 2. It is shown that activation kinetics of IK(NI), like those of r-eag, depend on holding potential and on [Mg2+]o, and that IK(NI), like r-eag, is reversibly inhibited by a rise in [Ca2+]i. 3 [2].
• 1. Rat eag potassium channels (r-eag) were expressed in Xenopus oocytes [3].

Biological context of Kcnh1

• Eag2 expresses outward-rectifying, non-inactivating voltage-dependent K(+) currents resembling those of Eag1, including a strong dependence of activation kinetics on prepulse potential [4].
• Effect of matching for the endothelial antigen EAG-1 on kidney graft survival in the rat [5].

Anatomical context of Kcnh1

• Spontaneously shed outer membranes from a 24-h, 12-liter culture of an unencapsulated variant of strain Eag were combined with outer membranes released from the cells by Tris buffer and extracted with the nonionic detergent octylpolyoxyethylene [6].
• Eag mRNA was detected in the organ of Corti but mainly in the fibrocytes of the spiral ligament but not in spiral prominence or in stria vascularis [7].
• Immunogenicity of lymphoid cells and vascularized organs for the non-MHC antigen EAG-1 [8].

Associations of Kcnh1 with chemical compounds

• 5. Both the slowing of deactivation and the inactivation induced by the deletion delta 7-12 were compensated by a single histidine-to-arginine change in the S4 segment, while this mutation (H343R) only had minor effects on the gating kinetics of the full-length r-eag channel [3].

Regulatory relationships of Kcnh1

• However, Eag2 currents start activating at subthreshold potentials that are 40-50 mV more negative than those reported for Eag1 [4].

Other interactions of Kcnh1

• We report the identification of a new K(+) channel pore-forming subunit of the ether-à-go-go (Eag) family, named Eag2, that expresses voltage-gated K(+) channels that have significant activation at voltages around -100 mV [4].

References