Corpus ID: 38824239

Kv1.5-Kv beta interactions: molecular determinants and pharmacological consequences.

  title={Kv1.5-Kv beta interactions: molecular determinants and pharmacological consequences.},
  author={T. Gonzalez and M. David and Cristina Moreno and A. Macias and C. Valenzuela},
  journal={Mini reviews in medicinal chemistry},
  volume={10 7},
Kv1.5 channels are homotetramers of alpha-pore subunits mainly present in human atrium and pulmonary vasculature. Thus, Kv1.5 is a pharmacological target for cardiovascular diseases. Kv beta 1.3 assemblies with Kv alpha 1.5 and modifies its gating and pharmacology. A further knowledge of alpha-beta interactions and pharmacology will lead a better design of new drugs. 
PKC inhibition results in a Kv1.5 + Kvβ1.3 pharmacology closer to Kv1.5 channels
The aim of the present study was to investigate the effects of PKC inhibition on bupivacaine and quinidine block of Kv1.5 + Kvβ1.3 channels, resulting in the formation of a functional channelosome. Expand
Ultra-rapid delayed rectifier channels: molecular basis and therapeutic implications.
An overview of the properties of I(Kur) channels in expression systems and native cardiomyocytes is provided and their efficacy in treatment of atrial fibrillation (AF) is discussed. Expand
Regulation of Voltage-Gated K+ Channel Kv1.5 by the Janus Kinase JAK3
JAK3 contributes to the regulation of membrane Kv1.5 protein abundance and activity, an effect sensitive to ouabain and thus possibly involving Na+/K+ ATPase activity. Expand
SGK3 Sensitivity of Voltage Gated K+ Channel Kv1.5 (KCNA5)
SGK3 is a positive regulator of KCNA5, which is at least partially effective by abrogating the effect of Nedd4-2, and thus did not require Na+/K+ ATPase activity. Expand
Up-Regulation of Voltage Gated K+ Channels Kv1.3 and Kv1.5 by Protein Kinase PKB/Akt
PKB/Akt up-regulates both, Kv 1.3 and Kv1.5 K+ channels, and enhances the channel protein abundance in the cell membrane. Expand
SPAK and OSR1 Sensitivity of Voltage-Gated K+ Channel Kv1.5
Both, SPAK and OSR1 decrease cell membrane Kv1.5 protein abundance and activity and modify the expression and/or activity of the voltage-gated K+ channel, which participates in the regulation of diverse functions including atrial cardiac action potential and tumor cell proliferation. Expand