期刊
PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY
卷 468, 期 5, 页码 817-824出版社
SPRINGER HEIDELBERG
DOI: 10.1007/s00424-016-1794-9
关键词
DCPIB; PIP2; Kir channels; Patch clamp; Two-electrode voltage clamp
类别
资金
- National Institutes of Health [R01HL59949-18, R01HL090882-4]
- NIH [T32HL094290]
- NRSA fellowship from NHLBI [F30HL097582]
Inwardly rectifying K+ (Kir) channels are important contributors to the resting membrane potential and regulate cellular excitability. The activity of Kir channels depends critically on the phospholipid PIP2. Several modulators of the activity of Kir channels alter the apparent affinity of the channel to PIP2. Channels with high apparent affinity to PIP2 may not respond to a given modulator, but mutations that decrease such affinity can render the channel susceptible to modulation. Here, we identify a known inhibitor of the swelling-activated Cl- current, DCPIB, as an effective inhibitor of a number of Kir channels both in native cardiac cells and in heterologous expression systems. We show that the apparent affinity to PIP2 determines whether DCPIB will serve as an efficient blocker of Kir channels. These effects are consistent with a model in which DCPIB competes with PIP2 for a common binding site.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据